The Enzyme Database

Displaying entries 101-150 of 577.

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EC 1.14.14.48     
Accepted name: jasmonoyl-L-amino acid 12-hydroxylase
Reaction: a jasmonoyl-L-amino acid + [reduced NADPH—hemoprotein reductase] + O2 = a 12-hydroxyjasmonoyl-L-amino acid + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: jasmonic acid = {(1R,2R)-3-oxo-2-[(2Z)pent-2-en-1-yl]cyclopentyl}acetic acid
(+)-7-epi-jasmonic acid = {(1R,2S)-3-oxo-2-[(2Z)pent-2-en-1-yl]cyclopentyl}acetic acid
Other name(s): CYP94B1 (gene name); CYP94B3 (gene name)
Systematic name: jasmonoyl-L-amino acid,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (12-hydroxylating)
Comments: A cytochrome P450 (heme thiolate) enzyme found in plants. The enzyme acts on jasmonoyl-L-amino acid conjugates, catalysing the hydroxylation of the C-12 position of jasmonic acid. While the best studied substrate is (+)-7-epi-jasmonoyl-L-isoleucine, the enzyme was shown to be active with jasmonoyl-L-valine and jasmonoyl-L-phenylalanine, and is likely to be active with other jasmonoyl-amino acid conjugates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Koo, A.J., Cooke, T.F. and Howe, G.A. Cytochrome P450 CYP94B3 mediates catabolism and inactivation of the plant hormone jasmonoyl-L-isoleucine. Proc. Natl. Acad. Sci. USA 108 (2011) 9298–9303. [DOI] [PMID: 21576464]
2.  Kitaoka, N., Matsubara, T., Sato, M., Takahashi, K., Wakuta, S., Kawaide, H., Matsui, H., Nabeta, K. and Matsuura, H. Arabidopsis CYP94B3 encodes jasmonyl-L-isoleucine 12-hydroxylase, a key enzyme in the oxidative catabolism of jasmonate. Plant Cell Physiol. 52 (2011) 1757–1765. [DOI] [PMID: 21849397]
3.  Heitz, T., Widemann, E., Lugan, R., Miesch, L., Ullmann, P., Desaubry, L., Holder, E., Grausem, B., Kandel, S., Miesch, M., Werck-Reichhart, D. and Pinot, F. Cytochromes P450 CYP94C1 and CYP94B3 catalyze two successive oxidation steps of plant hormone jasmonoyl-isoleucine for catabolic turnover. J. Biol. Chem. 287 (2012) 6296–6306. [DOI] [PMID: 22215670]
4.  Kitaoka, N., Kawaide, H., Amano, N., Matsubara, T., Nabeta, K., Takahashi, K. and Matsuura, H. CYP94B3 activity against jasmonic acid amino acid conjugates and the elucidation of 12-O-β-glucopyranosyl-jasmonoyl-L-isoleucine as an additional metabolite. Phytochemistry 99 (2014) 6–13. [DOI] [PMID: 24467969]
5.  Koo, A.J., Thireault, C., Zemelis, S., Poudel, A.N., Zhang, T., Kitaoka, N., Brandizzi, F., Matsuura, H. and Howe, G.A. Endoplasmic reticulum-associated inactivation of the hormone jasmonoyl-L-isoleucine by multiple members of the cytochrome P450 94 family in Arabidopsis. J. Biol. Chem. 289 (2014) 29728–29738. [DOI] [PMID: 25210037]
6.  Widemann, E., Grausem, B., Renault, H., Pineau, E., Heinrich, C., Lugan, R., Ullmann, P., Miesch, L., Aubert, Y., Miesch, M., Heitz, T. and Pinot, F. Sequential oxidation of jasmonoyl-phenylalanine and jasmonoyl-isoleucine by multiple cytochrome P450 of the CYP94 family through newly identified aldehyde intermediates. Phytochemistry 117 (2015) 388–399. [DOI] [PMID: 26164240]
[EC 1.14.14.48 created 2017]
 
 
EC 1.14.14.58     
Accepted name: trimethyltridecatetraene synthase
Reaction: (6E,10E)-geranyllinalool + [reduced NADPH—hemoprotein reductase] + O2 = (3E,7E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene + [oxidized NADPH—hemoprotein reductase] + but-3-en-2-one + 2 H2O
For diagram of acyclic diterpenoid biosynthesis, click here
Glossary: (6E,10E)-geranyllinalool = (6E,10E)-3,7,11,15-tetramethylhexadeca-1,6,10,14-tetraen-3-ol
Other name(s): CYP82G1; CYP92C5; CYP92C6; DMNT/TMTT homoterpene synthase
Systematic name: (6E,10E)-geranyllinalool,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plants Arabidopsis thaliana (thale cress) and Zea mays (maize). It forms this C16 homoterpene in response to herbivore attack. In vitro some variants of the enzyme also convert (3S,6E)-nerolidol to (3E)-4,8-dimethylnona-1,3,7-triene (see EC 1.14.14.59, dimethylnonatriene synthase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Lee, S., Badieyan, S., Bevan, D.R., Herde, M., Gatz, C. and Tholl, D. Herbivore-induced and floral homoterpene volatiles are biosynthesized by a single P450 enzyme (CYP82G1) in Arabidopsis. Proc. Natl. Acad. Sci. USA 107 (2010) 21205–21210. [DOI] [PMID: 21088219]
2.  Richter, A., Schaff, C., Zhang, Z., Lipka, A.E., Tian, F., Kollner, T.G., Schnee, C., Preiss, S., Irmisch, S., Jander, G., Boland, W., Gershenzon, J., Buckler, E.S. and Degenhardt, J. Characterization of biosynthetic pathways for the production of the volatile homoterpenes DMNT and TMTT in Zea mays. Plant Cell 28 (2016) 2651–2665. [DOI] [PMID: 27662898]
[EC 1.14.14.58 created 2018]
 
 
EC 1.14.14.59     
Accepted name: dimethylnonatriene synthase
Reaction: (3S,6E)-nerolidol + [reduced NADPH—hemoprotein reductase] + O2 = (3E)-4,8-dimethylnona-1,3,7-triene + [oxidized NADPH—hemoprotein reductase] + but-3-en-2-one + 2 H2O
For diagram of acyclic sesquiterpenoid biosynthesis, click here
Other name(s): CYP82G1; CYP92C5; DMNT/TMTT homoterpene synthase
Systematic name: (3S,6E)-nerolidol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plants Arabidopsis thaliana (thale cress) and Zea mays (maize). It forms this C11 homoterpene in response to herbivore attack. In vitro the enzyme also converts (6E,10E)-geranyllinalool to (3E,7E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene (see EC 1.14.14.58, trimethyltridecatetraene synthase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Lee, S., Badieyan, S., Bevan, D.R., Herde, M., Gatz, C. and Tholl, D. Herbivore-induced and floral homoterpene volatiles are biosynthesized by a single P450 enzyme (CYP82G1) in Arabidopsis. Proc. Natl. Acad. Sci. USA 107 (2010) 21205–21210. [DOI] [PMID: 21088219]
2.  Richter, A., Schaff, C., Zhang, Z., Lipka, A.E., Tian, F., Kollner, T.G., Schnee, C., Preiss, S., Irmisch, S., Jander, G., Boland, W., Gershenzon, J., Buckler, E.S. and Degenhardt, J. Characterization of biosynthetic pathways for the production of the volatile homoterpenes DMNT and TMTT in Zea mays. Plant Cell 28 (2016) 2651–2665. [DOI] [PMID: 27662898]
[EC 1.14.14.59 created 2018]
 
 
EC 1.14.14.80     
Accepted name: long-chain fatty acid ω-monooxygenase
Reaction: a long-chain fatty acid + [reduced NADPH—hemoprotein reductase] + O2 = an ω-hydroxy-long-chain fatty acid + [oxidized NADPH—hemoprotein reductase] + H2O
Other name(s): CYP704B1 (gene name); CYP52M1 (gene name); CYP4A (gene name); CYP86A (gene name)
Systematic name: long-chain fatty acid,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (ω-hydroxylating)
Comments: A cytochrome P-450 (heme thiolate) enzyme. The plant enzyme CYP704B1, which is involved in the synthesis of sporopollenin, a complex polymer found at the outer layer of spores and pollen, acts on palmitate (18:0), stearate (18:0) and oleate (18:1). The plant enzyme CYP86A1 also acts on laurate (12:0). The enzyme from the yeast Starmerella bombicola (CYP52M1) acts on C16 to C20 saturated and unsaturated fatty acids and can also hydroxylate the (ω-1) position. The mammalian enzyme CYP4A acts on laurate (12:0), myristate (14:0), palmitate (16:0), oleate (18:1), and arachidonate (20:4).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Benveniste, I., Tijet, N., Adas, F., Philipps, G., Salaun, J.P. and Durst, F. CYP86A1 from Arabidopsis thaliana encodes a cytochrome P450-dependent fatty acid ω-hydroxylase. Biochem. Biophys. Res. Commun. 243 (1998) 688–693. [DOI] [PMID: 9500987]
2.  Hoch, U., Zhang, Z., Kroetz, D.L. and Ortiz de Montellano, P.R. Structural determination of the substrate specificities and regioselectivities of the rat and human fatty acid ω-hydroxylases. Arch. Biochem. Biophys. 373 (2000) 63–71. [DOI] [PMID: 10620324]
3.  Dobritsa, A.A., Shrestha, J., Morant, M., Pinot, F., Matsuno, M., Swanson, R., Møller, B.L. and Preuss, D. CYP704B1 is a long-chain fatty acid ω-hydroxylase essential for sporopollenin synthesis in pollen of Arabidopsis. Plant Physiol. 151 (2009) 574–589. [DOI] [PMID: 19700560]
4.  Huang, F.C., Peter, A. and Schwab, W. Expression and characterization of CYP52 genes involved in the biosynthesis of sophorolipid and alkane metabolism from Starmerella bombicola. Appl. Environ. Microbiol. 80 (2014) 766–776. [DOI] [PMID: 24242247]
[EC 1.14.14.80 created 2015 as EC 1.14.13.205, transferred 2018 to EC 1.14.14.80]
 
 
EC 1.14.14.81     
Accepted name: flavanoid 3′,5′-hydroxylase
Reaction: a flavanone + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = a 3′,5′-dihydroxyflavanone + 2 [oxidized NADPH—hemoprotein reductase] + 2 H2O (overall reaction)
(1a) a flavanone + [reduced NADPH—hemoprotein reductase] + O2 = a 3′-hydroxyflavanone + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) a 3′-hydroxyflavanone + [reduced NADPH—hemoprotein reductase] + O2 = a 3′,5′-dihydroxyflavanone + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of myricetin biosynthesis, click here, for diagram of the biosynthesis of naringenin derivatives, click here and for diagram of flavonoid biosynthesis, click here
Other name(s): flavonoid 3′,5′-hydroxylase
Systematic name: flavanone,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3′,5′-dihydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein found in plants. The 3′,5′-dihydroxyflavanone is formed via the 3′-hydroxyflavanone. In Petunia hybrida the enzyme acts on naringenin, eriodictyol, dihydroquercetin (taxifolin) and dihydrokaempferol (aromadendrin). The enzyme catalyses the hydroxylation of 5,7,4′-trihydroxyflavanone (naringenin) at either the 3′ position to form eriodictyol or at both the 3′ and 5′ positions to form 5,7,3′,4′,5′-pentahydroxyflavanone (dihydrotricetin). The enzyme also catalyses the hydroxylation of 3,5,7,3′,4′-pentahydroxyflavanone (taxifolin) at the 5′ position, forming ampelopsin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 94047-23-1
References:
1.  Menting, J., Scopes, R.K. and Stevenson, T.W. Characterization of flavonoid 3′,5′-hydroxylase in microsomal membrane fraction of Petunia hybrida flowers. Plant Physiol. 106 (1994) 633–642. [PMID: 12232356]
2.  Shimada, Y., Nakano-Shimada, R., Ohbayashi, M., Okinaka, Y., Kiyokawa, S. and Kikuchi, Y. Expression of chimeric P450 genes encoding flavonoid-3′, 5′-hydroxylase in transgenic tobacco and petunia plants1. FEBS Lett. 461 (1999) 241–245. [DOI] [PMID: 10567704]
3.  de Vetten, N., ter Horst, J., van Schaik, H.P., de Boer, A., Mol, J. and Koes, R. A cytochrome b5 is required for full activity of flavonoid 3′, 5′-hydroxylase, a cytochrome P450 involved in the formation of blue flower colors. Proc. Natl. Acad. Sci. USA 96 (1999) 778–783. [DOI] [PMID: 9892710]
[EC 1.14.14.81 created 2004 as EC 1.14.13.88, transferred 2018 to EC 1.14.14.81]
 
 
EC 1.14.14.82     
Accepted name: flavonoid 3′-monooxygenase
Reaction: a flavonoid + [reduced NADPH—hemoprotein reductase] + O2 = a 3′-hydroxyflavonoid + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of flavonoid biosynthesis, click here and for diagram of the biosynthesis of naringenin derivatives, click here
Other name(s): CYP75B1 (gene name); flavonoid 3′-hydroxylase; flavonoid 3-hydroxylase (incorrect); NADPH:flavonoid-3′-hydroxylase (incorrect); flavonoid 3-monooxygenase (incorrect)
Systematic name: flavonoid,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3′-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein found in plants. Acts on a number of flavonoids, including the flavanone naringenin and the flavone apigenin. Does not act on 4-coumarate or 4-coumaroyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 75991-44-5
References:
1.  Forkmann, G., Heller, W. and Grisebach, H. Anthocyanin biosynthesis in flowers of Matthiola incana flavanone 3- and flavonoid 3′-hydroxylases. Z. Naturforsch. C: Biosci. 35 (1980) 691–695.
2.  Brugliera, F., Barri-Rewell, G., Holton, T.A. and Mason, J.G. Isolation and characterization of a flavonoid 3′-hydroxylase cDNA clone corresponding to the Ht1 locus of Petunia hybrida. Plant J. 19 (1999) 441–451. [PMID: 10504566]
3.  Schoenbohm, C., Martens, S., Eder, C., Forkmann, G. and Weisshaar, B. Identification of the Arabidopsis thaliana flavonoid 3′-hydroxylase gene and functional expression of the encoded P450 enzyme. Biol. Chem. 381 (2000) 749–753. [PMID: 11030432]
[EC 1.14.14.82 created 1983 as EC 1.14.13.21, transferred 2018 to EC 1.14.14.82]
 
