The Enzyme Database

Displaying entries 51-100 of 565.

<< Previous | Next >>    printer_iconPrintable version



EC 1.10.3.11     
Accepted name: ubiquinol oxidase (non-electrogenic)
Reaction: 2 ubiquinol + O2 = 2 ubiquinone + 2 H2O
Other name(s): plant alternative oxidase; cyanide-insensitive oxidase; AOX (gene name); ubiquinol oxidase; ubiquinol:O2 oxidoreductase (non-electrogenic)
Systematic name: ubiquinol:oxygen oxidoreductase (non-electrogenic)
Comments: The enzyme, described from the mitochondria of plants and some fungi and protists, is an alternative terminal oxidase that is not sensitive to cyanide inhibition and does not generate a proton motive force. Unlike the electrogenic terminal oxidases that contain hemes (cf. EC 1.10.3.10 and EC 1.10.3.14), this enzyme contains a dinuclear non-heme iron complex. The function of this oxidase is believed to be dissipating excess reducing power, minimizing oxidative stress, and optimizing photosynthesis in response to changing conditions.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bendall, D.S. and Bonner, W.D. Cyanide-insensitive respiration in plant mitochondria. Plant Physiol. 47 (1971) 236–245. [PMID: 16657603]
2.  Siedow, J.N., Umbach, A.L. and Moore, A.L. The active site of the cyanide-resistant oxidase from plant mitochondria contains a binuclear iron center. FEBS Lett. 362 (1995) 10–14. [DOI] [PMID: 7698344]
3.  Berthold, D.A., Andersson, M.E. and Nordlund, P. New insight into the structure and function of the alternative oxidase. Biochim. Biophys. Acta 1460 (2000) 241–254. [DOI] [PMID: 11106766]
4.  Williams, B.A., Elliot, C., Burri, L., Kido, Y., Kita, K., Moore, A.L. and Keeling, P.J. A broad distribution of the alternative oxidase in microsporidian parasites. PLoS Pathog. 6:e1000761 (2010). [DOI] [PMID: 20169184]
5.  Gandin, A., Duffes, C., Day, D.A. and Cousins, A.B. The absence of alternative oxidase AOX1A results in altered response of photosynthetic carbon assimilation to increasing CO2 in Arabidopsis thaliana. Plant Cell Physiol. 53 (2012) 1627–1637. [DOI] [PMID: 22848123]
[EC 1.10.3.11 created 2011, modified 2014]
 
 
EC 1.11.2.2     
Accepted name: myeloperoxidase
Reaction: Cl- + H2O2 + H+ = HClO + H2O
Other name(s): MPO; verdoperoxidase
Systematic name: chloride:hydrogen-peroxide oxidoreductase (hypochlorite-forming)
Comments: Contains calcium and covalently bound heme (proximal ligand histidine). It is present in phagosomes of neutrophils and monocytes, where the hypochlorite produced is strongly bactericidal. It differs from EC 1.11.1.10 chloride peroxidase in its preference for formation of hypochlorite over the chlorination of organic substrates under physiological conditions (pH 5-8). Hypochlorite in turn forms a number of antimicrobial products (Cl2, chloramines, hydroxyl radical, singlet oxygen). MPO also oxidizes bromide, iodide and thiocyanate. In the absence of halides, it oxidizes phenols and has a moderate peroxygenase activity toward styrene.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Agner, K. Myeloperoxidase. Adv. Enzymol. 3 (1943) 137–148.
2.  Harrison, J.E. and Schultz, J. Studies on the chlorinating activity of myeloperoxidase. J. Biol. Chem. 251 (1976) 1371–1374. [PMID: 176150]
3.  Furtmuller, P.G., Burner, U. and Obinger, C. Reaction of myeloperoxidase compound I with chloride, bromide, iodide, and thiocyanate. Biochemistry 37 (1998) 17923–17930. [PMID: 9922160]
4.  Tuynman, A., Spelberg, J.L., Kooter, I.M., Schoemaker, H.E. and Wever, R. Enantioselective epoxidation and carbon-carbon bond cleavage catalyzed by Coprinus cinereus peroxidase and myeloperoxidase. J. Biol. Chem. 275 (2000) 3025–3030. [DOI] [PMID: 10652281]
5.  Klebanoff, S.J. Myeloperoxidase: friend and foe. J. Leukoc. Biol. 77 (2005) 598–625. [DOI] [PMID: 15689384]
6.  Fiedler, T.J., Davey, C.A. and Fenna, R.E. X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 Å resolution. J. Biol. Chem. 275 (2000) 11964–11971. [DOI] [PMID: 10766826]
7.  Gaut, J.P., Yeh, G.C., Tran, H.D., Byun, J., Henderson, J.P., Richter, G.M., Brennan, M.L., Lusis, A.J., Belaaouaj, A., Hotchkiss, R.S. and Heinecke, J.W. Neutrophils employ the myeloperoxidase system to generate antimicrobial brominating and chlorinating oxidants during sepsis. Proc. Natl. Acad. Sci. USA 98 (2001) 11961–11966. [DOI] [PMID: 11593004]
[EC 1.11.2.2 created 2011]
 
 
EC 1.13.11.18     
Accepted name: persulfide dioxygenase
Reaction: S-sulfanylglutathione + O2 + H2O = glutathione + sulfite + 2 H+ (overall reaction)
(1a) S-sulfanylglutathione + O2 = S-sulfinatoglutathione + H+
(1b) S-sulfinatoglutathione + H2O = glutathione + sulfite + H+ (spontaneous)
Other name(s): sulfur oxygenase (incorrect); sulfur:oxygen oxidoreductase (incorrect); sulfur dioxygenase (incorrect)
Systematic name: S-sulfanylglutathione:oxygen oxidoreductase
Comments: An iron protein. Perthiols, formed spontaneously by interactions between thiols and elemental sulfur or sulfide, are the only acceptable substrate to the enzyme. The sulfite that is formed by the enzyme can be further converted into sulfate, thiosulfate or S-sulfoglutathione (GSSO3-) non-enzymically [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-58-9
References:
1.  Suzuki, I. and Silver, M. The initial product and properties of the sulfur-oxidizing enzyme of thiobacilli. Biochim. Biophys. Acta 122 (1966) 22–33. [PMID: 5968172]
2.  Rohwerder, T. and Sand, W. The sulfane sulfur of persulfides is the actual substrate of the sulfur-oxidizing enzymes from Acidithiobacillus and Acidiphilium spp. Microbiology 149 (2003) 1699–1710. [DOI] [PMID: 12855721]
3.  Liu, H., Xin, Y. and Xun, L. Distribution, diversity, and activities of sulfur dioxygenases in heterotrophic bacteria. Appl. Environ. Microbiol. 80 (2014) 1799–1806. [DOI] [PMID: 24389926]
4.  Holdorf, M.M., Owen, H.A., Lieber, S.R., Yuan, L., Adams, N., Dabney-Smith, C. and Makaroff, C.A. Arabidopsis ETHE1 encodes a sulfur dioxygenase that is essential for embryo and endosperm development. Plant Physiol. 160 (2012) 226–236. [DOI] [PMID: 22786886]
5.  Pettinati, I., Brem, J., McDonough, M.A. and Schofield, C.J. Crystal structure of human persulfide dioxygenase: structural basis of ethylmalonic encephalopathy. Hum. Mol. Genet. 24 (2015) 2458–2469. [DOI] [PMID: 25596185]
[EC 1.13.11.18 created 1972, modified 2015]
 
 
EC 1.13.11.32      
Transferred entry: 2-nitropropane dioxygenase. Now EC 1.13.12.16, nitronate monooxygenase
[EC 1.13.11.32 created 1984, modified 2006, deleted 2009]
 