 
EC 1.14.14.86     
Accepted name: ent-kaurene monooxygenase
Reaction: ent-kaur-16-ene + 3 [reduced NADPH—hemoprotein reductase] + 3 O2 = ent-kaur-16-en-19-oate + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction)
(1a) ent-kaur-16-ene + [reduced NADPH—hemoprotein reductase] + O2 = ent-kaur-16-en-19-ol + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) ent-kaur-16-en-19-ol + [reduced NADPH—hemoprotein reductase] + O2 = ent-kaur-16-en-19-al + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(1c) ent-kaur-16-en-19-al + [reduced NADPH—hemoprotein reductase] + O2 = ent-kaur-16-en-19-oate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of gibberellin A12 biosynthesis, click here
Other name(s): ent-kaurene oxidase (misleading)
Systematic name: ent-kaur-16-ene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (hydroxylating)
Comments: A cytochrome P-450 (heme thiolate) protein found in plants. Catalyses three successive oxidations of the 4-methyl group of ent-kaurene giving kaurenoic acid.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 149565-67-3
References:
1.  Ashman, P.J., Mackenzie, A. and Bramley, P.M. Characterization of ent-kaurene oxidase activity from Gibberella fujikuroi. Biochim. Biophys. Acta 1036 (1990) 151–157. [DOI] [PMID: 2223832]
2.  Archer, C., Ashman, P.J., Hedden, P., Bowyer, J.R. and Bramley, P.M. Purification of ent-kaurene oxidase from Gibberella fujikuroi and Cucurbita maxima. Biochem. Soc. Trans. 20 (1992) 218. [PMID: 1397591]
3.  Helliwell, C.A., Poole, A., Peacock, W.J. and Dennis, E.S. Arabidopsis ent-kaurene oxidase catalyzes three steps of gibberellin biosynthesis. Plant Physiol. 119 (1999) 507–510. [PMID: 9952446]
[EC 1.14.14.86 created 2002 as EC 1.14.13.78, transferred 2018 to EC 1.14.14.86]
 
 
EC 1.14.14.96     
Accepted name: 5-O-(4-coumaroyl)-D-quinate 3′-monooxygenase
Reaction: trans-5-O-(4-coumaroyl)-D-quinate + [reduced NADPH—hemoprotein reductase] + O2 = trans-5-O-caffeoyl-D-quinate + [oxidized NADPH—hemoprotein reductase] + H2O
Other name(s): 5-O-(4-coumaroyl)-D-quinate/shikimate 3′-hydroxylase; coumaroylquinate(coumaroylshikimate) 3′-monooxygenase; CYP98A3 (gene name)
Systematic name: trans-5-O-(4-coumaroyl)-D-quinate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3′-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein, found in plants. It also acts on trans-5-O-(4-coumaroyl)shikimate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 112131-08-5
References:
1.  Kühnl, T., Koch, U., Heller, W. and Wellman, E. Chlorogenic acid biosynthesis: characterization of a light-induced microsomal 5-O-(4-coumaroyl)-D-quinate/shikimate 3′-hydroxylase from carrot (Daucus carota L.) cell suspension cultures. Arch. Biochem. Biophys. 258 (1987) 226–232. [DOI] [PMID: 2821918]
2.  Schoch, G., Goepfert, S., Morant, M., Hehn, A., Meyer, D., Ullmann, P. and Werck-Reichhart, D. CYP98A3 from Arabidopsis thaliana is a 3′-hydroxylase of phenolic esters, a missing link in the phenylpropanoid pathway. J. Biol. Chem. 276 (2001) 36566–36574. [PMID: 11429408]
3.  Franke, R., Humphreys, J.M., Hemm, M.R., Denault, J.W., Ruegger, M.O., Cusumano, J.C. and Chapple, C. The Arabidopsis REF8 gene encodes the 3-hydroxylase of phenylpropanoid metabolism. Plant J. 30 (2002) 33–45. [PMID: 11967091]
4.  Matsuno, M., Compagnon, V., Schoch, G.A., Schmitt, M., Debayle, D., Bassard, J.E., Pollet, B., Hehn, A., Heintz, D., Ullmann, P., Lapierre, C., Bernier, F., Ehlting, J. and Werck-Reichhart, D. Evolution of a novel phenolic pathway for pollen development. Science 325 (2009) 1688–1692. [PMID: 19779199]
[EC 1.14.14.96 created 1990 as EC 1.14.13.36, transferred 2018 to EC 1.14.14.96]
 
 
EC 1.14.14.137     
Accepted name: (+)-abscisic acid 8′-hydroxylase
Reaction: (+)-abscisate + [reduced NADPH—hemoprotein reductase] + O2 = 8′-hydroxyabscisate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of abscisic-acid biosynthesis, click here
Other name(s): (+)-ABA 8′-hydroxylase; ABA 8′-hydroxylase; CYP707A1 (gene name)
Systematic name: abscisate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (8′-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein found in plants. Catalyses the first step in the oxidative degradation of abscisic acid and is considered to be the pivotal enzyme in controlling the rate of degradation of this plant hormone [1]. CO inhibits the reaction, but its effects can be reversed by the presence of blue light [1]. The 8′-hydroxyabscisate formed can be converted into (–)-phaseic acid, most probably spontaneously.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 153190-37-5
References:
1.  Cutler, A.J., Squires, T.M., Loewen, M.K. and Balsevich, J.J. Induction of (+)-abscisic acid 8′ hydroxylase by (+)-abscisic acid in cultured maize cells. J. Exp. Bot. 48 (1997) 1787–1795.
2.  Krochko, J.E., Abrams, G.D., Loewen, M.K., Abrams, S.R. and Cutler, A.J. (+)-Abscisic acid 8′-hydroxylase is a cytochrome P450 monooxygenase. Plant Physiol. 118 (1998) 849–860. [PMID: 9808729]
3.  Saito, S., Hirai, N., Matsumoto, C., Ohigashi, H., Ohta, D., Sakata, K. and Mizutani, M. Arabidopsis CYP707As encode (+)-abscisic acid 8′-hydroxylase, a key enzyme in the oxidative catabolism of abscisic acid. Plant Physiol. 134 (2004) 1439–1449. [PMID: 15064374]
[EC 1.14.14.137 created 2005 as EC 1.14.13.93, transferred 2018 EC 1.14.14.137]
 
 
EC 1.14.14.147     
Accepted name: 22α-hydroxysteroid 23-monooxygenase
Reaction: (1) 3-epi-6-deoxocathasterone + [reduced NADPH—hemoprotein reductase] + O2 = 6-deoxotyphasterol + [oxidized NADPH—hemoprotein reductase] + H2O
(2) (22S,24R)-22-hydroxy-5α-ergostan-3-one + [reduced NADPH—hemoprotein reductase] + O2 = 3-dehydro-6-deoxoteasterone + [oxidized NADPH—hemoprotein reductase] + H2O
Other name(s): cytochrome P450 90C1; CYP90D1; CYP90C1; 3-epi-6-deoxocathasterone,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (C-23-hydroxylating); 3-epi-6-deoxocathasterone 23-monooxygenase
Systematic name: 22α-hydroxysteroid,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (C-23-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein involved in brassinosteroid biosynthesis in plants. The enzyme has a relaxed substrate specificity, and C-23 hydroxylation can occur at different stages in the pathway. In Arabidopsis thaliana two isozymes, encoded by the CYP90C1 and CYP90D1 genes, have redundant activities.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kim, G.T., Fujioka, S., Kozuka, T., Tax, F.E., Takatsuto, S., Yoshida, S. and Tsukaya, H. CYP90C1 and CYP90D1 are involved in different steps in the brassinosteroid biosynthesis pathway in Arabidopsis thaliana. Plant J. 41 (2005) 710–721. [DOI] [PMID: 15703058]
2.  Ohnishi, T., Szatmari, A.M., Watanabe, B., Fujita, S., Bancos, S., Koncz, C., Lafos, M., Shibata, K., Yokota, T., Sakata, K., Szekeres, M. and Mizutani, M. C-23 hydroxylation by Arabidopsis CYP90C1 and CYP90D1 reveals a novel shortcut in brassinosteroid biosynthesis. Plant Cell 18 (2006) 3275–3288. [DOI] [PMID: 17138693]
[EC 1.14.14.147 created 2010 as EC 1.14.13.112, transferred 2018 to EC 1.14.14.147, modified 2022]
 
 
EC 1.14.14.149     
Accepted name: 5-epiaristolochene 1,3-dihydroxylase
Reaction: 5-epiaristolochene + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = capsidiol + 2 [oxidized NADPH—hemoprotein reductase] + 2 H2O
click here
Other name(s): 5-epi-aristolochene 1,3-dihydroxylase; EAH; CYP71D20
Systematic name: 5-epiaristolochene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (1- and 3-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. Kinetic studies suggest that 1β-hydroxyepiaristolochene is mainly formed first followed by hydroxylation at C-3. However the reverse order via 3α-hydroxyepiaristolochene does occur.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ralston, L., Kwon, S.T., Schoenbeck, M., Ralston, J., Schenk, D.J., Coates, R.M. and Chappell, J. Cloning, heterologous expression, and functional characterization of 5-epi-aristolochene-1,3-dihydroxylase from tobacco (Nicotiana tabacum). Arch. Biochem. Biophys. 393 (2001) 222–235. [DOI] [PMID: 11556809]
2.  Takahashi, S., Zhao, Y., O'Maille, P.E., Greenhagen, B.T., Noel, J.P., Coates, R.M. and Chappell, J. Kinetic and molecular analysis of 5-epiaristolochene 1,3-dihydroxylase, a cytochrome P450 enzyme catalyzing successive hydroxylations of sesquiterpenes. J. Biol. Chem. 280 (2005) 3686–3696. [DOI] [PMID: 15522862]
[EC 1.14.14.149 created 2011 as EC 1.14.13.119, transferred 2018 to EC 1.14.14.149]
 
 
EC 1.14.14.156     
Accepted name: tryptophan N-monooxygenase
Reaction: L-tryptophan + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = (E)-indol-3-ylacetaldoxime + 2 [oxidized NADPH—hemoprotein reductase] + CO2 + 3 H2O (overall reaction)
(1a) L-tryptophan + [reduced NADPH—hemoprotein reductase] + O2 = N-hydroxy-L-tryptophan + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) N-hydroxy-L-tryptophan + [reduced NADPH—hemoprotein reductase] + O2 = N,N-dihydroxy-L-tryptophan + [oxidized NADPH—hemoprotein reductase] + H2O
(1c) N,N-dihydroxy-L-tryptophan = (E)-indol-3-ylacetaldoxime + CO2 + H2O
Other name(s): tryptophan N-hydroxylase; CYP79B1; CYP79B2; CYP79B3
Systematic name: L-tryptophan,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein from the plant Arabidopsis thaliana. This enzyme catalyses two successive N-hydroxylations of L-tryptophan, the first steps in the biosynthesis of both auxin and the indole alkaloid phytoalexin camalexin. The product of the two hydroxylations, N,N-dihydroxy-L-tryptophan, is extremely labile and dehydrates spontaneously. The dehydrated product is then subject to a decarboxylation that produces an oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Mikkelsen, M.D., Hansen, C.H., Wittstock, U. and Halkier, B.A. Cytochrome P450 CYP79B2 from Arabidopsis catalyzes the conversion of tryptophan to indole-3-acetaldoxime, a precursor of indole glucosinolates and indole-3-acetic acid. J. Biol. Chem. 275 (2000) 33712–33717. [DOI] [PMID: 10922360]
2.  Hull, A.K., Vij, R. and Celenza, J.L. Arabidopsis cytochrome P450s that catalyze the first step of tryptophan-dependent indole-3-acetic acid biosynthesis. Proc. Natl. Acad. Sci. USA 97 (2000) 2379–2384. [DOI] [PMID: 10681464]
3.  Zhao, Y., Hull, A.K., Gupta, N.R., Goss, K.A., Alonso, J., Ecker, J.R., Normanly, J., Chory, J. and Celenza, J.L. Trp-dependent auxin biosynthesis in Arabidopsis: involvement of cytochrome P450s CYP79B2 and CYP79B3. Genes Dev. 16 (2002) 3100–3112. [DOI] [PMID: 12464638]
4.  Naur, P., Hansen, C.H., Bak, S., Hansen, B.G., Jensen, N.B., Nielsen, H.L. and Halkier, B.A. CYP79B1 from Sinapis alba converts tryptophan to indole-3-acetaldoxime. Arch. Biochem. Biophys. 409 (2003) 235–241. [DOI] [PMID: 12464264]
[EC 1.14.14.156 created 2011 as EC 1.14.13.125, transferred 2018 to EC 1.14.14.156]
 
 
EC 1.14.14.158     
Accepted name: carotenoid &epsilon; hydroxylase
Reaction: (1) α-carotene + [reduced NADPH-hemoprotein reductase] + O2 = α-cryptoxanthin + [oxidized NADPH-hemoprotein reductase] + H2O
(2) zeinoxanthin + [reduced NADPH-hemoprotein reductase] + O2 = lutein + [oxidized NADPH-hemoprotein reductase] + H2O
For diagram of lutein biosynthesis, click here
Other name(s): CYP97C1; LUT1; CYP97C; carotene &epsilon;-monooxygenase
Systematic name: α-carotene,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (3-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Pogson, B., McDonald, K.A., Truong, M., Britton, G. and DellaPenna, D. Arabidopsis carotenoid mutants demonstrate that lutein is not essential for photosynthesis in higher plants. Plant Cell 8 (1996) 1627–1639. [DOI] [PMID: 8837513]
2.  Tian, L., Musetti, V., Kim, J., Magallanes-Lundback, M. and DellaPenna, D. The Arabidopsis LUT1 locus encodes a member of the cytochrome P450 family that is required for carotenoid &epsilon;-ring hydroxylation activity. Proc. Natl. Acad. Sci. USA 101 (2004) 402–407. [DOI] [PMID: 14709673]
3.  Stigliani, A.L., Giorio, G. and D'Ambrosio, C. Characterization of P450 carotenoid β- and &epsilon;-hydroxylases of tomato and transcriptional regulation of xanthophyll biosynthesis in root, leaf, petal and fruit. Plant Cell Physiol. 52 (2011) 851–865. [PMID: 21450689]
4.  Chang, S., Berman, J., Sheng, Y., Wang, Y., Capell, T., Shi, L., Ni, X., Sandmann, G., Christou, P. and Zhu, C. Cloning and functional characterization of the maize (Zea mays L.) carotenoid &epsilon; hydroxylase gene. PLoS One 10:e0128758 (2015). [PMID: 26030746]
5.  Reddy, C.S., Lee, S.H., Yoon, J.S., Kim, J.K., Lee, S.W., Hur, M., Koo, S.C., Meilan, J., Lee, W.M., Jang, J.K., Hur, Y., Park, S.U. and Kim, A.YB. Molecular cloning and characterization of carotenoid pathway genes and carotenoid content in Ixeris dentata var. albiflora. Molecules 22 (2017) . [DOI] [PMID: 28858245]
[EC 1.14.14.158 created 2011 as EC 1.14.99.45, transferred 2018 to EC 1.14.14.158]
 