 
EC 1.13.11.51     
Accepted name: 9-cis-epoxycarotenoid dioxygenase
Reaction: (1) a 9-cis-epoxycarotenoid + O2 = 2-cis,4-trans-xanthoxin + a 12′-apo-carotenal
(2) 9-cis-violaxanthin + O2 = 2-cis,4-trans-xanthoxin + (3S,5R,6S)-5,6-epoxy-3-hydroxy-5,6-dihydro-12′-apo-β-caroten-12′-al
(3) 9′-cis-neoxanthin + O2 = 2-cis,4-trans-xanthoxin + (3S,5R,6R)-5,6-dihydroxy-6,7-didehydro-5,6-dihydro-12′-apo-β-caroten-12′-al
For diagram of abscisic-acid biosynthesis, click here
Other name(s): nine-cis-epoxycarotenoid dioxygenase; NCED; AtNCED3; PvNCED1; VP14
Systematic name: 9-cis-epoxycarotenoid 11,12-dioxygenase
Comments: Requires iron(II). Acts on 9-cis-violaxanthin and 9′-cis-neoxanthin but not on the all-trans isomers [2,3]. In vitro, it will cleave 9-cis-zeaxanthin. Catalyses the first step of abscisic-acid biosynthesis from carotenoids in chloroplasts, in response to water stress. The other enzymes involved in the abscisic-acid biosynthesis pathway are EC 1.1.1.288 (xanthoxin dehydrogenase), EC 1.2.3.14 (abscisic-aldehyde oxidase) and EC 1.14.13.93 [(+)-abscisic acid 8′-hydroxylase].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 199877-10-6
References:
1.  Schwartz, S.H., Tan, B.C., Gage, D.A., Zeevaart, J.A. and McCarty, D.R. Specific oxidative cleavage of carotenoids by VP14 of maize. Science 276 (1997) 1872–1874. [DOI] [PMID: 9188535]
2.  Tan, B.C., Schwartz, S.H., Zeevaart, J.A. and McCarty, D.R. Genetic control of abscisic acid biosynthesis in maize. Proc. Natl. Acad. Sci. USA 94 (1997) 12235–12240. [DOI] [PMID: 9342392]
3.  Qin, X. and Zeevaart, J.A. The 9-cis-epoxycarotenoid cleavage reaction is the key regulatory step of abscisic acid biosynthesis in water-stressed bean. Proc. Natl. Acad. Sci. USA 96 (1999) 15354–15361. [DOI] [PMID: 10611388]
4.  Thompson, A.J., Jackson, A.C., Symonds, R.C., Mulholland, B.J., Dadswell, A.R., Blake, P.S., Burbidge, A. and Taylor, I.B. Ectopic expression of a tomato 9-cis-epoxycarotenoid dioxygenase gene causes over-production of abscisic acid. Plant J. 23 (2000) 363–374. [DOI] [PMID: 10929129]
5.  Iuchi, S., Kobayashi, M., Taji, T., Naramoto, M., Seki, M., Kato, T., Tabata, S., Kakubari, Y., Yamaguchi-Shinozaki, K. and Shinozaki, K. Regulation of drought tolerance by gene manipulation of 9-cis-epoxycarotenoid dioxygenase, a key enzyme in abscisic acid biosynthesis in Arabidopsis. Plant J. 27 (2001) 325–333. [DOI] [PMID: 11532178]
6.  Iuchi, S., Kobayashi, M., Taji, T., Naramoto, M., Seki, M., Kato, T., Tabata, S., Kakubari, Y., Yamaguchi-Shinozaki, K. and Shinozaki, K. Regulation of drought tolerance by gene manipulation of 9-cis-epoxycarotenoid dioxygenase, a key enzyme in abscisic acid biosynthesis in Arabidopsis. Plant J. 30 (2002) 611.
[EC 1.13.11.51 created 2005]
 
 
EC 1.13.11.58     
Accepted name: linoleate 9S-lipoxygenase
Reaction: linoleate + O2 = (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Glossary: linoleate = (9Z,12Z)-octadeca-9,12-dienoate
Other name(s): 9-lipoxygenase; 9S-lipoxygenase; linoleate 9-lipoxygenase; LOX1 (gene name); 9S-LOX
Systematic name: linoleate:oxygen 9S-oxidoreductase
Comments: Contains nonheme iron. A common plant lipoxygenase that oxidizes linoleate and α-linolenate, the two most common polyunsaturated fatty acids in plants, by inserting molecular oxygen at the C9 position with (S)-configuration. The enzyme plays a physiological role during the early stages of seedling growth. The enzyme from Arabidopsis thaliana shows comparable activity towards linoleate and linolenate [4]. EC 1.13.11.12 (linoleate 13S-lipoxygenase) catalyses a similar reaction at another position of these fatty acids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Vellosillo, T., Martinez, M., Lopez, M.A., Vicente, J., Cascon, T., Dolan, L., Hamberg, M. and Castresana, C. Oxylipins produced by the 9-lipoxygenase pathway in Arabidopsis regulate lateral root development and defense responses through a specific signaling cascade. Plant Cell 19 (2007) 831–846. [DOI] [PMID: 17369372]
2.  Boeglin, W.E., Itoh, A., Zheng, Y., Coffa, G., Howe, G.A. and Brash, A.R. Investigation of substrate binding and product stereochemistry issues in two linoleate 9-lipoxygenases. Lipids 43 (2008) 979–987. [DOI] [PMID: 18795358]
3.  Andreou, A.Z., Hornung, E., Kunze, S., Rosahl, S. and Feussner, I. On the substrate binding of linoleate 9-lipoxygenases. Lipids 44 (2009) 207–215. [DOI] [PMID: 19037675]
4.  Bannenberg, G., Martinez, M., Hamberg, M. and Castresana, C. Diversity of the enzymatic activity in the lipoxygenase gene family of Arabidopsis thaliana. Lipids 44 (2009) 85–95. [DOI] [PMID: 18949503]
[EC 1.13.11.58 created 2011]
 
 
EC 1.13.11.59     
Accepted name: torulene dioxygenase
Reaction: torulene + O2 = 4′-apo-β,&psi;-caroten-4′-al + 3-methylbut-2-enal
Glossary: torulene = 3′,4′-didehydro-β,&psi;-carotene
Other name(s): CAO-2; CarT
Systematic name: torulene:oxygen oxidoreductase
Comments: It is assumed that 3-methylbut-2-enal is formed. The enzyme cannot cleave the saturated 3′,4′-bond of γ-carotene which implies that a 3′,4′-double bond is neccessary for this reaction.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Prado-Cabrero, A., Estrada, A.F., Al-Babili, S. and Avalos, J. Identification and biochemical characterization of a novel carotenoid oxygenase: elucidation of the cleavage step in the Fusarium carotenoid pathway. Mol. Microbiol. 64 (2007) 448–460. [DOI] [PMID: 17493127]
2.  Saelices, L., Youssar, L., Holdermann, I., Al-Babili, S. and Avalos, J. Identification of the gene responsible for torulene cleavage in the Neurospora carotenoid pathway. Mol. Genet. Genomics 278 (2007) 527–537. [DOI] [PMID: 17610084]
3.  Estrada, A.F., Maier, D., Scherzinger, D., Avalos, J. and Al-Babili, S. Novel apocarotenoid intermediates in Neurospora crassa mutants imply a new biosynthetic reaction sequence leading to neurosporaxanthin formation. Fungal Genet. Biol. 45 (2008) 1497–1505. [DOI] [PMID: 18812228]
[EC 1.13.11.59 created 2011]
 
 
EC 1.13.11.63     
Accepted name: β-carotene 15,15′-dioxygenase
Reaction: β-carotene + O2 = 2 all-trans-retinal
For diagram of retinal and derivatives biosynthesis, click here
Other name(s): blh (gene name); BCO1 (gene name); BCDO (gene name); carotene dioxygenase; carotene 15,15′-dioxygenase; BCMO1 (misleading); β-carotene 15,15′-monooxygenase (incorrect)
Systematic name: β-carotene:oxygen 15,15′-dioxygenase (bond-cleaving)
Comments: Requires Fe2+. The enzyme cleaves β-carotene symmetrically, producing two molecules of all-trans-retinal. Both atoms of the oxygen molecule are incorporated into the products [8]. The enzyme can also process β-cryptoxanthin, 8′-apo-β-carotenal, 4′-apo-β-carotenal, α-carotene and γ-carotene in decreasing order. The presence of at least one unsubstituted β-ionone ring in a substrate greater than C30 is mandatory [5]. A prokaryotic enzyme has been reported from the uncultured marine bacterium 66A03, where it is involved in the proteorhodopsin system, which uses retinal as its chromophore [6,7].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Goodman, D.S., Huang, H.S. and Shiratori, T. Mechanism of the biosynthesis of vitamin A from β-carotene. J. Biol. Chem. 241 (1966) 1929–1932. [PMID: 5946623]
2.  Goodman, D.S., Huang, H.S., Kanai, M. and Shiratori, T. The enzymatic conversion of all-trans β-carotene into retinal. J. Biol. Chem. 242 (1967) 3543–3554.
3.  Yan, W., Jang, G.F., Haeseleer, F., Esumi, N., Chang, J., Kerrigan, M., Campochiaro, M., Campochiaro, P., Palczewski, K. and Zack, D.J. Cloning and characterization of a human β,β-carotene-15,15′-dioxygenase that is highly expressed in the retinal pigment epithelium. Genomics 72 (2001) 193–202. [DOI] [PMID: 11401432]
4.  Leuenberger, M.G., Engeloch-Jarret, C. and Woggon, W.D. The reaction mechanism of the enzyme-catalysed central cleavage of β-carotene to retinal. Angew. Chem. 40 (2001) 2614–2616. [DOI] [PMID: 11458349]
5.  Kim, Y.S. and Oh, D.K. Substrate specificity of a recombinant chicken β-carotene 15,15′-monooxygenase that converts β-carotene into retinal. Biotechnol. Lett. 31 (2009) 403–408. [DOI] [PMID: 18979213]
6.  Kim, Y.S., Kim, N.H., Yeom, S.J., Kim, S.W. and Oh, D.K. In vitro characterization of a recombinant Blh protein from an uncultured marine bacterium as a β-carotene 15,15′-dioxygenase. J. Biol. Chem. 284 (2009) 15781–15793. [DOI] [PMID: 19366683]
7.  Kim, Y.S., Park, C.S. and Oh, D.K. Retinal production from β-carotene by β-carotene 15,15′-dioxygenase from an unculturable marine bacterium. Biotechnol. Lett. 32 (2010) 957–961. [DOI] [PMID: 20229064]
8.  dela Seña, C., Riedl, K.M., Narayanasamy, S., Curley, R.W., Jr., Schwartz, S.J. and Harrison, E.H. The human enzyme that converts dietary provitamin A carotenoids to vitamin A is a dioxygenase. J. Biol. Chem. 289 (2014) 13661–13666. [DOI] [PMID: 24668807]
[EC 1.13.11.63 created 2012 (EC 1.14.99.36 created 1972 as EC 1.13.11.21, transferred 2001 to EC 1.14.99.36, incorporated 2015), modified 2016]
 
 
EC 1.13.11.69     
Accepted name: carlactone synthase
Reaction: 9-cis-10′-apo-β-carotenal + 2 O2 = carlactone + (2E,4E,6E)-7-hydroxy-4-methylhepta-2,4,6-trienal
For diagram of strigol biosynthesis, click here
Glossary: carlactone = 3-methyl-5-{[(1Z,3E)-2-methyl-4-(2,6,6-trimethylcyclohex-1-en-1-yl)buta-1,3-dien-1-yl]oxy}-5H-furan-2-one
Other name(s): CCD8 (gene name); MAX4 (gene name); NCED8 (gene name)
Systematic name: 9-cis-10′-apo-β-carotenal:oxygen oxidoreductase (14,15-cleaving, carlactone-forming)
Comments: Requires Fe2+. The enzyme participates in a pathway leading to biosynthesis of strigolactones, plant hormones involved in promotion of symbiotic associations known as arbuscular mycorrhiza. Also catalyses EC 1.13.11.70, all-trans-10′-apo-β-carotenal 13,14-cleaving dioxygenase, but 10-fold slower.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sorefan, K., Booker, J., Haurogne, K., Goussot, M., Bainbridge, K., Foo, E., Chatfield, S., Ward, S., Beveridge, C., Rameau, C. and Leyser, O. MAX4 and RMS1 are orthologous dioxygenase-like genes that regulate shoot branching in Arabidopsis and pea. Genes Dev. 17 (2003) 1469–1474. [DOI] [PMID: 12815068]
2.  Schwartz, S.H., Qin, X. and Loewen, M.C. The biochemical characterization of two carotenoid cleavage enzymes from Arabidopsis indicates that a carotenoid-derived compound inhibits lateral branching. J. Biol. Chem. 279 (2004) 46940–46945. [DOI] [PMID: 15342640]
3.  Alder, A., Jamil, M., Marzorati, M., Bruno, M., Vermathen, M., Bigler, P., Ghisla, S., Bouwmeester, H., Beyer, P. and Al-Babili, S. The path from β-carotene to carlactone, a strigolactone-like plant hormone. Science 335 (2012) 1348–1351. [DOI] [PMID: 22422982]
[EC 1.13.11.69 created 2012]
 
 
EC 1.13.11.70     
Accepted name: all-trans-10′-apo-β-carotenal 13,14-cleaving dioxygenase
Reaction: all-trans-10′-apo-β-carotenal + O2 = 13-apo-β-carotenone + (2E,4E,6E)-4-methylocta-2,4,6-trienedial
For diagram of 10′-apo-β-carotenal biosynthesis, click here
Other name(s): CCD8 (gene name); MAX4 (gene name); NCED8 (gene name); all-trans-10′-apo-β-carotenal:O2 oxidoreductase (13,14-cleaving)
Systematic name: all-trans-10′-apo-β-carotenal:oxygen oxidoreductase (13,14-cleaving)
Comments: Requires Fe2+. The enzyme from the plant Arabidopsis thaliana also catalyses EC 1.13.11.69, carlactone synthase, 10-fold faster.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Schwartz, S.H., Qin, X. and Loewen, M.C. The biochemical characterization of two carotenoid cleavage enzymes from Arabidopsis indicates that a carotenoid-derived compound inhibits lateral branching. J. Biol. Chem. 279 (2004) 46940–46945. [DOI] [PMID: 15342640]
[EC 1.13.11.70 created 2012]
 
 
EC 1.13.11.80     
Accepted name: (3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase
Reaction: (3,5-dihydroxyphenyl)acetyl-CoA + O2 = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA
Glossary: (3,5-dihydroxyphenyl)acetyl-CoA = 2-(3,5-dihydroxyphenyl)acetyl-CoA
Other name(s): DpgC
Systematic name: (3,5-dihydroxyphenyl)acetyl-CoA:oxygen oxidoreductase
Comments: The enzyme, characterized from bacteria Streptomyces toyocaensis and Amycolatopsis orientalis, is involved in the biosynthesis of (3,5-dihydroxyphenyl)glycine, a component of the glycopeptide antibiotic vancomycin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Chen, H., Tseng, C.C., Hubbard, B.K. and Walsh, C.T. Glycopeptide antibiotic biosynthesis: enzymatic assembly of the dedicated amino acid monomer (S)-3,5-dihydroxyphenylglycine. Proc. Natl. Acad. Sci. USA 98 (2001) 14901–14906. [DOI] [PMID: 11752437]
2.  Widboom, P.F., Fielding, E.N., Liu, Y. and Bruner, S.D. Structural basis for cofactor-independent dioxygenation in vancomycin biosynthesis. Nature 447 (2007) 342–345. [DOI] [PMID: 17507985]
3.  Fielding, E.N., Widboom, P.F. and Bruner, S.D. Substrate recognition and catalysis by the cofactor-independent dioxygenase DpgC. Biochemistry 46 (2007) 13994–14000. [DOI] [PMID: 18004875]
[EC 1.13.11.80 created 2015]
 