 
EC 1.14.14.165     
Accepted name: indole-3-carbonyl nitrile 4-hydroxylase
Reaction: indole-3-carbonyl nitrile + [reduced NADPH—hemoprotein reductase] + O2 = 4-hydroxyindole-3-carbonyl nitrile + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: indole-3-carbonyl nitrile = 2-(1H-indole-3-yl)-2-oxoacetonitrile
4-hydroxyindole-3-carbonyl nitrile = 2-(4-hydroxy-1H-indole-3-yl)-2-oxoacetonitrile
Other name(s): CYP82C2
Systematic name: indole-3-carbonyl nitrile,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (4-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein characterized from the plant Arabidopsis thaliana. Involved in biosynthesis of small cyanogenic compounds that take part in pathogen defense. The enzyme also catalyses the 5-hydroxylation of xanthotoxin [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kruse, T., Ho, K., Yoo, H.D., Johnson, T., Hippely, M., Park, J.H., Flavell, R. and Bobzin, S. In planta biocatalysis screen of P450s identifies 8-methoxypsoralen as a substrate for the CYP82C subfamily, yielding original chemical structures. Chem. Biol. 15 (2008) 149–156. [PMID: 18291319]
2.  Rajniak, J., Barco, B., Clay, N.K. and Sattely, E.S. A new cyanogenic metabolite in Arabidopsis required for inducible pathogen defence. Nature 525 (2015) 376–379. [PMID: 26352477]
[EC 1.14.14.165 created 2018]
 
 
EC 1.14.14.178     
Accepted name: steroid 22S-hydroxylase
Reaction: (1) a C27-steroid + O2 + [reduced NADPH—hemoprotein reductase] = a (22S)-22-hydroxy-C27-steroid + 2 H2O + [oxidized NADPH—hemoprotein reductase]
(2) a C28-steroid + O2 + [reduced NADPH—hemoprotein reductase] = a (22S)-22-hydroxy-C28-steroid + 2 H2O + [oxidized NADPH—hemoprotein reductase]
(3) a C29-steroid + O2 + [reduced NADPH—hemoprotein reductase] = a (22S)-22-hydroxy-C29-steroid + 2 H2O + [oxidized NADPH—hemoprotein reductase]
Other name(s): CYP90B1 (gene name); DWF4 (gene name); steroid C-22 hydroxylase
Systematic name: steroid,NADPH—hemoprotein reductase:oxygen 22S-oxidoreductase (hydroxylating)
Comments: This plant cytochrome P-450 (heme thiolate) enzyme participates in the biosynthesis of brassinosteroids. While in vivo substrates include C28-steroids such as campestanol, campesterol, and 6-oxocampestanol, the enzyme is able to catalyse the C-22 hydroxylation of a variety of C27, C28 and C29 steroids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Asami, T., Mizutani, M., Fujioka, S., Goda, H., Min, Y.K., Shimada, Y., Nakano, T., Takatsuto, S., Matsuyama, T., Nagata, N., Sakata, K. and Yoshida, S. Selective interaction of triazole derivatives with DWF4, a cytochrome P450 monooxygenase of the brassinosteroid biosynthetic pathway, correlates with brassinosteroid deficiency in planta. J. Biol. Chem. 276 (2001) 25687–25691. [DOI] [PMID: 11319239]
2.  Choe, S., Fujioka, S., Noguchi, T., Takatsuto, S., Yoshida, S. and Feldmann, K.A. Overexpression of DWARF4 in the brassinosteroid biosynthetic pathway results in increased vegetative growth and seed yield in Arabidopsis. Plant J. 26 (2001) 573–582. [DOI] [PMID: 11489171]
3.  Asami, T., Mizutani, M., Shimada, Y., Goda, H., Kitahata, N., Sekimata, K., Han, S.Y., Fujioka, S., Takatsuto, S., Sakata, K. and Yoshida, S. Triadimefon, a fungicidal triazole-type P450 inhibitor, induces brassinosteroid deficiency-like phenotypes in plants and binds to DWF4 protein in the brassinosteroid biosynthesis pathway. Biochem. J. 369 (2003) 71–76. [DOI] [PMID: 12350224]
4.  Fujita, S., Ohnishi, T., Watanabe, B., Yokota, T., Takatsuto, S., Fujioka, S., Yoshida, S., Sakata, K. and Mizutani, M. Arabidopsis CYP90B1 catalyses the early C-22 hydroxylation of C27, C28 and C29 sterols. Plant J. 45 (2006) 765–774. [DOI] [PMID: 16460510]
5.  Ohnishi, T., Watanabe, B., Sakata, K. and Mizutani, M. CYP724B2 and CYP90B3 function in the early C-22 hydroxylation steps of brassinosteroid biosynthetic pathway in tomato. Biosci. Biotechnol. Biochem. 70 (2006) 2071–2080. [DOI] [PMID: 16960392]
[EC 1.14.14.178 created 2022]
 
 
EC 1.14.14.179     
Accepted name: brassinosteroid 6-oxygenase
Reaction: 6-deoxocastasterone + 2 O2 + 2 [reduced NADPH—hemoprotein reductase] = castasterone + 3 H2O + 2 [oxidized NADPH—hemoprotein reductase] (overall reaction)
(1a) 6-deoxocastasterone + O2 + [reduced NADPH—hemoprotein reductase] = 6α-hydroxy-6-deoxocastasterone + H2O + [oxidized NADPH—hemoprotein reductase]
(1b) 6α-hydroxy-6-deoxocastasterone + O2 + [reduced NADPH—hemoprotein reductase] = castasterone + 2 H2O + [oxidized NADPH—hemoprotein reductase]
For diagram of brassinolide biosynthesis, click here
Other name(s): CYP85A1 (gene name); CYP85A2 (gene name); brassinosteroid 6-oxidase
Systematic name: 6-deoxocastasterone,NADPH—hemoprotein reductase:oxygen 6-oxidoreductase (castasterone-forming)
Comments: This cytochrome P-450 (heme thiolate) plant enzyme catalyses the C-6 hydoxylation of several brassinosteroid biosynthesis intermediates, and the further oxidation of the hydroxyl group to an oxo group. Substrates include 6-deoxocastasterone, 6-deoxotyphasterol, 3-dehydro-6-deoxoteasterone, and 6-deoxoteasterone. The CYP85A2 isozyme of Arabidopsis thaliana (but not the CYP85A1 isozyme) also catalyses the activity of EC 1.14.14.180, brassinolide synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Shimada, Y., Fujioka, S., Miyauchi, N., Kushiro, M., Takatsuto, S., Nomura, T., Yokota, T., Kamiya, Y., Bishop, G.J. and Yoshida, S. Brassinosteroid-6-oxidases from Arabidopsis and tomato catalyze multiple C-6 oxidations in brassinosteroid biosynthesis. Plant Physiol. 126 (2001) 770–779. [DOI] [PMID: 11402205]
2.  Perez-Espana, V.H., Sanchez-Leon, N. and Vielle-Calzada, J.P. CYP85A1 is required for the initiation of female gametogenesis in Arabidopsis thaliana. Plant Signal Behav. 6 (2011) 321–326. [DOI] [PMID: 21364326]
[EC 1.14.14.179 created 2022]
 
 
EC 1.14.14.180     
Accepted name: brassinolide synthase
Reaction: castasterone + O2 + [reduced NADPH—hemoprotein reductase] = brassinolide + 2 H2O + [oxidized NADPH—hemoprotein reductase]
For diagram of brassinolide biosynthesis, click here
Other name(s): CYP85A2 (gene name); CYP85A3 (gene name)
Systematic name: castasterone,NADPH—hemoprotein reductase:oxygen oxidoreductase (lactonizing, brassinolide-forming)
Comments: This cytochrome P-450 (heme thiolate) plant enzyme catalyses the lactonization of several brassinosteroids, including castasterone, teasterone, and typhasterol. The CYP85A2 enzyme of Arabidopsis thaliana also catalyses the activity of EC 1.14.14.179, brassinosteroid 6-oxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Nomura, T., Kushiro, T., Yokota, T., Kamiya, Y., Bishop, G.J. and Yamaguchi, S. The last reaction producing brassinolide is catalyzed by cytochrome P-450s, CYP85A3 in tomato and CYP85A2 in Arabidopsis. J. Biol. Chem. 280 (2005) 17873–17879. [DOI] [PMID: 15710611]
2.  Kim, T.W., Hwang, J.Y., Kim, Y.S., Joo, S.H., Chang, S.C., Lee, J.S., Takatsuto, S. and Kim, S.K. Arabidopsis CYP85A2, a cytochrome P450, mediates the Baeyer-Villiger oxidation of castasterone to brassinolide in brassinosteroid biosynthesis. Plant Cell 17 (2005) 2397–2412. [DOI] [PMID: 16024588]
3.  Katsumata, T., Hasegawa, A., Fujiwara, T., Komatsu, T., Notomi, M., Abe, H., Natsume, M. and Kawaide, H. Arabidopsis CYP85A2 catalyzes lactonization reactions in the biosynthesis of 2-deoxy-7-oxalactone brassinosteroids. Biosci. Biotechnol. Biochem. 72 (2008) 2110–2117. [DOI] [PMID: 18685225]
[EC 1.14.14.180 created 2022]
 
 
EC 1.14.15.9     
Accepted name: spheroidene monooxygenase
Reaction: (1) spheroidene + 4 reduced ferredoxin [iron-sulfur] cluster + 2 O2 + 4 H+ = spheroiden-2-one + 4 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O (overall reaction)
(1a) spheroidene + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = 2-hydroxyspheroidene + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(1b) 2-hydroxyspheroidene + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = 2,2-dihydroxyspheroidene + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(1c) 2,2-dihydroxyspheroidene = spheroiden-2-one + H2O (spontaneous)
(2) spirilloxanthin + 4 reduced ferredoxin [iron-sulfur] cluster + 2 O2 + 4 H+ = 2-oxospirilloxanthin + 4 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O (overall reaction)
(2a) spirilloxanthin + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = 2-hydroxyspirilloxanthin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(2b) 2-hydroxyspirilloxanthin + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = 2,2-dihydroxyspirilloxanthin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(2c) 2,2-dihydroxyspirilloxanthin = 2-oxospirilloxanthin + H2O (spontaneous)
(3) 2-oxospirilloxanthin + 4 reduced ferredoxin [iron-sulfur] cluster + 2 O2 + 4 H+ = 2,2′-dioxospirilloxanthin + 4 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O (overall reaction)
(3a) 2-oxospirilloxanthin + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = 2′-hydroxy-2-oxospirilloxanthin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(3b) 2′-hydroxy-2-oxospirilloxanthin + reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = 2′,2′-dihydroxy-2-oxospirilloxanthin + oxidized ferredoxin [iron-sulfur] cluster + H2O
(3c) 2′,2′-dihydroxy-2-oxospirilloxanthin = 2,2′-dioxospirilloxanthin + H2O (spontaneous)
For diagram of 2,2′-dioxospirilloxanthin biosynthesis, click here and for diagram of 4.2.1.131, click here
Glossary: spheroidene = 3,4-didehydro-1-methoxy-1,2,7′,8′-tetrahydro-&psi;,&psi;-carotene
Other name(s): CrtA; acyclic carotenoid 2-ketolase; spirilloxanthin monooxygenase; 2-oxo-spirilloxanthin monooxygenase
Systematic name: spheroidene,reduced-ferredoxin:oxygen oxidoreductase (spheroiden-2-one-forming)
Comments: The enzyme is involved in spheroidenone biosynthesis and in 2,2′-dioxospirilloxanthin biosynthesis. The enzyme from Rhodobacter sphaeroides contains heme at its active site [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Lee, P.C., Holtzapple, E. and Schmidt-Dannert, C. Novel activity of Rhodobacter sphaeroides spheroidene monooxygenase CrtA expressed in Escherichia coli. Appl. Environ. Microbiol. 76 (2010) 7328–7331. [DOI] [PMID: 20851979]
2.  Gerjets, T., Steiger, S. and Sandmann, G. Catalytic properties of the expressed acyclic carotenoid 2-ketolases from Rhodobacter capsulatus and Rubrivivax gelatinosus. Biochim. Biophys. Acta 1791 (2009) 125–131. [DOI] [PMID: 19136077]
[EC 1.14.15.9 created 2012, modified 2016]
 