 
EC 1.13.11.92     
Accepted name: fatty acid α-dioxygenase
Reaction: a fatty acid + O2 = a (2R)-2-hydroperoxyfatty acid
Other name(s): DOX1 (gene name)
Systematic name: fatty acid:oxygen 2-oxidoreductase [(2R)-2-hydroperoxyfatty acid-forming]
Comments: Contains heme. This plant enzyme catalyses the (2R)-hydroperoxidation of fatty acids. It differs from lipoxygenases and cyclooxygenases in that the oxygen addition does not target an unsaturated region in the fatty acid. In vitro the product undergoes spontaneous decarboxylation, resulting in formation of a chain-shortened aldehyde. In vivo the product may be reduced to a (2R)-2-hydroxyfatty acid. The enzyme, which is involved in responses to different abiotic and biotic stresses, has a wide substrate range that includes both saturated and unsaturated fatty acids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Akakabe, Y., Matsui, K., and Kajiwara, T. Enantioselective α-hydroperoxylation of long-chain fatty acids with crude enzyme of marine green alga Ulva pertusa. Tetrahedron Lett. 40 (1999) 1137–1140. [DOI]
2.  Hamberg, M., Sanz, A. and Castresana, C. α-oxidation of fatty acids in higher plants. Identification of a pathogen-inducible oxygenase (piox) as an α-dioxygenase and biosynthesis of 2-hydroperoxylinolenic acid. J. Biol. Chem. 274 (1999) 24503–24513. [DOI] [PMID: 10455113]
3.  Saffert, A., Hartmann-Schreier, J., Schon, A. and Schreier, P. A dual function α-dioxygenase-peroxidase and NAD(+) oxidoreductase active enzyme from germinating pea rationalizing α-oxidation of fatty acids in plants. Plant Physiol. 123 (2000) 1545–1552. [DOI] [PMID: 10938370]
4.  Koeduka, T., Matsui, K., Akakabe, Y. and Kajiwara, T. Catalytic properties of rice α-oxygenase. A comparison with mammalian prostaglandin H synthases. J. Biol. Chem. 277 (2002) 22648–22655. [DOI] [PMID: 11909851]
5.  Liu, W., Rogge, C.E., Bambai, B., Palmer, G., Tsai, A.L. and Kulmacz, R.J. Characterization of the heme environment in Arabidopsis thaliana fatty acid α-dioxygenase-1. J. Biol. Chem. 279 (2004) 29805–29815. [DOI] [PMID: 15100225]
6.  Meisner, A.K., Saffert, A., Schreier, P. and Schon, A. Fatty acid α-dioxygenase from Pisum sativum: temporal and spatial regulation during germination and plant development. J. Plant Physiol. 166 (2009) 333–343. [DOI] [PMID: 18760499]
[EC 1.13.11.92 created 2021]
 
 
EC 1.13.12.5     
Accepted name: Renilla-type luciferase
Reaction: coelenterazine h + O2 = excited coelenteramide h monoanion + CO2 (over-all reaction)
(1a) coelenterazine h + O2 = coelenterazine h dioxetanone
(1b) coelenterazine h dioxetanone = excited coelenteramide h monoanion + CO2
For diagram of reaction, click here
Glossary: coelenterazine h = Renilla luciferin = 2,8-dibenzyl-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one
coelenteramide h = Renilla oxyluciferin = N-[3-benzyl-5-(4-hydroxyphenyl)pyrazin-2-yl]-2-phenylacetamide
Other name(s): Renilla-luciferin 2-monooxygenase; luciferase (Renilla luciferin); Renilla-luciferin:oxygen 2-oxidoreductase (decarboxylating)
Systematic name: coelenterazine h:oxygen 2-oxidoreductase (decarboxylating)
Comments: This enzyme has been studied from the soft coral Renilla reniformis. Before the reaction occurs the substrate is sequestered by a coelenterazine-binding protein. Elevation in the concentration of calcium ions releases the substrate, which then interacts with the luciferase. Upon binding the substrate, the enzyme catalyses an oxygenation, producing a very short-lived hydroperoxide that cyclizes into a dioxetanone structure, which collapses, releasing a CO2 molecule. The spontaneous breakdown of the dioxetanone releases the energy (about 50 kcal/mole) that is necessary to generate the excited state of the coelenteramide product, which is the singlet form of the monoanion. In vivo the product undergoes the process of nonradiative energy transfer to an accessory protein, a green fluorescent protein (GFP), which results in green bioluminescence. In vitro, in the absence of GFP, the product emits blue light.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 61869-41-8
References:
1.  Cormier, M.J., Hori, K. and Anderson, J.M. Bioluminescence in coelenterates. Biochim. Biophys. Acta 346 (1974) 137–164. [PMID: 4154104]
2.  Hori, K., Anderson, J.M., Ward, W.W. and Cormier, M.J. Renilla luciferin as the substrate for calcium induced photoprotein bioluminescence. Assignment of luciferin tautomers in aequorin and mnemiopsin. Biochemistry 14 (1975) 2371–2376. [PMID: 237531]
3.  Anderson, J.M., Charbonneau, H. and Cormier, M.J. Mechanism of calcium induction of Renilla bioluminescence. Involvement of a calcium-triggered luciferin binding protein. Biochemistry 13 (1974) 1195–1200. [PMID: 4149963]
4.  Shimomura, O. and Johnson, F.H. Chemical nature of bioluminescence systems in coelenterates. Proc. Natl. Acad. Sci. USA 72 (1975) 1546–1549. [DOI] [PMID: 236561]
5.  Charbonneau, H. and Cormier, M.J. Ca2+-induced bioluminescence in Renilla reniformis. Purification and characterization of a calcium-triggered luciferin-binding protein. J. Biol. Chem. 254 (1979) 769–780. [PMID: 33174]
6.  Lorenz, W.W., McCann, R.O., Longiaru, M. and Cormier, M.J. Isolation and expression of a cDNA encoding Renilla reniformis luciferase. Proc. Natl. Acad. Sci. USA 88 (1991) 4438–4442. [DOI] [PMID: 1674607]
7.  Loening, A.M., Fenn, T.D. and Gambhir, S.S. Crystal structures of the luciferase and green fluorescent protein from Renilla reniformis. J. Mol. Biol. 374 (2007) 1017–1028. [DOI] [PMID: 17980388]
[EC 1.13.12.5 created 1976, modified 1981, modified 1982, modified 2004, modified 2017]
 
 
EC 1.13.12.14      
Transferred entry: chlorophyllide-a oxygenase. Now EC 1.14.13.122, chlorophyllide-a oxygenase
[EC 1.13.12.14 created 2006, deleted 2011]
 
 
EC 1.13.12.16     
Accepted name: nitronate monooxygenase
Reaction: ethylnitronate + O2 = acetaldehyde + nitrite + other products
Other name(s): NMO; 2-nitropropane dioxygenase (incorrect)
Systematic name: nitronate:oxygen 2-oxidoreductase (nitrite-forming)
Comments: Previously classified as 2-nitropropane dioxygenase (EC 1.13.11.32), but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Neither hydrogen peroxide nor superoxide were detected during enzyme turnover. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Francis, K., Russell, B. and Gadda, G. Involvement of a flavosemiquinone in the enzymatic oxidation of nitroalkanes catalyzed by 2-nitropropane dioxygenase. J. Biol. Chem. 280 (2005) 5195–5204. [DOI] [PMID: 15582992]
2.  Ha, J.Y., Min, J.Y., Lee, S.K., Kim, H.S., Kim do, J., Kim, K.H., Lee, H.H., Kim, H.K., Yoon, H.J. and Suh, S.W. Crystal structure of 2-nitropropane dioxygenase complexed with FMN and substrate. Identification of the catalytic base. J. Biol. Chem. 281 (2006) 18660–18667. [DOI] [PMID: 16682407]
3.  Gadda, G. and Francis, K. Nitronate monooxygenase, a model for anionic flavin semiquinone intermediates in oxidative catalysis. Arch. Biochem. Biophys. 493 (2010) 53–61. [DOI] [PMID: 19577534]
4.  Francis, K. and Gadda, G. Kinetic evidence for an anion binding pocket in the active site of nitronate monooxygenase. Bioorg. Chem. 37 (2009) 167–172. [DOI] [PMID: 19683782]
[EC 1.13.12.16 created 1984 as EC 1.13.11.32, transferred 2009 to EC 1.13.12.16, modified 2011]
 
 
EC 1.13.12.24     
Accepted name: calcium-regulated photoprotein
Reaction: [apoaequorin] + coelenterazine + O2 + 3 Ca2+ = [excited state blue fluorescent protein] + CO2 (overall reaction)
(1a) [apoaequorin] + coelenterazine = [apoaequorin containing coelenterazine]
(1b) [apoaequorin containing coelenterazine] + O2 = [aequorin]
(1c) [aequorin] + 3 Ca2+ = [aequorin] 1,2-dioxetan-3-one
(1d) [aequorin] 1,2-dioxetan-3-one = [excited state blue fluorescent protein] + CO2
Glossary: coelenterazine = 8-benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one
coelenteramide = N-[3-benzyl-5-(4-hydroxyphenyl)pyrazin-2-yl]-2-(4-hydroxyphenyl)acetamide
aequorin = the non-covalent complex formed by apoaequorin polypeptide and coelenterazine-2-hydroperoxide.
blue fluorescent protein = the non-covalent complex formed by Ca2+-bound apoaequorin polypeptide and coelenteramide
Other name(s): Ca2+-regulated photoprotein; calcium-activated photoprotein; aequorin; obelin; halistaurin; mitrocomin; phialidin; clytin; mnemiopsin; berovin
Systematic name: coelenterazine:oxygen 2-oxidoreductase (decarboxylating, calcium-dependent)
Comments: Ca2+-regulated photoproteins are found in a variety of bioluminescent marine organisms, mostly coelenterates, and are responsible for their light emission. The best studied enzyme is from the jellyfish Aequorea victoria. The enzyme tightly binds the imidazolopyrazinone derivative coelenterazine, which is then peroxidized by oxygen. The hydroperoxide is stably bound until three Ca2+ ions bind to the protein, inducing a structural change that results in the formation of a 1,2-dioxetan-3-one ring, followed by decarboxylation and generation of a protein-bound coelenteramide in an excited state. The calcium-bound protein-product complex is known as a blue fluorescent protein. In vivo the energy is transferred to a green fluorescent protein (GFP) by Förster resonance energy transfer. In vitro, in the absence of GFP, coelenteramide emits a photon of blue light while returning to its ground state.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Shimomura, O., Johnson, F. H., and Saiga, Y. Purification and properties of aequorin, a bio-(chemi-) luminescent protein from the jellyfish, Aequorea aequorea. Fed. Proc. 21 (1962) 401.
2.  Morise, H., Shimomura, O., Johnson, F.H. and Winant, J. Intermolecular energy transfer in the bioluminescent system of Aequorea. Biochemistry 13 (1974) 2656–2662. [PMID: 4151620]
3.  Inouye, S., Noguchi, M., Sakaki, Y., Takagi, Y., Miyata, T., Iwanaga, S., Miyata, T. and Tsuji, F.I. Cloning and sequence analysis of cDNA for the luminescent protein aequorin. Proc. Natl. Acad. Sci. USA 82 (1985) 3154–3158. [DOI] [PMID: 3858813]
4.  Head, J.F., Inouye, S., Teranishi, K. and Shimomura, O. The crystal structure of the photoprotein aequorin at 2.3 Å resolution. Nature 405 (2000) 372–376. [DOI] [PMID: 10830969]
5.  Deng, L., Vysotski, E.S., Markova, S.V., Liu, Z.J., Lee, J., Rose, J. and Wang, B.C. All three Ca2+-binding loops of photoproteins bind calcium ions: the crystal structures of calcium-loaded apo-aequorin and apo-obelin. Protein Sci. 14 (2005) 663–675. [DOI] [PMID: 15689515]
[EC 1.13.12.24 created 2018]
 
 
EC 1.14.11.8     
Accepted name: trimethyllysine dioxygenase
Reaction: N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2 = (3S)-3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
Other name(s): trimethyllysine α-ketoglutarate dioxygenase; TML-α-ketoglutarate dioxygenase; TML hydroxylase; 6-N,6-N,6-N-trimethyl-L-lysine,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Systematic name: N6,N6,N6-trimethyl-L-lysine,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Comments: Requires Fe2+ and ascorbate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 74622-49-4
References:
1.  Hulse, J.D., Ellis, S.R. and Henderson, L.M. Carnitine biosynthesis. β-Hydroxylation of trimethyllysine by an α-ketoglutarate-dependent mitochondrial dioxygenase. J. Biol. Chem. 253 (1978) 1654–1659. [PMID: 627563]
2.  Al Temimi, A.H., Pieters, B.J., Reddy, Y.V., White, P.B. and Mecinovic, J. Substrate scope for trimethyllysine hydroxylase catalysis. Chem. Commun. (Camb.) 52 (2016) 12849–12852. [PMID: 27730239]
3.  Lesniak, R.K., Markolovic, S., Tars, K. and Schofield, C.J. Human carnitine biosynthesis proceeds via (2S,3S)-3-hydroxy-N&epsilon;-trimethyllysine. Chem. Commun. (Camb.) 53 (2016) 440–442. [PMID: 27965989]
4.  Reddy, Y.V., Al Temimi, A.H., White, P.B. and Mecinovic, J. Evidence that trimethyllysine hydroxylase catalyzes the formation of (2S,3S)-3-hydroxy-N&epsilon;-trimethyllysine. Org. Lett. 19 (2017) 400–403. [PMID: 28045275]
[EC 1.14.11.8 created 1983]
 
 
EC 1.14.11.9     
Accepted name: flavanone 3-dioxygenase
Reaction: a (2S)-flavan-4-one + 2-oxoglutarate + O2 = a (2R,3R)-dihydroflavonol + succinate + CO2
For diagram of flavonoid biosynthesis, click here and for diagram of naringenin derivatives biosynthesis, click here
Other name(s): naringenin 3-hydroxylase; flavanone 3-hydroxylase; flavanone 3β-hydroxylase; flavanone synthase I; (2S)-flavanone 3-hydroxylase; naringenin,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating); F3H; flavanone,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Systematic name: (2S)-flavan-4-one,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Comments: Requires Fe2+ and ascorbate. This plant enzyme catalyses an early step in the flavonoid biosynthesis pathway, leading to the production of flavanols and anthocyanins. Substrates include (2S)-naringenin, (2S)-eriodictyol, (2S)-dihydrotricetin and (2S)-pinocembrin. Some enzymes are bifuctional and also catalyse EC 1.14.20.6, flavonol synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 75991-43-4
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.  Charrier, B., Coronado, C., Kondorosi, A. and Ratet, P. Molecular characterization and expression of alfalfa (Medicago sativa L.) flavanone-3-hydroxylase and dihydroflavonol-4-reductase encoding genes. Plant Mol. Biol. 29 (1995) 773–786. [PMID: 8541503]
3.  Pelletier, M.K. and Shirley, B.W. Analysis of flavanone 3-hydroxylase in Arabidopsis seedlings. Coordinate regulation with chalcone synthase and chalcone isomerase. Plant Physiol. 111 (1996) 339–345. [PMID: 8685272]
4.  Wellmann, F., Matern, U. and Lukačin, R. Significance of C-terminal sequence elements for Petunia flavanone 3β-hydroxylase activity. FEBS Lett. 561 (2004) 149–154. [DOI] [PMID: 15013767]
5.  Jin, Z., Grotewold, E., Qu, W., Fu, G. and Zhao, D. Cloning and characterization of a flavanone 3-hydroxylase gene from Saussurea medusa. DNA Seq 16 (2005) 121–129. [DOI] [PMID: 16147863]
6.  Shen, G., Pang, Y., Wu, W., Deng, Z., Zhao, L., Cao, Y., Sun, X. and Tang, K. Cloning and characterization of a flavanone 3-hydroxylase gene from Ginkgo biloba. Biosci Rep 26 (2006) 19–29. [DOI] [PMID: 16779664]
[EC 1.14.11.9 created 1983, modified 1989, modified 2004, modified 2016]
 