 
EC 1.14.15.17     
Accepted name: pheophorbide a oxygenase
Reaction: pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster (overall reaction)
(1a) pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = epoxypheophorbide a + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(1b) epoxypheophorbide a + H2O = red chlorophyll catabolite (spontaneous)
For diagram of chlorophyll catabolism, click here
Glossary: red chlorophyll catabolite = RCC = (7S,8S,101R)-8-(2-carboxyethyl)-8,23-dihydro-17-ethyl-19-formyl-101-(methoxycarbonyl)-3,7,13,18-tetramethyl-2-vinyl-7H-10,12-ethanobiladiene-ab-1,102(21H)-dione
Other name(s): pheide a monooxygenase; pheide a oxygenase; PaO; PAO
Systematic name: pheophorbide-a,ferredoxin:oxygen oxidoreductase (biladiene-forming)
Comments: This enzyme catalyses a key reaction in chlorophyll degradation, which occurs during leaf senescence and fruit ripening in higher plants. The enzyme from Arabidopsis contains a Rieske-type iron-sulfur cluster [2] and requires reduced ferredoxin, which is generated either by NADPH through the pentose-phosphate pathway or by the action of photosystem I [4]. While still attached to this enzyme, the product is rapidly converted into primary fluorescent chlorophyll catabolite by the action of EC 1.3.7.12, red chlorophyll catabolite reductase [2,6]. Pheophorbide b acts as an inhibitor. In 18O2 labelling experiments, only the aldehyde oxygen is labelled, suggesting that the other oxygen atom may originate from H2O [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hörtensteiner, S., Wüthrich, K.L., Matile, P., Ongania, K.H. and Kräutler, B. The key step in chlorophyll breakdown in higher plants. Cleavage of pheophorbide a macrocycle by a monooxygenase. J. Biol. Chem. 273 (1998) 15335–15339. [DOI] [PMID: 9624113]
2.  Pružinská, A., Tanner, G., Anders, I., Roca, M. and Hörtensteiner, S. Chlorophyll breakdown: pheophorbide a oxygenase is a Rieske-type iron-sulfur protein, encoded by the accelerated cell death 1 gene. Proc. Natl. Acad. Sci. USA 100 (2003) 15259–15264. [DOI] [PMID: 14657372]
3.  Chung, D.W., Pružinská, A., Hörtensteiner, S. and Ort, D.R. The role of pheophorbide a oxygenase expression and activity in the canola green seed problem. Plant Physiol. 142 (2006) 88–97. [DOI] [PMID: 16844830]
4.  Rodoni, S., Mühlecker, W., Anderl, M., Kräutler, B., Moser, D., Thomas, H., Matile, P. and Hörtensteiner, S. Chlorophyll breakdown in senescent chloroplasts. Cleavage of pheophorbide a in two enzymic steps. Plant Physiol. 115 (1997) 669–676. [PMID: 12223835]
5.  Hörtensteiner, S. Chlorophyll degradation during senescence. Annu. Rev. Plant Biol. 57 (2006) 55–77. [DOI] [PMID: 16669755]
6.  Pružinská, A., Anders, I., Aubry, S., Schenk, N., Tapernoux-Lüthi, E., Müller, T., Kräutler, B. and Hörtensteiner, S. In vivo participation of red chlorophyll catabolite reductase in chlorophyll breakdown. Plant Cell 19 (2007) 369–387. [DOI] [PMID: 17237353]
[EC 1.14.15.17 created 2007 as EC 1.14.12.20, transferred 2016 to EC 1.14.15.17]
 
 
EC 1.14.15.24     
Accepted name: β-carotene 3-hydroxylase
Reaction: β-carotene + 4 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + 2 O2 = zeaxanthin + 4 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O (overall reaction)
(1a) β-carotene + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2 = β-cryptoxanthin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(1b) β-cryptoxanthin + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2 = zeaxanthin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
For diagram of lutein biosynthesis, click here and for diagram of zeaxanthin biosynthesis, click here
Other name(s): β-carotene 3,3′-monooxygenase; CrtZ
Systematic name: β-carotene,reduced ferredoxin [iron-sulfur] cluster:oxygen 3-oxidoreductase
Comments: Requires ferredoxin and iron(II). Also acts on other carotenoids with a β-end group. In some species canthaxanthin is the preferred substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sun, Z., Gantt, E. and Cunningham, F.X., Jr. Cloning and functional analysis of the β-carotene hydroxylase of Arabidopsis thaliana. J. Biol. Chem. 271 (1996) 24349–24352. [DOI] [PMID: 8798688]
2.  Fraser, P.D., Miura, Y. and Misawa, N. In vitro characterization of astaxanthin biosynthetic enzymes. J. Biol. Chem. 272 (1997) 6128–6135. [DOI] [PMID: 9045623]
3.  Fraser, P.D., Shimada, H. and Misawa, N. Enzymic confirmation of reactions involved in routes to astaxanthin formation, elucidated using a direct substrate in vitro assay. Eur. J. Biochem. 252 (1998) 229–236. [DOI] [PMID: 9523693]
4.  Bouvier, F., Keller, Y., d'Harlingue, A. and Camara, B. Xanthophyll biosynthesis: molecular and functional characterization of carotenoid hydroxylases from pepper fruits (Capsicum annuum L.). Biochim. Biophys. Acta 1391 (1998) 320–328. [DOI] [PMID: 9555077]
5.  Linden, H. Carotenoid hydroxylase from Haematococcus pluvialis: cDNA sequence, regulation and functional complementation. Biochim. Biophys. Acta 1446 (1999) 203–212. [DOI] [PMID: 10524195]
6.  Zhu, C., Yamamura, S., Nishihara, M., Koiwa, H. and Sandmann, G. cDNAs for the synthesis of cyclic carotenoids in petals of Gentiana lutea and their regulation during flower development. Biochim. Biophys. Acta 1625 (2003) 305–308. [DOI] [PMID: 12591618]
7.  Choi, S.K., Matsuda, S., Hoshino, T., Peng, X. and Misawa, N. Characterization of bacterial β-carotene 3,3′-hydroxylases, CrtZ, and P450 in astaxanthin biosynthetic pathway and adonirubin production by gene combination in Escherichia coli. Appl. Microbiol. Biotechnol. 72 (2006) 1238–1246. [DOI] [PMID: 16614859]
[EC 1.14.15.24 created 2011 as EC 1.14.13.129, transferred 2017 to EC 1.14.15.24]
 
 
EC 1.14.18.4     
Accepted name: phosphatidylcholine 12-monooxygenase
Reaction: a 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + 2 ferrocytochrome b5 + O2 + 2 H+ = a 1-acyl-2-[(12R)-12-hydroxyoleoyl]-sn-glycero-3-phosphocholine + 2 ferricytochrome b5 + H2O
Glossary: ricinoleic acid = (9Z,12R)-12-hydroxyoctadec-9-enoic acid
Other name(s): ricinoleic acid synthase; oleate Δ12-hydroxylase; oleate Δ12-monooxygenase
Systematic name: 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine,ferrocytochrome-b5:oxygen oxidoreductase (12-hydroxylating)
Comments: The enzyme, characterized from the plant Ricinus communis (castor bean), is involved in production of the 12-hydroxylated fatty acid ricinoleate. The enzyme, which shares sequence similarity with fatty-acyl desaturases, requires a cytochrome b5 as the electron donor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 77950-95-9
References:
1.  Galliard, T. and Stumpf, P.K. Fat metabolism in higher plants. 30. Enzymatic synthesis of ricinoleic acid by a microsomal preparation from developing Ricinus communis seeds. J. Biol. Chem. 241 (1966) 5806–5812. [PMID: 4289003]
2.  Moreau, R.A. and Stumpf, P.K. Recent studies of the enzymic-synthesis of ricinoleic acid by developing castor beans. Plant Physiol. 67 (1981) 672–676. [PMID: 16661734]
3.  Smith, M.A., Jonsson, L., Stymne, S. and Stobart, K. Evidence for cytochrome b5 as an electron donor in ricinoleic acid biosynthesis in microsomal preparations from developing castor bean (Ricinus communis L.). Biochem. J. 287 (1992) 141–144. [PMID: 1417766]
4.  Lin, J.T., McKeon, T.A., Goodrich-Tanrikulu, M. and Stafford, A.E. Characterization of oleoyl-12-hydroxylase in castor microsomes using the putative substrate, 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine. Lipids 31 (1996) 571–577. [DOI] [PMID: 8784737]
5.  Broun, P. and Somerville, C. Accumulation of ricinoleic, lesquerolic, and densipolic acids in seeds of transgenic Arabidopsis plants that express a fatty acyl hydroxylase cDNA from castor bean. Plant Physiol. 113 (1997) 933–942. [PMID: 9085577]
[EC 1.14.18.4 created 1984 as EC 1.14.13.26, transferred 2015 to EC 1.14.18.4]
 
 
EC 1.14.18.5     
Accepted name: sphingolipid C4-monooxygenase
Reaction: a dihydroceramide + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4R)-4-hydroxysphinganine ceramide + 2 ferricytochrome b5 + H2O
Other name(s): sphinganine C4-monooxygenase; sphingolipid C4-hydroxylase; SUR2 (gene name); SBH1 (gene name); SBH2 (gene name); DEGS2 (gene name)
Systematic name: dihydroceramide,ferrocytochrome b5:oxygen oxidoreductase (C4-hydroxylating)
Comments: The enzyme, which belongs to the familiy of endoplasmic reticular cytochrome b5-dependent enzymes, is involved in the biosynthesis of sphingolipids in eukaryotes. Some enzymes are bifunctional and also catalyse EC 1.14.19.17, sphingolipid 4-desaturase [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Haak, D., Gable, K., Beeler, T. and Dunn, T. Hydroxylation of Saccharomyces cerevisiae ceramides requires Sur2p and Scs7p. J. Biol. Chem. 272 (1997) 29704–29710. [DOI] [PMID: 9368039]
2.  Grilley, M.M., Stock, S.D., Dickson, R.C., Lester, R.L. and Takemoto, J.Y. Syringomycin action gene SYR2 is essential for sphingolipid 4-hydroxylation in Saccharomyces cerevisiae. J. Biol. Chem. 273 (1998) 11062–11068. [DOI] [PMID: 9556590]
3.  Sperling, P., Ternes, P., Moll, H., Franke, S., Zähringer, U. and Heinz, E. Functional characterization of sphingolipid C4-hydroxylase genes from Arabidopsis thaliana. FEBS Lett. 494 (2001) 90–94. [DOI] [PMID: 11297741]
4.  Ternes, P., Franke, S., Zähringer, U., Sperling, P. and Heinz, E. Identification and characterization of a sphingolipid Δ4-desaturase family. J. Biol. Chem. 277 (2002) 25512–25518. [DOI] [PMID: 11937514]
5.  Mizutani, Y., Kihara, A. and Igarashi, Y. Identification of the human sphingolipid C4-hydroxylase, hDES2, and its up-regulation during keratinocyte differentiation. FEBS Lett. 563 (2004) 93–97. [DOI] [PMID: 15063729]
[EC 1.14.18.5 created 2012 as EC 1.14.13.169, transferred 2015 to EC 1.14.18.5]
 
 
EC 1.14.18.6     
Accepted name: 4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase
Reaction: a phytoceramide + 2 ferrocytochrome b5 + O2 + 2 H+ = a (2′R)-2′-hydroxyphytoceramide + 2 ferricytochrome b5 + H2O
Glossary: a phytoceramide = a (4R)-4-hydroxysphinganine ceramide = an N-acyl-4-hydroxysphinganine
Other name(s): FA2H (gene name); SCS7 (gene name)
Systematic name: (4R)-4-hydroxysphinganine ceramide,ferrocytochrome-b5:oxygen oxidoreductase (fatty acyl 2-hydroxylating)
Comments: The enzyme, characterized from yeast and mammals, catalyses the hydroxylation of carbon 2 of long- or very-long-chain fatty acids attached to (4R)-4-hydroxysphinganine during de novo ceramide synthesis. The enzymes from yeast and from mammals contain an N-terminal cytochrome b5 domain that acts as the direct electron donor to the desaturase active site. The newly introduced 2-hydroxyl group has R-configuration. cf. EC 1.14.18.7, dihydroceramide fatty acyl 2-hydroxylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Mitchell, A.G. and Martin, C.E. Fah1p, a Saccharomyces cerevisiae cytochrome b5 fusion protein, and its Arabidopsis thaliana homolog that lacks the cytochrome b5 domain both function in the α-hydroxylation of sphingolipid-associated very long chain fatty acids. J. Biol. Chem. 272 (1997) 28281–28288. [DOI] [PMID: 9353282]
2.  Dunn, T.M., Haak, D., Monaghan, E. and Beeler, T.J. Synthesis of monohydroxylated inositolphosphorylceramide (IPC-C) in Saccharomyces cerevisiae requires Scs7p, a protein with both a cytochrome b5-like domain and a hydroxylase/desaturase domain. Yeast 14 (1998) 311–321. [DOI] [PMID: 9559540]
3.  Alderson, N.L., Rembiesa, B.M., Walla, M.D., Bielawska, A., Bielawski, J. and Hama, H. The human FA2H gene encodes a fatty acid 2-hydroxylase. J. Biol. Chem. 279 (2004) 48562–48568. [DOI] [PMID: 15337768]
4.  Eckhardt, M., Yaghootfam, A., Fewou, S.N., Zoller, I. and Gieselmann, V. A mammalian fatty acid hydroxylase responsible for the formation of α-hydroxylated galactosylceramide in myelin. Biochem. J. 388 (2005) 245–254. [DOI] [PMID: 15658937]
5.  Guo, L., Zhang, X., Zhou, D., Okunade, A.L. and Su, X. Stereospecificity of fatty acid 2-hydroxylase and differential functions of 2-hydroxy fatty acid enantiomers. J. Lipid Res. 53 (2012) 1327–1335. [DOI] [PMID: 22517924]
[EC 1.14.18.6 created 2015]
 
 
EC 1.14.18.7     
Accepted name: dihydroceramide fatty acyl 2-hydroxylase
Reaction: a dihydroceramide + 2 ferrocytochrome b5 + O2 + 2 H+ = a (2′R)-2′-hydroxydihydroceramide + 2 ferricytochrome b5 + H2O
Glossary: a dihydroceramide = an N-acylsphinganine
Other name(s): FAH1 (gene name); FAH2 (gene name); plant sphingolipid fatty acid 2-hydroxylase
Systematic name: dihydroceramide,ferrocytochrome-b5:oxygen oxidoreductase (fatty acyl 2-hydroxylating)
Comments: The enzyme, characterized from plants, catalyses the hydroxylation of carbon 2 of long- or very-long-chain fatty acids attached to sphinganine during de novo ceramide synthesis. The enzyme requires an external cytochrome b5 as the electron donor. The newly introduced 2-hydroxyl group has R-configuration. cf. EC 1.14.18.6, 4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Nagano, M., Ihara-Ohori, Y., Imai, H., Inada, N., Fujimoto, M., Tsutsumi, N., Uchimiya, H. and Kawai-Yamada, M. Functional association of cell death suppressor, Arabidopsis Bax inhibitor-1, with fatty acid 2-hydroxylation through cytochrome b5. Plant J. 58 (2009) 122–134. [DOI] [PMID: 19054355]
2.  Nagano, M., Takahara, K., Fujimoto, M., Tsutsumi, N., Uchimiya, H. and Kawai-Yamada, M. Arabidopsis sphingolipid fatty acid 2-hydroxylases (AtFAH1 and AtFAH2) are functionally differentiated in fatty acid 2-hydroxylation and stress responses. Plant Physiol. 159 (2012) 1138–1148. [DOI] [PMID: 22635113]
3.  Nagano, M., Uchimiya, H. and Kawai-Yamada, M. Plant sphingolipid fatty acid 2-hydroxylases have unique characters unlike their animal and fungus counterparts. Plant Signal. Behav. 7 (2012) 1388–1392. [DOI] [PMID: 22918503]
[EC 1.14.18.7 created 2015]
 