 
EC 1.14.11.19      
Transferred entry: anthocyanidin synthase. Now EC 1.14.20.4, anthocyanidin synthase
[EC 1.14.11.19 created 2001, modified 2017, deleted 2018]
 
 
EC 1.14.11.60     
Accepted name: scopoletin 8-hydroxylase
Reaction: scopoletin + 2-oxoglutarate + O2 = fraxetin + succinate + CO2
Glossary: fraxetin = 7,8-dihydroxy-6-methoxy-2H-chromen-2-one
scopoletin = 7-hydroxy-6-methoxy-2H-chromen-2-one
Other name(s): S8H (gene name)
Systematic name: scopoletin,2-oxoglutarate:oxygen oxidoreductase (8-hydroxylating)
Comments: Requires iron(II) and ascorbate. A protein involved in biosynthesis of iron(III)-chelating coumarins in higher plants.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Siwinska, J., Siatkowska, K., Olry, A., Grosjean, J., Hehn, A., Bourgaud, F., Meharg, A.A., Carey, M., Lojkowska, E. and Ihnatowicz, A. Scopoletin 8-hydroxylase: a novel enzyme involved in coumarin biosynthesis and iron-deficiency responses in Arabidopsis. J. Exp. Bot. 69 (2018) 1735–1748. [PMID: 29361149]
2.  Rajniak, J., Giehl, R.FH., Chang, E., Murgia, I., von Wiren, N. and Sattely, E.S. Biosynthesis of redox-active metabolites in response to iron deficiency in plants. Nat. Chem. Biol. 14 (2018) 442–450. [PMID: 29581584]
[EC 1.14.11.60 created 2018]
 
 
EC 1.14.11.61     
Accepted name: feruloyl-CoA 6-hydroxylase
Reaction: trans-feruloyl-CoA + 2-oxoglutarate + O2 = trans-6-hydroxyferuloyl-CoA + succinate + CO2
Glossary: trans-feruloyl-CoA = 4-hydroxy-3-methoxycinnamoyl-CoA = (E)-3-(4-hydroxy-3-methoxyphenyl)propenoyl-CoA
Systematic name: feruloyl-CoA,2-oxoglutarate:oxygen oxidoreductase (6-hydroxylating)
Comments: Requires iron(II) and ascorbate. The product spontaneously undergoes trans-cis isomerization and lactonization to form scopoletin, liberating CoA in the process. The enzymes from the plants Ruta graveolens and Ipomoea batatas also act on trans-4-coumaroyl-CoA. cf. EC 1.14.11.62, trans-4-coumaroyl-CoA 2-hydroxylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kai, K., Mizutani, M., Kawamura, N., Yamamoto, R., Tamai, M., Yamaguchi, H., Sakata, K. and Shimizu, B. Scopoletin is biosynthesized via ortho-hydroxylation of feruloyl CoA by a 2-oxoglutarate-dependent dioxygenase in Arabidopsis thaliana. Plant J. 55 (2008) 989–999. [PMID: 18547395]
2.  Bayoumi, S.A., Rowan, M.G., Blagbrough, I.S. and Beeching, J.R. Biosynthesis of scopoletin and scopolin in cassava roots during post-harvest physiological deterioration: the E-Z-isomerisation stage. Phytochemistry 69 (2008) 2928–2936. [PMID: 19004461]
3.  Vialart, G., Hehn, A., Olry, A., Ito, K., Krieger, C., Larbat, R., Paris, C., Shimizu, B., Sugimoto, Y., Mizutani, M. and Bourgaud, F. A 2-oxoglutarate-dependent dioxygenase from Ruta graveolens L. exhibits p-coumaroyl CoA 2′-hydroxylase activity (C2′H): a missing step in the synthesis of umbelliferone in plants. Plant J. 70 (2012) 460–470. [DOI] [PMID: 22168819]
4.  Matsumoto, S., Mizutani, M., Sakata, K. and Shimizu, B. Molecular cloning and functional analysis of the ortho-hydroxylases of p-coumaroyl coenzyme A/feruloyl coenzyme A involved in formation of umbelliferone and scopoletin in sweet potato, Ipomoea batatas (L.) Lam. Phytochemistry 74 (2012) 49–57. [PMID: 22169019]
[EC 1.14.11.61 created 2019]
 
 
EC 1.14.11.66     
Accepted name: [histone H3]-trimethyl-L-lysine9 demethylase
Reaction: a [histone H3]-N6,N6,N6-trimethyl-L-lysine9 + 2 2-oxoglutarate + 2 O2 = a [histone H3]-N6-methyl-L-lysine9 + 2 succinate + 2 formaldehyde + 2 CO2 (overall reaction)
(1a) a [histone H3]-N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2 = a [histone H3]-N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
(1b) a [histone H3]-N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2 = a [histone H3]-N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
Other name(s): KDM4A (gene name); KDM4B (gene name); KDM4C (gene name); KDM4D (gene name); JHDM3A (gene name); JMJD2 (gene name); JMJD2A (gene name); GASC1 (gene name)
Systematic name: [histone H3]-N6,N6,N6-trimethyl-L-lysine9,2-oxoglutarate:oxygen oxidoreductase
Comments: Requires iron(II). This entry describes a group of enzymes that demethylate N-methylated Lys-9 residues in the tail of the histone protein H3 (H3K9). This lysine residue can exist in three methylation states (mono-, di- and trimethylated), but this group of enzymes only act on the the tri- and di-methylated forms. The enzymes are dioxygenases and act by hydroxylating the methyl group, forming an unstable hemiaminal that leaves as formaldehyde. cf. EC 1.14.11.65, [histone H3]-dimethyl-L-lysine9 demethylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Cloos, P.A., Christensen, J., Agger, K., Maiolica, A., Rappsilber, J., Antal, T., Hansen, K.H. and Helin, K. The putative oncogene GASC1 demethylates tri- and dimethylated lysine 9 on histone H3. Nature 442 (2006) 307–311. [PMID: 16732293]
2.  Fodor, B.D., Kubicek, S., Yonezawa, M., O'Sullivan, R.J., Sengupta, R., Perez-Burgos, L., Opravil, S., Mechtler, K., Schotta, G. and Jenuwein, T. Jmjd2b antagonizes H3K9 trimethylation at pericentric heterochromatin in mammalian cells. Genes Dev. 20 (2006) 1557–1562. [PMID: 16738407]
3.  Klose, R.J., Yamane, K., Bae, Y., Zhang, D., Erdjument-Bromage, H., Tempst, P., Wong, J. and Zhang, Y. The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36. Nature 442 (2006) 312–316. [PMID: 16732292]
4.  Whetstine, J.R., Nottke, A., Lan, F., Huarte, M., Smolikov, S., Chen, Z., Spooner, E., Li, E., Zhang, G., Colaiacovo, M. and Shi, Y. Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases. Cell 125 (2006) 467–481. [PMID: 16603238]
[EC 1.14.11.66 created 2019]
 