 
EC 1.14.18.10     
Accepted name: plant 4,4-dimethylsterol C-4α-methyl-monooxygenase
Reaction: 24-methylidenecycloartanol + 6 ferrocytochrome b5 + 3 O2 + 6 H+ = 3β-hydroxy-4β,14α-dimethyl-9β,19-cyclo-5α-ergost-24(241)-en-4α-carboxylate + 6 ferricytochrome b5 + 4 H2O (overall reaction)
(1a) 24-methylidenecycloartanol + 2 ferrocytochrome b5 + O2 + 2 H+ = 4α-(hydroxymethyl)-4β,14α-dimethyl-9β,19-cyclo-5α-ergost-24(241)-en-3β-ol + 2 ferricytochrome b5 + H2O
(1b) 4α-(hydroxymethyl)-4β,14α-dimethyl-9β,19-cyclo-5α-ergost-24(241)-en-3β-ol + 2 ferrocytochrome b5 + O2 + 2 H+ = 4α-formyl-4β,14α-dimethyl-9β,19-cyclo-5α-ergost-24(241)-en-3β-ol + 2 ferricytochrome b5 + 2 H2O
(1c) 4α-formyl-4β,14α-dimethyl-9β,19-cyclo-5α-ergost-24(241)-en-3β-ol + 2 ferrocytochrome b5 + O2 + 2 H+ = 3β-hydroxy-4β,14α-dimethyl-9β,19-cyclo-5α-ergost-24(241)-en-4α-carboxylate + 2 ferricytochrome b5 + H2O
Glossary: 24-methylidenecycloartanol = 4α,4β,14α-trimethyl-9β,19-cyclo-5α-ergost-24(241)-en-3β-ol
Other name(s): SMO1 (gene name)
Systematic name: 24-methylidenecycloartanol,ferrocytochrome-b5:oxygen oxidoreductase (C-4α-methyl-hydroxylating)
Comments: This plant enzyme catalyses a step in the biosynthesis of sterols. It acts on the 4α-methyl group of the 4,4-dimethylated intermediate 24-methylidenecycloartanol and catalyses three successive oxidations, turning it into a carboxyl group. The carboxylate is subsequently removed by EC 1.1.1.418, plant 3β-hydroxysteroid-4α-carboxylate 3-dehydrogenase (decarboxylating), which also catalyses the epimerization of the remaining 4β-methyl into the 4α position. Unlike the fungal/animal enzyme EC 1.14.18.9, 4α-methylsterol monooxygenase, this enzyme is not able to remove the methyl group from C-4-monomethylated substrates. That activity is performed in plants by a second enzyme, EC 1.14.18.11, plant 4α-monomethylsterol monooxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Pascal, S., Taton, M. and Rahier, A. Plant sterol biosynthesis. Identification and characterization of two distinct microsomal oxidative enzymatic systems involved in sterol C4-demethylation. J. Biol. Chem. 268 (1993) 11639–11654. [PMID: 8505296]
2.  Rahier, A., Smith, M. and Taton, M. The role of cytochrome b5 in 4α-methyl-oxidation and C5(6) desaturation of plant sterol precursors. Biochem. Biophys. Res. Commun. 236 (1997) 434–437. [DOI] [PMID: 9240456]
3.  Darnet, S., Bard, M. and Rahier, A. Functional identification of sterol-4α-methyl oxidase cDNAs from Arabidopsis thaliana by complementation of a yeast erg25 mutant lacking sterol-4α-methyl oxidation. FEBS Lett. 508 (2001) 39–43. [PMID: 11707264]
4.  Darnet, S. and Rahier, A. Plant sterol biosynthesis: identification of two distinct families of sterol 4α-methyl oxidases. Biochem. J. 378 (2004) 889–898. [PMID: 14653780]
[EC 1.14.18.10 created 2019]
 
 
EC 1.14.18.11     
Accepted name: plant 4α-monomethylsterol monooxygenase
Reaction: 24-methylidenelophenol + 6 ferrocytochrome b5 + 3 O2 + 6 H+ = 3β-hydroxyergosta-7,24(241)-dien-4α-carboxylate + 6 ferricytochrome b5 + 4 H2O (overall reaction)
(1a) 24-methylidenelophenol + 2 ferrocytochrome b5 + O2 + 2 H+ = 4α-(hydroxymethyl)ergosta-7,24(241)-dien-3β-ol + 2 ferricytochrome b5 + H2O
(1b) 4α-(hydroxymethyl)ergosta-7,24(241)-dien-3β-ol + 2 ferrocytochrome b5 + O2 + 2 H+ = 4α-formylergosta-7,24(241)-dien-3β-ol + 2 ferricytochrome b5 + 2 H2O
(1c) 4α-formylergosta-7,24(241)-dien-3β-ol + 2 ferrocytochrome b5 + O2 + 2 H+ = 3β-hydroxyergosta-7,24(241)-dien-4α-carboxylate + 2 ferricytochrome b5 + H2O
Glossary: 24-methylidenelophenol = 4α-methyl-5α-ergosta-7,24-dien-3β-ol
Other name(s): SMO2 (gene name)
Systematic name: 24-ethylidenelophenol,ferrocytochrome-b5:oxygen oxidoreductase (C-4α-methyl-hydroxylating)
Comments: This plant enzyme catalyses a step in the biosynthesis of sterols. It acts on the methyl group of the 4α-methylated intermediates 24-ethylidenelophenol and 24-methylidenelophenol and catalyses three successive oxidations, turning it into a carboxyl group. The carboxylate is subsequently removed by EC 1.1.1.418, plant 3β-hydroxysteroid-4α-carboxylate 3-dehydrogenase (decarboxylating). Unlike the fungal/animal enzyme EC 1.14.18.9, 4α-methylsterol monooxygenase, this enzyme is not able to act on 4,4-dimethylated substrates. That activity, which occurs earlier in the pathway, is performed in plants by a second enzyme, EC 1.14.18.10, plant 4,4-dimethylsterol C-4α-methyl-monooxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Pascal, S., Taton, M. and Rahier, A. Plant sterol biosynthesis. Identification and characterization of two distinct microsomal oxidative enzymatic systems involved in sterol C4-demethylation. J. Biol. Chem. 268 (1993) 11639–11654. [PMID: 8505296]
2.  Rahier, A., Smith, M. and Taton, M. The role of cytochrome b5 in 4α-methyl-oxidation and C5(6) desaturation of plant sterol precursors. Biochem. Biophys. Res. Commun. 236 (1997) 434–437. [DOI] [PMID: 9240456]
3.  Darnet, S., Bard, M. and Rahier, A. Functional identification of sterol-4α-methyl oxidase cDNAs from Arabidopsis thaliana by complementation of a yeast erg25 mutant lacking sterol-4α-methyl oxidation. FEBS Lett. 508 (2001) 39–43. [PMID: 11707264]
4.  Darnet, S. and Rahier, A. Plant sterol biosynthesis: identification of two distinct families of sterol 4α-methyl oxidases. Biochem. J. 378 (2004) 889–898. [PMID: 14653780]
[EC 1.14.18.11 created 2019]
 
 
EC 1.14.19.2     
Accepted name: stearoyl-[acyl-carrier-protein] 9-desaturase
Reaction: stearoyl-[acyl-carrier protein] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = oleoyl-[acyl-carrier protein] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
Other name(s): stearyl acyl carrier protein desaturase; stearyl-ACP desaturase; acyl-[acyl-carrier-protein] desaturase; acyl-[acyl-carrier protein],hydrogen-donor:oxygen oxidoreductase
Systematic name: stearoyl-[acyl-carrier protein],reduced ferredoxin:oxygen oxidoreductase (9,10 cis-dehydrogenating)
Comments: The enzyme is found in the lumen of plastids, where de novo biosynthesis of fatty acids occurs, and acts on freshly synthesized saturated fatty acids that are still linked to acyl-carrier protein. The enzyme determines the position of the double bond by its distance from the carboxylic acid end of the fatty acid. It also acts on palmitoyl-[acyl-carrier-protein] [4,5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-86-3
References:
1.  Jaworski, J.G. and Stumpf, P.K. Fat metabolism in higher plants. Properties of a soluble stearyl-acyl carrier protein desaturase from maturing Carthamus tinctorius. Arch. Biochem. Biophys. 162 (1974) 158–165. [DOI] [PMID: 4831331]
2.  Nagai, J. and Bloch, K. Enzymatic desaturation of stearyl acyl carrier protein. J. Biol. Chem. 243 (1968) 4626–4633. [PMID: 4300868]
3.  Shanklin, J. and Somerville, C. Stearoyl-acyl-carrier-protein desaturase from higher plants is structurally unrelated to the animal and fungal homologs. Proc. Natl. Acad. Sci. USA 88 (1991) 2510–2514. [DOI] [PMID: 2006187]
4.  Cahoon, E.B., Lindqvist, Y., Schneider, G. and Shanklin, J. Redesign of soluble fatty acid desaturases from plants for altered substrate specificity and double bond position. Proc. Natl. Acad. Sci. USA 94 (1997) 4872–4877. [DOI] [PMID: 9144157]
5.  Cao, Y., Xian, M., Yang, J., Xu, X., Liu, W. and Li, L. Heterologous expression of stearoyl-acyl carrier protein desaturase (S-ACP-DES) from Arabidopsis thaliana in Escherichia coli. Protein Expr. Purif. 69 (2010) 209–214. [DOI] [PMID: 19716420]
[EC 1.14.19.2 created 1972 as EC 1.14.99.6, modified 2000, transferred 2000 to EC 1.14.19.2, modified 2015]
 
 
EC 1.14.19.17     
Accepted name: sphingolipid 4-desaturase
Reaction: a dihydroceramide + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4E)-sphing-4-enine ceramide + 2 ferricytochrome b5 + 2 H2O
Glossary: a dihydroceramide = an N-acylsphinganine
Other name(s): dehydroceramide desaturase
Systematic name: dihydroceramide,ferrocytochrome b5:oxygen oxidoreductase (4,5-dehydrogenating)
Comments: The enzyme, which has been characterized from plants, fungi, and mammals, generates a trans double bond at position 4 of sphinganine bases in sphingolipids [1]. The preferred substrate is dihydroceramide, but the enzyme is also active with dihydroglucosylceramide [2]. Unlike EC 1.14.19.29, sphingolipid 8-desaturase, this enzyme does not contain an integral cytochrome b5 domain [4] and requires an external cytochrome b5 [3]. The product serves as an important signalling molecules in mammals and is required for spermatide differentiation [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Stoffel, W., Assmann, G. and Bister, K. Metabolism of sphingosine bases. XVII. Stereospecificities in the introduction of the 4t-double bond into sphinganine yielding 4t-sphingenine (sphingosine). Hoppe-Seylers Z. Physiol. Chem. 352 (1971) 1531–1544. [PMID: 5140816]
2.  Michel, C., van Echten-Deckert, G., Rother, J., Sandhoff, K., Wang, E. and Merrill, A.H., Jr. Characterization of ceramide synthesis. A dihydroceramide desaturase introduces the 4,5-trans-double bond of sphingosine at the level of dihydroceramide. J. Biol. Chem. 272 (1997) 22432–22437. [DOI] [PMID: 9312549]
3.  Causeret, C., Geeraert, L., Van der Hoeven, G., Mannaerts, G.P. and Van Veldhoven, P.P. Further characterization of rat dihydroceramide desaturase: tissue distribution, subcellular localization, and substrate specificity. Lipids 35 (2000) 1117–1125. [DOI] [PMID: 11104018]
4.  Ternes, P., Franke, S., Zähringer, U., Sperling, P. and Heinz, E. Identification and characterization of a sphingolipid Δ4-desaturase family. J. Biol. Chem. 277 (2002) 25512–25518. [DOI] [PMID: 11937514]
5.  Michaelson, L.V., Zäuner, S., Markham, J.E., Haslam, R.P., Desikan, R., Mugford, S., Albrecht, S., Warnecke, D., Sperling, P., Heinz, E. and Napier, J.A. Functional characterization of a higher plant sphingolipid Δ4-desaturase: defining the role of sphingosine and sphingosine-1-phosphate in Arabidopsis. Plant Physiol. 149 (2009) 487–498. [DOI] [PMID: 18978071]
[EC 1.14.19.17 created 2015]
 
 
EC 1.14.19.22     
Accepted name: acyl-lipid ω-6 desaturase (cytochrome b5)
Reaction: an oleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a linoleoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Other name(s): oleate desaturase (ambiguous); linoleate synthase (ambiguous); oleoyl-CoA desaturase (incorrect); oleoylphosphatidylcholine desaturase (ambiguous); phosphatidylcholine desaturase (ambiguous); n-6 desaturase (ambiguous); FAD2 (gene name)
Systematic name: 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine,ferrocytochrome-b5:oxygen oxidoreductase (12,13 cis-dehydrogenating)
Comments: This microsomal enzyme introduces a cis double bond in fatty acids attached to lipid molecules at a location 6 carbons away from the methyl end of the fatty acid. The distance from the carboxylic acid end of the molecule does not affect the location of the new double bond. The most common substrates are oleoyl groups attached to either the sn-1 or sn-2 position of the glycerol backbone in phosphatidylcholine. cf. EC 1.14.19.23, acyl-lipid ω-6 desaturase (ferredoxin).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 72536-70-0
References:
1.  Pugh, E.L. and Kates, M. Characterization of a membrane-bound phospholipid desaturase system of Candida lipolytica. Biochim. Biophys. Acta 380 (1975) 442–453. [DOI] [PMID: 166662]
2.  Slack, C.R., Roughan, P.G. and Browse, J. Evidence for an oleoyl phosphatidylcholine desaturase in microsomal preparations from cotyledons of safflower (Carthamus tinctorius) seed. Biochem. J. 179 (1979) 649–656. [PMID: 475773]
3.  Stymne, S. and Appelqvist, L.-A. The biosynthesis of linoleate from oleoyl-CoA via oleoyl-phosphatidylcholine in microsomes of developing safflower seeds. Eur. J. Biochem. 90 (1978) 223–229. [DOI] [PMID: 710426]
4.  Smith, M.A., Cross, A.R., Jones, O.T., Griffiths, W.T., Stymne, S. and Stobart, K. Electron-transport components of the 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine Δ12-desaturase (Δ12-desaturase) in microsomal preparations from developing safflower (Carthamus tinctorius L.) cotyledons. Biochem. J. 272 (1990) 23–29. [PMID: 2264826]
5.  Kearns, E.V., Hugly, S. and Somerville, C.R. The role of cytochrome b5 in Δ12 desaturation of oleic acid by microsomes of safflower (Carthamus tinctorius L.). Arch. Biochem. Biophys. 284 (1991) 431–436. [DOI] [PMID: 1989527]
6.  Miquel, M. and Browse, J. Arabidopsis mutants deficient in polyunsaturated fatty acid synthesis. Biochemical and genetic characterization of a plant oleoyl-phosphatidylcholine desaturase. J. Biol. Chem. 267 (1992) 1502–1509. [PMID: 1730697]
[EC 1.14.19.22 created 1984 as EC 1.3.1.35, transferred 2015 to EC 1.14.19.22]
 