 
EC 1.14.11.67     
Accepted name: [histone H3]-trimethyl-L-lysine4 demethylase
Reaction: a [histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 3 2-oxoglutarate + 3 O2 = a [histone H3]-L-lysine4 + 3 succinate + 3 formaldehyde + 3 CO2 (overall reaction)
(1a) a [histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2 = a [histone H3]-N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
(1b) a [histone H3]-N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2 = a [histone H3]-N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
(1c) a [histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2 = a [histone H3]-L-lysine4 + succinate + formaldehyde + CO2
Other name(s): KDM5A (gene name); KDM5B (gene name); KDM5C (gene name); KDM5D (gene name); JARID1A (gene name)
Systematic name: [histone H3]-N6,N6,N6-trimethyl-L-lysine4,2-oxoglutarate:oxygen oxidoreductase
Comments: Requires iron(II). This entry describes a group of enzymes that demethylate N-methylated L-lysine residues at position 4 of histone H3 (H3K4). The enzymes are dioxygenases and act by hydroxylating the methyl group, forming an unstable hemiaminal that leaves as formaldehyde. They can act on tri-, di-, and mono-methylated forms.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Seward, D.J., Cubberley, G., Kim, S., Schonewald, M., Zhang, L., Tripet, B. and Bentley, D.L. Demethylation of trimethylated histone H3 Lys4 in vivo by JARID1 JmjC proteins. Nat. Struct. Mol. Biol. 14 (2007) 240–242. [PMID: 17310255]
2.  Klose, R.J., Yan, Q., Tothova, Z., Yamane, K., Erdjument-Bromage, H., Tempst, P., Gilliland, D.G., Zhang, Y. and Kaelin, W.G., Jr. The retinoblastoma binding protein RBP2 is an H3K4 demethylase. Cell 128 (2007) 889–900. [PMID: 17320163]
3.  Iwase, S., Lan, F., Bayliss, P., de la Torre-Ubieta, L., Huarte, M., Qi, H.H., Whetstine, J.R., Bonni, A., Roberts, T.M. and Shi, Y. The X-linked mental retardation gene SMCX/JARID1C defines a family of histone H3 lysine 4 demethylases. Cell 128 (2007) 1077–1088. [PMID: 17320160]
4.  Christensen, J., Agger, K., Cloos, P.A., Pasini, D., Rose, S., Sennels, L., Rappsilber, J., Hansen, K.H., Salcini, A.E. and Helin, K. RBP2 belongs to a family of demethylases, specific for tri-and dimethylated lysine 4 on histone 3. Cell 128 (2007) 1063–1076. [PMID: 17320161]
[EC 1.14.11.67 created 2019]
 
 
EC 1.14.11.70     
Accepted name: 7-deoxycylindrospermopsin hydroxylase
Reaction: (1) 7-deoxycylindrospermopsin + 2-oxoglutarate + O2 = cylindrospermopsin + succinate + CO2
(2) 7-deoxycylindrospermopsin + 2-oxoglutarate + O2 = 7-epi-cylindrospermopsin + succinate + CO2
Glossary: cylindrospermopsin = (2aS,3R,4S,5aS,7R)-7-[(R)-(2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)(hydroxy)methyl]-3-methyl-2a,3,4,5,5a,6,7,8-octahydro-2H-1,8,8b-triazaacenaphthylen-4-yl hydrogen sulfate
Other name(s): cyrI (gene name)
Systematic name: 7-deoxycylindrospermopsin,2-oxoglutarate:oxygen oxidoreductase (7-hydroxylating)
Comments: Requires Fe(II). The enzyme, found in some cyanobacterial species, catalyses the last step in the biosynthesis of the toxins cylindrospermopsin and 7-epi-cylindrospermopsin. The ratio of the two products differs among different strains.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Mazmouz, R., Chapuis-Hugon, F., Pichon V., Mejean, A., and Ploux, O. The last step of the biosynthesis of the cyanotoxins cylindrospermopsin and 7-epi-cylindrospermopsin is catalysed by CyrI, a 2-oxoglutarate-dependent iron oxygenase. ChemBioChem 12 (2011) 858–862.
2.  Mazmouz, R., Essadik, I., Hamdane, D., Mejean, A. and Ploux, O. Characterization of CyrI, the hydroxylase involved in the last step of cylindrospermopsin biosynthesis: Binding studies, site-directed mutagenesis and stereoselectivity. Arch. Biochem. Biophys. 647 (2018) 1–9. [PMID: 29653078]
[EC 1.14.11.70 created 2019]
 
 
EC 1.14.12.20      
Transferred entry: pheophorbide a oxygenase. Now classified as EC 1.14.15.17, pheophorbide a oxygenase.
[EC 1.14.12.20 created 2007, deleted 2016]
 
 
EC 1.14.13.41      
Transferred entry: tyrosine N-monooxygenase. Now EC 1.14.14.36, tyrosine N-monooxygenase
[EC 1.14.13.41 created 1992, modified 2001, modified 2005, deleted 2016]
 
 
EC 1.14.13.64     
Accepted name: 4-hydroxybenzoate 1-hydroxylase
Reaction: 4-hydroxybenzoate + NAD(P)H + 2 H+ + O2 = hydroquinone + NAD(P)+ + H2O + CO2
Other name(s): 4-hydroxybenzoate 1-monooxygenase
Systematic name: 4-hydroxybenzoate,NAD(P)H:oxygen oxidoreductase (1-hydroxylating, decarboxylating)
Comments: Requires FAD. The enzyme from Candida parapsilosis is specific for 4-hydroxybenzoate derivatives and prefers NADH to NADPH as electron donor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 134214-78-1
References:
1.  van Berkel, W.J.H., Eppink, M.H.M., Middelhoven, W.J., Vervoort, J. and Rietjens, I.M.C.M. Catabolism of 4-hydroxybenzoate in Candida parapsilosis proceeds through initial oxidative decarboxylation by a FAD-dependent 4-hydroxybenzoate 1-hydroxylase. FEMS Microbiol. Lett. 121 (1994) 207–216. [DOI] [PMID: 7926672]
[EC 1.14.13.64 created 1999]
 
 
EC 1.14.13.68      
Transferred entry: 4-hydroxyphenylacetaldehyde oxime monooxygenase. Now EC 1.14.14.37, 4-hydroxyphenylacetaldehyde oxime monooxygenase
[EC 1.14.13.68 created 2000, modified 2005, deleted 2016]
 
 
EC 1.14.13.78      
Transferred entry: ent-kaurene oxidase. Now EC 1.14.14.86, ent-kaurene monooxygenase
[EC 1.14.13.78 created 2002, deleted 2018]
 