 
EC 1.14.19.23     
Accepted name: acyl-lipid (n+3)-(Z)-desaturase (ferredoxin)
Reaction: an oleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = a linoleoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
Other name(s): acyl-lipid ω6-desaturase (ferredoxin); oleate desaturase (ambiguous); linoleate synthase (ambiguous); oleoyl-CoA desaturase (ambiguous); oleoylphosphatidylcholine desaturase (ambiguous); phosphatidylcholine desaturase (ambiguous); FAD6 (gene name)
Systematic name: oleoyl-[glycerolipid],ferredoxin:oxygen oxidoreductase (12,13 cis-dehydrogenating)
Comments: This plastidial enzyme is able to insert a cis double bond in monounsaturated fatty acids incorporated into glycerolipids. The enzyme introduces the new bond at a position 3 carbons away from the existing double bond, towards the methyl end of the fatty acid. The native substrates are oleoyl (18:1 Δ9) and (Z)-hexadec-7-enoyl (16:1 Δ7) groups attached to either position of the glycerol backbone in glycerolipids, resulting in the introduction of the second double bond at positions 12 and 10, respectively This prompted the suggestion that this is an ω6 desaturase. However, when acting on palmitoleoyl groups(16:1 Δ9), the enzyme introduces the second double bond at position 12 (ω4), indicating it is an (n+3) desaturase [3]. cf. EC 1.14.19.34, acyl-lipid (9+3)-(E)-desaturase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Schmidt, H. and Heinz, E. Desaturation of oleoyl groups in envelope membranes from spinach chloroplasts. Proc. Natl. Acad. Sci. USA 87 (1990) 9477–9480. [DOI] [PMID: 11607123]
2.  Schmidt, H. and Heinz, E. Involvement of ferredoxin in desaturation of lipid-bound oleate in chloroplasts. Plant Physiol. 94 (1990) 214–220. [PMID: 16667689]
3.  Hitz, W.D., Carlson, T.J., Booth, J.R., Jr., Kinney, A.J., Stecca, K.L. and Yadav, N.S. Cloning of a higher-plant plastid ω-6 fatty acid desaturase cDNA and its expression in a cyanobacterium. Plant Physiol. 105 (1994) 635–641. [PMID: 8066133]
4.  Falcone, D.L., Gibson, S., Lemieux, B. and Somerville, C. Identification of a gene that complements an Arabidopsis mutant deficient in chloroplast ω 6 desaturase activity. Plant Physiol. 106 (1994) 1453–1459. [PMID: 7846158]
5.  Schmidt, H., Dresselhaus, T., Buck, F. and Heinz, E. Purification and PCR-based cDNA cloning of a plastidial n-6 desaturase. Plant Mol. Biol. 26 (1994) 631–642. [PMID: 7948918]
[EC 1.14.19.23 created 2015]
 
 
EC 1.14.19.25     
Accepted name: acyl-lipid ω-3 desaturase (cytochrome b5)
Reaction: a linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = an α-linolenoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
Glossary: linoleoyl-[glycerolipid] = (9Z,12Z)-octadeca-9,12-dienoyl-[glycerolipid]
α-linolenoyl-[glycerolipid] = (9Z,12Z,15Z)-octadeca-9,12,15-trienoyl-[glycerolipid]
Other name(s): FAD3
Systematic name: (9Z,12Z)-octadeca-9,12-dienoyl-[glycerolipid],ferrocytochrome b5:oxygen oxidoreductase (15,16 cis-dehydrogenating)
Comments: This microsomal enzyme introduces a cis double bond three carbons away from the methyl end of a fatty acid incorporated into a glycerolipid. The distance from the carboxylic acid end of the molecule does not have an effect. The plant enzyme acts on carbon 15 of linoleoyl groups incorporated into both the sn-1 and sn-2 positions of the glycerol backbone of phosphatidylcholine and other phospholipids, converting them into α-linolenoyl groups. The enzyme from the fungus Mortierella alpina acts on γ-linolenoyl and arachidonoyl groups, converting them into stearidonoyl and icosapentaenoyl groups, respectively [3]. cf. EC 1.14.19.35, sn-2 acyl-lipid ω-3 desaturase (ferredoxin).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Browse, J., McConn, M., James, D., Jr. and Miquel, M. Mutants of Arabidopsis deficient in the synthesis of α-linolenate. Biochemical and genetic characterization of the endoplasmic reticulum linoleoyl desaturase. J. Biol. Chem. 268 (1993) 16345–16351. [PMID: 8102138]
2.  Arondel, V., Lemieux, B., Hwang, I., Gibson, S., Goodman, H.M. and Somerville, C.R. Map-based cloning of a gene controlling ω-3 fatty acid desaturation in Arabidopsis. Science 258 (1992) 1353–1355. [DOI] [PMID: 1455229]
3.  Sakuradani, E., Abe, T., Iguchi, K. and Shimizu, S. A novel fungal ω3-desaturase with wide substrate specificity from arachidonic acid-producing Mortierella alpina 1S-4. Appl. Microbiol. Biotechnol. 66 (2005) 648–654. [DOI] [PMID: 15538555]
[EC 1.14.19.25 created 2015]
 
 
EC 1.14.19.29     
Accepted name: sphingolipid 8-(E/Z)-desaturase
Reaction: (1) a (4R)-4-hydroxysphinganine ceramide + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4R,8E)-4-hydroxysphing-8-enine ceramide + 2 ferricytochrome b5 + 2 H2O
(2) a (4R)-4-hydroxysphinganine ceramide + 2 ferrocytochrome b5 + O2 + 2 H+ = a (4R,8Z)-4-hydroxysphing-8-enine ceramide + 2 ferricytochrome b5 + 2 H2O
Glossary: a (4R)-4-hydroxysphinganine-ceramide = a phytoceramide
(4R)-4-hydroxysphinganine = phytosphinganine
Other name(s): 8-sphingolipid desaturase (ambiguous); 8 fatty acid desaturase (ambiguous); DELTA8-sphingolipid desaturase (ambiguous)
Systematic name: (4R)-4-hydroxysphinganine ceramide,ferrocytochrome b5:oxygen oxidoreductase (8,9 cis/trans-dehydrogenating)
Comments: The enzymes from higher plants convert sphinganine, 4E-sphing-4-enine and phytosphinganine into E/Z-mixtures of Δ8-desaturated products displaying different proportions of geometrical isomers depending on plant species. The nature of the actual desaturase substrate has not yet been studied experimentally. The enzymes contain an N-terminal cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase [1]. The homologous enzymes from some yeasts and diatoms, EC 1.14.19.18, sphingolipid 8-(E)-desaturase, act on sphing-4-enine ceramides and produce only the trans isomer.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sperling, P., Zähringer, U. and Heinz, E. A sphingolipid desaturase from higher plants. Identification of a new cytochrome b5 fusion protein. J. Biol. Chem. 273 (1998) 28590–28596. [DOI] [PMID: 9786850]
2.  Sperling, P., Blume, A., Zähringer, U., and Heinz, E. Further characterization of Δ8-sphingolipid desaturases from higher plants. Biochem Soc Trans. 28 (2000) 638–641. [PMID: 11171153]
3.  Sperling, P., Libisch, B., Zähringer, U., Napier, J.A. and Heinz, E. Functional identification of a Δ8-sphingolipid desaturase from Borago officinalis. Arch. Biochem. Biophys. 388 (2001) 293–298. [DOI] [PMID: 11368168]
4.  Beckmann, C., Rattke, J., Oldham, N.J., Sperling, P., Heinz, E. and Boland, W. Characterization of a Δ8-sphingolipid desaturase from higher plants: a stereochemical and mechanistic study on the origin of E,Z isomers. Angew. Chem. Int. Ed. Engl. 41 (2002) 2298–2300. [DOI] [PMID: 12203571]
5.  Ryan, P.R., Liu, Q., Sperling, P., Dong, B., Franke, S. and Delhaize, E. A higher plant Δ8 sphingolipid desaturase with a preference for (Z)-isomer formation confers aluminum tolerance to yeast and plants. Plant Physiol. 144 (2007) 1968–1977. [DOI] [PMID: 17600137]
6.  Chen, M., Markham, J.E. and Cahoon, E.B. Sphingolipid Δ8 unsaturation is important for glucosylceramide biosynthesis and low-temperature performance in Arabidopsis. Plant J. 69 (2012) 769–781. [DOI] [PMID: 22023480]
[EC 1.14.19.29 created 2015]
 
 
EC 1.14.19.35     
Accepted name: sn-2 acyl-lipid ω-3 desaturase (ferredoxin)
Reaction: (1) a (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = a (7Z,10Z,13Z)-hexadeca-7,10,13-trienoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
(2) a linoleoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = an α-linolenoyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
Glossary: (9Z,12Z)-octadeca-9,12-dienoyl-[glycerolipid] = linoleoyl-[glycerolipid]
(9Z,12Z,15Z)-octadeca-9,12,15-trienoyl-[glycerolipid] = α-linolenoyl-[glycerolipid]
Other name(s): FAD7; FAD8
Systematic name: (7Z,10Z)-hexadeca-7,10-dienoyl-[glycerolipid],ferredoxin:oxygen oxidoreductase (13,14 cis-dehydrogenating)
Comments: This plastidial enzyme desaturates 16:2 fatty acids attached to the sn-2 position of glycerolipids to 16:3 fatty acids, and converts18:2 to 18:3 in both the sn-1 and sn-2 positions. It acts on all 16:2- or 18:2-containing chloroplast membrane lipids, including phosphatidylglycerol, monogalactosyldiacylglycerol, digalactosyldiaclyglycerol, and sulfoquinovosyldiacylglycerol. The enzyme introduces a cis double bond at a location 3 carbons away from the methyl end of the fatty acid. The distance from the carboxylic acid end of the molecule does not affect the location of the new double bond. cf. EC 1.14.19.25, acyl-lipid ω-3 desaturase (cytochrome b5) and EC 1.14.19.36, sn-1 acyl-lipid ω-3 desaturase (ferredoxin).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Iba, K., Gibson, S., Nishiuchi, T., Fuse, T., Nishimura, M., Arondel, V., Hugly, S. and Somerville, C. A gene encoding a chloroplast ω-3 fatty acid desaturase complements alterations in fatty acid desaturation and chloroplast copy number of the fad7 mutant of Arabidopsis thaliana. J. Biol. Chem. 268 (1993) 24099–24105. [PMID: 8226956]
2.  McConn, M., Hugly, S., Browse, J. and Somerville, C. A mutation at the fad8 locus of Arabidopsis identifies a second chloroplast ω-3 desaturase. Plant Physiol. 106 (1994) 1609–1614. [PMID: 12232435]
3.  Venegas-Caleron, M., Muro-Pastor, A.M., Garces, R. and Martinez-Force, E. Functional characterization of a plastidial ω-3 desaturase from sunflower (Helianthus annuus) in cyanobacteria. Plant Physiol. Biochem. 44 (2006) 517–525. [DOI] [PMID: 17064923]
[EC 1.14.19.35 created 2015]
 
 
EC 1.14.19.37     
Accepted name: acyl-CoA 5-desaturase
Reaction: (1) (11Z,14Z)-icosa-11,14-dienoyl-CoA + reduced acceptor + O2 = (5Z,11Z,14Z)-icosa-5,11,14-trienoyl-CoA + acceptor + 2 H2O
(2) (11Z,14Z,17Z)-icosa-11,14,17-trienoyl-CoA + reduced acceptor + O2 = (5Z,11Z,14Z,17Z)-icosa-5,11,14,17-tetraenoyl-CoA + acceptor + 2 H2O
Glossary: (5Z,11Z,14Z)-icosa-5,11,14-trienoate = sciadonate
(5Z,11Z,14Z,17Z)-icosa-5,11,14,17-tetraenoate = juniperonate
Other name(s): acyl-CoA 5-desaturase (non-methylene-interrupted)
Systematic name: acyl-CoA,acceptor:oxygen oxidoreductase (5,6 cis-dehydrogenating)
Comments: The enzyme, characterized from the plant Anemone leveillei, introduces a cis double bond at carbon 5 of acyl-CoAs that do not contain a double bond at position 8. In vivo it forms non-methylene-interrupted polyunsaturated fatty acids such as sciadonate and juniperonate. When expressed in Arabidopsis thaliana the enzyme could also act on unsaturated substrates such as palmitoyl-CoA. cf. EC 1.14.19.44, acyl-CoA (8-3)-desaturase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sayanova, O., Haslam, R., Venegas Caleron, M. and Napier, J.A. Cloning and characterization of unusual fatty acid desaturases from Anemone leveillei: identification of an acyl-coenzyme A C20 Δ5-desaturase responsible for the synthesis of sciadonic acid. Plant Physiol. 144 (2007) 455–467. [DOI] [PMID: 17384161]
[EC 1.14.19.37 created 2015]
 
 
EC 1.14.19.41     
Accepted name: sterol 22-desaturase
Reaction: ergosta-5,7,24(28)-trien-3β-ol + NADPH + H+ + O2 = ergosta-5,7,22,24(28)-tetraen-3β-ol + NADP+ + 2 H2O
For diagram of sterol sidechain modification, click here
Other name(s): ERG5 (gene name); CYP710A (gene name)
Systematic name: ergosta-5,7,24(28)-trien-3β-ol,NADPH:oxygen oxidoreductase (22,23-dehydrogenating)
Comments: A heme-thiolate protein (P-450). The enzyme, found in yeast and plants, catalyses the introduction of a double bond between the C-22 and C-23 carbons of certain sterols. In yeast the enzyme acts on ergosta-5,7,24(28)-trien-3β-ol, a step in the biosynthesis of ergosterol. The enzyme from the plant Arabidopsis thaliana acts on sitosterol and 24-epi-campesterol, producing stigmasterol and brassicasterol, respectively.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kelly, S.L., Lamb, D.C., Corran, A.J., Baldwin, B.C., Parks, L.W. and Kelly, D.E. Purification and reconstitution of activity of Saccharomyces cerevisiae P450 61, a sterol Δ22-desaturase. FEBS Lett. 377 (1995) 217–220. [DOI] [PMID: 8543054]
2.  Skaggs, B.A., Alexander, J.F., Pierson, C.A., Schweitzer, K.S., Chun, K.T., Koegel, C., Barbuch, R. and Bard, M. Cloning and characterization of the Saccharomyces cerevisiae C-22 sterol desaturase gene, encoding a second cytochrome P-450 involved in ergosterol biosynthesis. Gene 169 (1996) 105–109. [DOI] [PMID: 8635732]
3.  Morikawa, T., Mizutani, M., Aoki, N., Watanabe, B., Saga, H., Saito, S., Oikawa, A., Suzuki, H., Sakurai, N., Shibata, D., Wadano, A., Sakata, K. and Ohta, D. Cytochrome P450 CYP710A encodes the sterol C-22 desaturase in Arabidopsis and tomato. Plant Cell 18 (2006) 1008–1022. [DOI] [PMID: 16531502]
[EC 1.14.19.41 created 2015]
 
 
EC 1.14.19.42     
Accepted name: palmitoyl-[glycerolipid] 7-desaturase
Reaction: a 1-acyl-2-palmitoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = a 1-acyl-2-[(7Z)-hexadec-7-enoyl]-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
Other name(s): FAD5
Systematic name: 1-acyl-2-palmitoyl-[glycerolipid],ferredoxin:oxygen oxidoreductase (7,8-cis-dehydrogenating)
Comments: The enzyme introduces a cis double bond at carbon 7 of a palmitoyl group attached to the sn-2 position of glycerolipids. The enzyme from the plant Arabidopsis thaliana is specific for palmitate in monogalactosyldiacylglycerol.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kunst, L., Browse, J., Somerville, C.R. A mutant of Arabidopsis deficient in desaturation of palmitic acid in leaf lipids. Plant Physiol. 90 (1989) 943–947. [PMID: 16666902]
2.  Heilmann, I., Mekhedov, S., King, B., Browse, J. and Shanklin, J. Identification of the Arabidopsis palmitoyl-monogalactosyldiacylglycerol Δ7-desaturase gene FAD5, and effects of plastidial retargeting of Arabidopsis desaturases on the fad5 mutant phenotype. Plant Physiol. 136 (2004) 4237–4245. [DOI] [PMID: 15579662]
[EC 1.14.19.42 created 2015]
 
 
EC 1.14.19.43     
Accepted name: palmitoyl-[glycerolipid] 3-(E)-desaturase
Reaction: a 1-acyl-2-palmitoyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ = a 1-acyl-2-[(3E)-hexadec-3-enoyl]-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
Other name(s): FAD4
Systematic name: 1-acyl-2-palmitoyl-[glycerolipid],ferredoxin:oxygen oxidoreductase (3,4-trans -dehydrogenating)
Comments: The enzyme introduces an unusual trans double bond at carbon 3 of a palmitoyl group attached to the sn-2 position of glycerolipids. The enzyme from the plant Arabidopsis thaliana is specific for palmitate in phosphatidylglycerol. The enzyme from tobacco can also accept oleate and α-linolenate if present at the sn-2 position of phosphatidylglycerol [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Fritz, M., Lokstein, H., Hackenberg, D., Welti, R., Roth, M., Zähringer, U., Fulda, M., Hellmeyer, W., Ott, C., Wolter, F.P. and Heinz, E. Channeling of eukaryotic diacylglycerol into the biosynthesis of plastidial phosphatidylglycerol. J. Biol. Chem. 282 (2007) 4613–4625. [DOI] [PMID: 17158889]
2.  Gao, J., Ajjawi, I., Manoli, A., Sawin, A., Xu, C., Froehlich, J.E., Last, R.L. and Benning, C. FATTY ACID DESATURASE4 of Arabidopsis encodes a protein distinct from characterized fatty acid desaturases. Plant J. 60 (2009) 832–839. [DOI] [PMID: 19682287]
[EC 1.14.19.43 created 2015]
 
 
EC 1.14.19.52     
Accepted name: camalexin synthase
Reaction: 2-(L-cystein-S-yl)-2-(1H-indol-3-yl)acetonitrile + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = camalexin + hydrogen cyanide + CO2 + 2 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction)
(1a) 2-(L-cystein-S-yl)-2-(1H-indol-3-yl)acetonitrile + [reduced NADPH—hemoprotein reductase] + O2 = (R)-dihydrocamalexate + hydrogen cyanide + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(1b) (R)-dihydrocamalexate + [reduced NADPH—hemoprotein reductase] + O2 = camalexin + CO2 + [oxidized NADPH—hemoprotein reductase] + 2 H2O
Glossary: camalexin = 3-(thiazol-2-yl)indole
(R)-dihydrocamalexate = (4R)-2-(1H-indol-3-yl)-4,5-dihydrothiazole-4-carboxylate
Other name(s): CYP71B15 (gene name); bifunctional dihydrocamalexate synthase/camalexin synthase
Systematic name: 2-(cystein-S-yl)-2-(1H-indol-3-yl)-acetonitrile, [reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (camalexin-forming)
Comments: This cytochrome P-450 (heme thiolate) enzyme, which has been characterized from the plant Arabidopsis thaliana, catalyses the last two steps in the biosynthesis of camalexin, the main phytoalexin in that plant. The enzyme catalyses two successive oxidation events. During the first oxidation the enzyme introduces a C-N double bond, liberating hydrogen cyanide, and during the second oxidation it catalyses a decarboxylation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Schuhegger, R., Nafisi, M., Mansourova, M., Petersen, B.L., Olsen, C.E., Svatos, A., Halkier, B.A. and Glawischnig, E. CYP71B15 (PAD3) catalyzes the final step in camalexin biosynthesis. Plant Physiol. 141 (2006) 1248–1254. [DOI] [PMID: 16766671]
2.  Böttcher, C., Westphal, L., Schmotz, C., Prade, E., Scheel, D. and Glawischnig, E. The multifunctional enzyme CYP71B15 (PHYTOALEXIN DEFICIENT3) converts cysteine-indole-3-acetonitrile to camalexin in the indole-3-acetonitrile metabolic network of Arabidopsis thaliana. Plant Cell 21 (2009) 1830–1845. [DOI] [PMID: 19567706]
[EC 1.14.19.52 created 2017]
 
 
EC 1.14.19.75     
Accepted name: very-long-chain acyl-lipid ω-9 desaturase
Reaction: (1) 1-hexacosanoyl-2-acyl-[phosphoglycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = 1-[(17Z)-hexacos-17-enoyl]-2-acyl-[phosphoglycerolipid] + 2 ferricytochrome b5 + 2 H2O
(2) 1-tetracosanoyl-2-acyl-[phosphoglycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = 1-[(15Z)-tetracos-15-enoyl]-2-acyl-[phosphoglycerolipid] + 2 ferricytochrome b5 + 2 H2O
Other name(s): ADS2 (gene name)
Systematic name: very-long-chain acyl-[glycerolipid],ferrocytochrome b5:oxygen oxidoreductase (ω98-cis-dehydrogenating)
Comments: The enzyme, characterized from the plant Arabidopsis thaliana, acts on both 24:0 and 26:0 fatty acids, introducing a cis double bond at a position 9 carbons from the methyl end. These very-long-chain fatty acids are found as a minor component of seed lipids, but also in the membrane phosphatidylethanolamine and phosphatidylserine, in sphingolipids, as precursors and components of cuticular and epicuticular waxes, and in suberin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Fukuchi-Mizutani, M., Tasaka, Y., Tanaka, Y., Ashikari, T., Kusumi, T. and Murata, N. Characterization of δA9 acyl-lipid desaturase homologues from Arabidopsis thaliana. Plant Cell Physiol. 39 (1998) 247–253. [PMID: 9559566]
2.  Smith, M.A., Dauk, M., Ramadan, H., Yang, H., Seamons, L.E., Haslam, R.P., Beaudoin, F., Ramirez-Erosa, I. and Forseille, L. Involvement of Arabidopsis acyl-coenzyme A desaturase-like2 (At2g31360) in the biosynthesis of the very-long-chain monounsaturated fatty acid components of membrane lipids. Plant Physiol. 161 (2013) 81–96. [PMID: 23175755]
[EC 1.14.19.75 created 2018]
 
 
EC 1.14.19.79     
Accepted name: 3β,22α-dihydroxysteroid 3-dehydrogenase
Reaction: (1) (22S)-22-hydroxycampesterol + [reduced NADPH-hemoprotein reductase] + O2 = (22S)-22-hydroxycampest-4-en-3-one + [oxidized NADPH-hemoprotein reductase] + 2 H2O
(2) 6-deoxoteasterone + [reduced NADPH-hemoprotein reductase] + O2 = 3-dehydro-6-deoxoteasterone + [oxidized NADPH-hemoprotein reductase] + 2 H2O
Glossary: 6-deoxoteasterone = (22R,23R)-5α-campestane-3β,22,23-triol
Other name(s): CYP90A1 (gene name)
Systematic name: 3β,22α-dihydroxysteroid,[reduced NADPH-hemoprotein reductase]:oxygen 3-oxidoreductase
Comments: This cytochrome P-450 (heme-thiolate) enzyme, characterized from the plant Arabidopsis thaliana, catalyses C-3 dehydrogenation of all 3β-hydroxy brassinosteroid synthesis intermediates with 22-hydroxylated or 22,23-dihydroxylated side chains.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ohnishi, T., Godza, B., Watanabe, B., Fujioka, S., Hategan, L., Ide, K., Shibata, K., Yokota, T., Szekeres, M. and Mizutani, M. CYP90A1/CPD, a brassinosteroid biosynthetic cytochrome P450 of Arabidopsis, catalyzes C-3 oxidation. J. Biol. Chem. 287 (2012) 31551–31560. [DOI] [PMID: 22822057]
[EC 1.14.19.79 created 2022]
 
 
EC 1.14.20.4     
Accepted name: anthocyanidin synthase
Reaction: a (2R,3S,4S)-leucoanthocyanidin + 2-oxoglutarate + O2 = an anthocyanidin + succinate + CO2 + 2 H2O (overall reaction)
(1a) a (2R,3S,4S)-leucoanthocyanidin + 2-oxoglutarate + O2 = a (4S)- 2,3-dehydroflavan-3,4-diol + succinate + CO2 + H2O
(1b) a (4S)- 2,3-dehydroflavan-3,4-diol = an anthocyanidin + H2O
For diagram of anthocyanin biosynthesis, click here
Glossary: taxifolin = 3,4-dihydroquercitin
Other name(s): leucocyanidin oxygenase; leucocyanidin,2-oxoglutarate:oxygen oxidoreductase; ANS (gene name)
Systematic name: (2R,3S,4S)-leucoanthocyanidin,2-oxoglutarate:oxygen oxidoreductase
Comments: The enzyme requires iron(II) and ascorbate. It is involved in the pathway by which many flowering plants make anthocyanin flower pigments (glycosylated anthocyandins). The enzyme hydroxylates the C-3 carbon, followed by a trans diaxial elimination, forming a C-2,C-3 enol. The product loses a second water molecule to form anthocyanidins. When assayed in vitro, non-enzymic epimerization of the product can lead to formation of dihydroflavanols. Thus when the substrate is leucocyanidin, a mixture of (+)-taxifolin and (+)-epitaxifolin are formed. The enzyme can also oxidize the formed (+)-taxifolin to quercetin (cf. EC 1.14.20.6, flavonol synthase) [2,3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 180984-01-4
References:
1.  Saito, K., Kobayashi, M., Gong, Z., Tanaka, Y. and Yamazaki, M. Direct evidence for anthocyanidin synthase as a 2-oxoglutarate-dependent oxygenase: molecular cloning and functional expression of cDNA from a red forma of Perilla frutescens. Plant J. 17 (1999) 181–190. [DOI] [PMID: 10074715]
2.  Turnbull, J.J., Sobey, W.J., Aplin, R.T., Hassan, A., Firmin, J.L., Schofield, C.J. and Prescott, A.G. Are anthocyanidins the immediate products of anthocyanidin synthase? Chem. Commun. (2000) 2473–2474.
3.  Wilmouth, R.C., Turnbull, J.J., Welford, R.W., Clifton, I.J., Prescott, A.G. and Schofield, C.J. Structure and mechanism of anthocyanidin synthase from Arabidopsis thaliana. Structure 10 (2002) 93–103. [DOI] [PMID: 11796114]
4.  Turnbull, J.J., Nagle, M.J., Seibel, J.F., Welford, R.W., Grant, G.H. and Schofield, C.J. The C-4 stereochemistry of leucocyanidin substrates for anthocyanidin synthase affects product selectivity. Bioorg. Med. Chem. Lett. 13 (2003) 3853–3857. [DOI] [PMID: 14552794]
5.  Wellmann, F., Griesser, M., Schwab, W., Martens, S., Eisenreich, W., Matern, U. and Lukacin, R. Anthocyanidin synthase from Gerbera hybrida catalyzes the conversion of (+)-catechin to cyanidin and a novel procyanidin. FEBS Lett. 580 (2006) 1642–1648. [DOI] [PMID: 16494872]
[EC 1.14.20.4 created 2001 as EC 1.14.11.19, transferred 2018 to EC 1.14.20.4]
 
 
EC 1.14.99.45      
Transferred entry: carotene &epsilon;-monooxygenase. Now EC 1.14.14.158, carotene &epsilon;-monooxygenase
[EC 1.14.99.45 created 2011, deleted 2018]
 
 
EC 1.14.99.54     
Accepted name: lytic cellulose monooxygenase (C1-hydroxylating)
Reaction: [(1→4)-β-D-glucosyl]n+m + reduced acceptor + O2 = [(1→4)-β-D-glucosyl]m-1-(1→4)-D-glucono-1,5-lactone + [(1→4)-β-D-glucosyl]n + acceptor + H2O
Other name(s): lytic polysaccharide monooxygenase (ambiguous); LPMO (ambiguous); LPMO9A
Systematic name: cellulose, hydrogen-donor:oxygen oxidoreductase (D-glucosyl C1-hydroxylating)
Comments: This copper-containing enzyme, found in fungi and bacteria, cleaves cellulose in an oxidative manner. The cellulose fragments that are formed contain a D-glucono-1,5-lactone residue at the reducing end, which hydrolyses quickly and spontaneously to the aldonic acid. The electrons are provided in vivo by the cytochrome b domain of EC 1.1.99.18, cellobiose dehydrogenase (acceptor) [1]. Ascorbate can serve as the electron donor in vitro.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Phillips, C.M., Beeson, W.T., Cate, J.H. and Marletta, M.A. Cellobiose dehydrogenase and a copper-dependent polysaccharide monooxygenase potentiate cellulose degradation by Neurospora crassa. ACS Chem. Biol. 6 (2011) 1399–1406. [DOI] [PMID: 22004347]
2.  Beeson, W.T., Phillips, C.M., Cate, J.H. and Marletta, M.A. Oxidative cleavage of cellulose by fungal copper-dependent polysaccharide monooxygenases. J. Am. Chem. Soc. 134 (2012) 890–892. [DOI] [PMID: 22188218]
3.  Li, X., Beeson, W.T., 4th, Phillips, C.M., Marletta, M.A. and Cate, J.H. Structural basis for substrate targeting and catalysis by fungal polysaccharide monooxygenases. Structure 20 (2012) 1051–1061. [DOI] [PMID: 22578542]
4.  Bey, M., Zhou, S., Poidevin, L., Henrissat, B., Coutinho, P.M., Berrin, J.G. and Sigoillot, J.C. Cello-oligosaccharide oxidation reveals differences between two lytic polysaccharide monooxygenases (family GH61) from Podospora anserina. Appl. Environ. Microbiol. 79 (2013) 488–496. [DOI] [PMID: 23124232]
5.  Frommhagen, M., Sforza, S., Westphal, A.H., Visser, J., Hinz, S.W., Koetsier, M.J., van Berkel, W.J., Gruppen, H. and Kabel, M.A. Discovery of the combined oxidative cleavage of plant xylan and cellulose by a new fungal polysaccharide monooxygenase. Biotechnol. Biofuels 8:101 (2015). [DOI] [PMID: 26185526]
6.  Patel, I., Kracher, D., Ma, S., Garajova, S., Haon, M., Faulds, C.B., Berrin, J.G., Ludwig, R. and Record, E. Salt-responsive lytic polysaccharide monooxygenases from the mangrove fungus Pestalotiopsis sp. NCi6. Biotechnol Biofuels 9:108 (2016). [DOI] [PMID: 27213015]
7.  Courtade, G., Wimmer, R., Rohr, A.K., Preims, M., Felice, A.K., Dimarogona, M., Vaaje-Kolstad, G., Sorlie, M., Sandgren, M., Ludwig, R., Eijsink, V.G. and Aachmann, F.L. Interactions of a fungal lytic polysaccharide monooxygenase with β-glucan substrates and cellobiose dehydrogenase. Proc. Natl. Acad. Sci. USA 113 (2016) 5922–5927. [DOI] [PMID: 27152023]
[EC 1.14.99.54 created 2017]
 
 
EC 1.14.99.56     
Accepted name: lytic cellulose monooxygenase (C4-dehydrogenating)
Reaction: [(1→4)-β-D-glucosyl]n+m + reduced acceptor + O2 = 4-dehydro-β-D-glucosyl-[(1→4)-β-D-glucosyl]n-1 + [(1→4)-β-D-glucosyl]m + acceptor + H2O
Systematic name: cellulose, hydrogen-donor:oxygen oxidoreductase (D-glucosyl 4-dehydrogenating)
Comments: This copper-containing enzyme, found in fungi and bacteria, cleaves cellulose in an oxidative manner. The cellulose fragments that are formed contain a 4-dehydro-D-glucose residue at the non-reducing end. Some enzymes also oxidize cellulose at the C-1 position of the reducing end forming a D-glucono-1,5-lactone residue [cf. EC 1.14.99.54, lytic cellulose monooxygenase (C1-hydroxylating)].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Beeson, W.T., Phillips, C.M., Cate, J.H. and Marletta, M.A. Oxidative cleavage of cellulose by fungal copper-dependent polysaccharide monooxygenases. J. Am. Chem. Soc. 134 (2012) 890–892. [DOI] [PMID: 22188218]
2.  Li, X., Beeson, W.T., 4th, Phillips, C.M., Marletta, M.A. and Cate, J.H. Structural basis for substrate targeting and catalysis by fungal polysaccharide monooxygenases. Structure 20 (2012) 1051–1061. [DOI] [PMID: 22578542]
3.  Forsberg, Z., Mackenzie, A.K., Sorlie, M., Rohr, A.K., Helland, R., Arvai, A.S., Vaaje-Kolstad, G. and Eijsink, V.G. Structural and functional characterization of a conserved pair of bacterial cellulose-oxidizing lytic polysaccharide monooxygenases. Proc. Natl. Acad. Sci. USA 111 (2014) 8446–8451. [DOI] [PMID: 24912171]
4.  Borisova, A.S., Isaksen, T., Dimarogona, M., Kognole, A.A., Mathiesen, G., Varnai, A., Rohr, A.K., Payne, C.M., Sorlie, M., Sandgren, M. and Eijsink, V.G. Structural and functional characterization of a lytic polysaccharide monooxygenase with broad substrate specificity. J. Biol. Chem. 290 (2015) 22955–22969. [DOI] [PMID: 26178376]
5.  Patel, I., Kracher, D., Ma, S., Garajova, S., Haon, M., Faulds, C.B., Berrin, J.G., Ludwig, R. and Record, E. Salt-responsive lytic polysaccharide monooxygenases from the mangrove fungus Pestalotiopsis sp. NCi6. Biotechnol Biofuels 9:108 (2016). [DOI] [PMID: 27213015]
[EC 1.14.99.56 created 2017]
 
 
EC 1.14.99.59     
Accepted name: tryptamine 4-monooxygenase
Reaction: tryptamine + reduced acceptor + O2 = 4-hydroxytryptamine + acceptor + H2O
For diagram of psilocybin biosynthesis, click here
Glossary: psilocybin = 3-[2-(dimethylamino)ethyl]-1H-indol-4-yl phosphate
Other name(s): PsiH
Systematic name: tryptamine,hydrogen-donor:oxygen oxidoreductase (4-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the fungus Psilocybe cubensis. Involved in the biosynthesis of the psychoactive compound psilocybin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Fricke, J., Blei, F. and Hoffmeister, D. Enzymatic synthesis of psilocybin. Angew. Chem. Int. Ed. Engl. 56 (2017) 12352–12355. [DOI] [PMID: 28763571]
[EC 1.14.99.59 created 2017]
 
 
EC 1.14.99.64     
Accepted name: zeaxanthin 4-ketolase
Reaction: (1) zeaxanthin + 2 reduced acceptor + 2 O2 = adonixanthin + 2 acceptor + 3 H2O
(2) adonixanthin + 2 reduced acceptor + 2 O2 = (3S,3′S)-astaxanthin + 2 acceptor + 3 H2O
Glossary: zeaxanthin = β,β-carotene-3,3′-diol
adonixanthin = 3,3′-dihydroxy-β,β-carotene-4-one
(3S,3′S)-astaxanthin = (3S,3′S)-3,3′-dihydroxy-β,β-carotene-4,4′-dione
Other name(s): BKT (ambiguous); crtW148 (gene name)
Systematic name: zeaxanthin,donor:oxygen oxidoreductase (adonixanthin-forming)
Comments: The enzyme has a similar activity to that of EC 1.14.99.63, β-carotene 4-ketolase, but unlike that enzyme is able to also act on zeaxanthin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Zhong, Y.J., Huang, J.C., Liu, J., Li, Y., Jiang, Y., Xu, Z.F., Sandmann, G. and Chen, F. Functional characterization of various algal carotenoid ketolases reveals that ketolating zeaxanthin efficiently is essential for high production of astaxanthin in transgenic Arabidopsis. J. Exp. Bot. 62 (2011) 3659–3669. [PMID: 21398427]
2.  Huang, J., Zhong, Y., Sandmann, G., Liu, J. and Chen, F. Cloning and selection of carotenoid ketolase genes for the engineering of high-yield astaxanthin in plants. Planta 236 (2012) 691–699. [PMID: 22526507]
[EC 1.14.99.64 created 2018]
 
 
EC 1.16.5.1      
Transferred entry: ascorbate ferrireductase (transmembrane). Now EC 7.2.1.3, ascorbate ferrireductase (transmembrane)
[EC 1.16.5.1 created 2011, deleted 2018]
 
 
EC 1.17.7.1     
Accepted name: (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (ferredoxin)
Reaction: (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + H2O + 2 oxidized ferredoxin = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + 2 reduced ferredoxin
For diagram of Non-Mevalonate terpenoid biosynthesis, click here
Other name(s): 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (ambiguous); (E)-4-hydroxy-3-methylbut-2-en-1-yl-diphosphate:protein-disulfide oxidoreductase (hydrating) (incorrect); (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (ambiguous); gcpE (gene name); ISPG (gene name); (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase
Systematic name: (E)-4-hydroxy-3-methylbut-2-en-1-yl-diphosphate:oxidized ferredoxin oxidoreductase
Comments: An iron-sulfur protein found in plant chloroplasts and cyanobacteria that contains a [4Fe-4S] cluster [1]. Forms part of an alternative non-mevalonate pathway for isoprenoid biosynthesis. Bacteria have a similar enzyme that uses flavodoxin rather than ferredoxin (cf. EC 1.17.7.3). The enzyme from the plant Arabidopsis thaliana is active with photoreduced 5-deazaflavin but not with flavodoxin [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Okada, K. and Hase, T. Cyanobacterial non-mevalonate pathway: (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase interacts with ferredoxin in Thermosynechococcus elongatus BP-1. J. Biol. Chem. 280 (2005) 20672–20679. [DOI] [PMID: 15792953]
2.  Seemann, M., Wegner, P., Schünemann, V., Tse Sum Bui, B., Wolff, M., Marquet, A., Trautwein, A.X. and Rohmer, M. Isoprenoid biosynthesis in chloroplasts via the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (GcpE) from Arabidopsis thaliana is a [4Fe-4S] protein. J. Biol. Inorg. Chem. 10 (2005) 131–137. [DOI] [PMID: 15650872]
3.  Seemann, M., Tse Sum Bui, B., Wolff, M., Tritsch, D., Campos, N., Boronat, A., Marquet, A. and Rohmer, M. Isoprenoid biosynthesis through the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (GcpE) is a [4Fe-4S] protein. Angew. Chem. Int. Ed. Engl. 41 (2002) 4337–4339. [DOI] [PMID: 12434382]
4.  Seemann, M., Tse Sum Bui, B., Wolff, M., Miginiac-Maslow, M. and Rohmer, M. Isoprenoid biosynthesis in plant chloroplasts via the MEP pathway: direct thylakoid/ferredoxin-dependent photoreduction of GcpE/IspG. FEBS Lett. 580 (2006) 1547–1552. [DOI] [PMID: 16480720]
[EC 1.17.7.1 created 2003 as EC 1.17.4.3, transferred 2009 to EC 1.17.7.1, modified 2014]
 
 
EC 1.17.7.2     
Accepted name: 7-hydroxymethyl chlorophyll a reductase
Reaction: chlorophyll a + H2O + 2 oxidized ferredoxin = 71-hydroxychlorophyll a + 2 reduced ferredoxin + 2 H+
For diagram of the chlorophyll cycle, click here
Glossary: 71-hydroxychlorophyll a = 7-hydroxymethyl-chlorophyll a
Other name(s): HCAR; 71-hydroxychlorophyll-a:ferredoxin oxidoreductase
Systematic name: chlorophyll-a:ferredoxin oxidoreductase
Comments: Contains FAD and an iron-sulfur center. This enzyme, which is present in plant chloroplasts, carries out the second step in the conversion of chlorophyll b to chlorophyll a. It similarly reduces chlorophyllide a.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Meguro, M., Ito, H., Takabayashi, A., Tanaka, R. and Tanaka, A. Identification of the 7-hydroxymethyl chlorophyll a reductase of the chlorophyll cycle in Arabidopsis. Plant Cell 23 (2011) 3442–3453. [DOI] [PMID: 21934147]
[EC 1.17.7.2 created 2011]
 
 
EC 1.23.1.3     
Accepted name: (–)-pinoresinol reductase
Reaction: (–)-lariciresinol + NADP+ = (–)-pinoresinol + NADPH + H+
For diagram of (–)-lariciresinol biosynthesis, click here
Glossary: (–)-lariciresinol = 4-[(2R,3S,4S)-4-[(4-hydroxy-3-methoxyphenyl)methyl]-3-(hydroxymethyl)oxolan-2-yl]-2-methoxyphenol
(–)-pinoresinol = (1R,3aS,4R,6aS)-4,4′-(tetrahydro-1H,3H-furo[3,4-c]furan-1,4-diyl)bis(2-methoxyphenol)
Other name(s): pinoresinol/lariciresinol reductase; pinoresinol-lariciresinol reductases; (–)-pinoresinol-(–)-lariciresinol reductase; PLR
Systematic name: (–)-lariciresinol:NADP+ oxidoreductase
Comments: The reaction is catalysed in vivo in the opposite direction to that shown. A multifunctional enzyme that usually further reduces the product to (+)-secoisolariciresinol [EC 1.23.1.4, (–)-lariciresinol reductase]. Isolated from the plants Thuja plicata (western red cedar) [1], Linum perenne (perennial flax) [2] and Arabidopsis thaliana (thale cress) [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Fujita, M., Gang, D.R., Davin, L.B. and Lewis, N.G. Recombinant pinoresinol-lariciresinol reductases from western red cedar (Thuja plicata) catalyze opposite enantiospecific conversions. J. Biol. Chem. 274 (1999) 618–627. [DOI] [PMID: 9872995]
2.  Hemmati, S., Schmidt, T.J. and Fuss, E. (+)-Pinoresinol/(-)-lariciresinol reductase from Linum perenne Himmelszelt involved in the biosynthesis of justicidin B. FEBS Lett. 581 (2007) 603–610. [DOI] [PMID: 17257599]
3.  Nakatsubo, T., Mizutani, M., Suzuki, S., Hattori, T. and Umezawa, T. Characterization of Arabidopsis thaliana pinoresinol reductase, a new type of enzyme involved in lignan biosynthesis. J. Biol. Chem. 283 (2008) 15550–15557. [DOI] [PMID: 18347017]
[EC 1.23.1.3 created 2013]
 
 


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