 
EC 1.14.13.81     
Accepted name: magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase
Reaction: magnesium-protoporphyrin IX 13-monomethyl ester + 3 NADPH + 3 H+ + 3 O2 = 3,8-divinyl protochlorophyllide a + 3 NADP+ + 5 H2O (overall reaction)
(1a) magnesium-protoporphyrin IX 13-monomethyl ester + NADPH + H+ + O2 = 131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + NADP+ + H2O
(1b) 131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + NADPH + H+ + O2 = 131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + NADP+ + 2 H2O
(1c) 131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + NADPH + H+ + O2 = 3,8-divinyl protochlorophyllide a + NADP+ + 2 H2O
For diagram of chlorophyll biosynthesis (earlier stages), click here
Other name(s): Mg-protoporphyrin IX monomethyl ester (oxidative) cyclase
Systematic name: magnesium-protoporphyrin-IX 13-monomethyl ester,NADPH:oxygen oxidoreductase (hydroxylating)
Comments: Requires Fe(II) for activity. The enzyme participates in the biosynthesis of chlorophyllide a in aerobic organisms. The same transformation is achieved in anaerobic organisms by EC 1.21.98.3, anaerobic magnesium-protoporphyrin IX monomethyl ester cyclase. Some facultative phototrophic bacteria, such as Rubrivivax gelatinosus, possess both enzymes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 92353-62-3
References:
1.  Walker, C.J., Mansfield, K.E., Rezzano, I.N., Hanamoto, C.M., Smith, K.M. and Castelfranco, P.A. The magnesium-protoporphyrin IX (oxidative) cyclase system. Studies on the mechanism and specificity of the reaction sequence. Biochem. J. 255 (1988) 685–692. [PMID: 3202840]
2.  Bollivar, D.W. and Beale, S.I. The chlorophyll biosynthetic enzyme Mg-protoporphyrin IX monomethyl ester (oxidative) cyclase (characterization and partial purification from Chlamydomonas reinhardtii and Synechocystis sp. PCC 6803). Plant Physiol. 112 (1996) 105–114. [PMID: 12226378]
3.  Pinta, V., Picaud, M., Reiss-Husson, F. and Astier, C. Rubrivivax gelatinosus acsF (previously orf358) codes for a conserved, putative binuclear-iron-cluster-containing protein involved in aerobic oxidative cyclization of Mg-protoporphyrin IX monomethylester. J. Bacteriol. 184 (2002) 746–753. [DOI] [PMID: 11790744]
4.  Tottey, S., Block, M.A., Allen, M., Westergren, T., Albrieux, C., Scheller, H.V., Merchant, S. and Jensen, P.E. Arabidopsis CHL27, located in both envelope and thylakoid membranes, is required for the synthesis of protochlorophyllide. Proc. Natl. Acad. Sci. USA 100 (2003) 16119–16124. [DOI] [PMID: 14673103]
[EC 1.14.13.81 created 2003, modified 2017]
 
 
EC 1.14.13.88      
Transferred entry: flavanoid 3,5-hydroxylase. Now EC 1.14.14.81, flavanoid 3,5-hydroxylase
[EC 1.14.13.88 created 2004, deleted 2018]
 
 
EC 1.14.13.101     
Accepted name: senecionine N-oxygenase
Reaction: senecionine + NADPH + H+ + O2 = senecionine N-oxide + NADP+ + H2O
Other name(s): senecionine monooxygenase (N-oxide-forming); SNO
Systematic name: senecionine,NADPH:oxygen oxidoreductase (N-oxide-forming)
Comments: A flavoprotein. NADH cannot replace NADPH. While pyrrolizidine alkaloids of the senecionine and monocrotaline types are generally good substrates (e.g. senecionine, retrorsine and monocrotaline), the enzyme does not use ester alkaloids lacking an hydroxy group at C-7 (e.g. supinine and phalaenopsine), 1,2-dihydro-alkaloids (e.g. sarracine) or unesterified necine bases (e.g. senkirkine) as substrates [1]. Senecionine N-oxide is used by insects as a chemical defense: senecionine N-oxide is non-toxic, but it is bioactivated to a toxic form by the action of cytochrome P-450 oxidase when absorbed by insectivores.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 220581-68-0
References:
1.  Lindigkeit, R., Biller, A., Buch, M., Schiebel, H.M., Boppre, M. and Hartmann, T. The two facies of pyrrolizidine alkaloids: the role of the tertiary amine and its N-oxide in chemical defense of insects with acquired plant alkaloids. Eur. J. Biochem. 245 (1997) 626–636. [DOI] [PMID: 9182998]
2.  Naumann, C., Hartmann, T. and Ober, D. Evolutionary recruitment of a flavin-dependent monooxygenase for the detoxification of host plant-acquired pyrrolizidine alkaloids in the alkaloid-defended arctiid moth Tyria jacobaeae. Proc. Natl. Acad. Sci. USA 99 (2002) 6085–6090. [DOI] [PMID: 11972041]
[EC 1.14.13.101 created 2006]
 
 
EC 1.14.13.112      
Transferred entry: 3-epi-6-deoxocathasterone 23-monooxygenase. Now EC 1.14.14.147, 3-epi-6-deoxocathasterone 23-monooxygenase
[EC 1.14.13.112 created 2010, deleted 2018]
 
 
EC 1.14.13.119      
Transferred entry: 5-epiaristolochene 1,3-dihydroxylase. Now EC 1.14.14.149, 5-epiaristolochene 1,3-dihydroxylase
[EC 1.14.13.119 created 2011, deleted 2018]
 
 
EC 1.14.13.122     
Accepted name: chlorophyllide-a oxygenase
Reaction: chlorophyllide a + 2 O2 + 2 NADPH + 2 H+ = chlorophyllide b + 3 H2O + 2 NADP+ (overall reaction)
(1a) chlorophyllide a + O2 + NADPH + H+ = 71-hydroxychlorophyllide a + H2O + NADP+
(1b) 71-hydroxychlorophyllide a + O2 + NADPH + H+ = chlorophyllide b + 2 H2O + NADP+
Other name(s): chlorophyllide a oxygenase; chlorophyll-b synthase; CAO
Systematic name: chlorophyllide-a:oxygen 71-oxidoreductase
Comments: Chlorophyll b is required for the assembly of stable light-harvesting complexes (LHCs) in the chloroplast of green algae, cyanobacteria and plants [2,3]. Contains a mononuclear iron centre [3]. The enzyme catalyses two successive hydroxylations at the 7-methyl group of chlorophyllide a. The second step yields the aldehyde hydrate, which loses H2O spontaneously to form chlorophyllide b [2]. Chlorophyll a and protochlorophyllide a are not substrates [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 216503-73-0
References:
1.  Espineda, C.E., Linford, A.S., Devine, D. and Brusslan, J.A. The AtCAO gene, encoding chlorophyll a oxygenase, is required for chlorophyll b synthesis in Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 96 (1999) 10507–10511. [DOI] [PMID: 10468639]
2.  Oster, U., Tanaka, R., Tanaka, A. and Rüdiger, W. Cloning and functional expression of the gene encoding the key enzyme for chlorophyll b biosynthesis (CAO) from Arabidopsis thaliana. Plant J. 21 (2000) 305–310. [DOI] [PMID: 10758481]
3.  Eggink, L.L., LoBrutto, R., Brune, D.C., Brusslan, J., Yamasato, A., Tanaka, A. and Hoober, J.K. Synthesis of chlorophyll b: localization of chlorophyllide a oxygenase and discovery of a stable radical in the catalytic subunit. BMC Plant Biol. 4 (2004) 5. [DOI] [PMID: 15086960]
4.  Porra, R.J., Schafer, W., Cmiel, E., Katheder, I. and Scheer, H. The derivation of the formyl-group oxygen of chlorophyll b in higher plants from molecular oxygen. Achievement of high enrichment of the 7-formyl-group oxygen from 18O2 in greening maize leaves. Eur. J. Biochem. 219 (1994) 671–679. [PMID: 8307032]
[EC 1.14.13.122 created 2006 as EC 1.13.12.14, transferred 2011 to EC 1.14.13.122, modified 2011]
 
 
EC 1.14.13.124      
Transferred entry: phenylalanine N-monooxygenase, now classified as EC 1.14.14.40, phenylalanine N-monooxygenase
[EC 1.14.13.124 created 2011, deleted 2017]
 
 
EC 1.14.13.125      
Transferred entry: tryptophan N-monooxygenase. Now EC 1.14.14.156, tryptophan N-monooxygenase
[EC 1.14.13.125 created 2011, deleted 2018]
 
 
EC 1.14.13.129      
Transferred entry: β-carotene 3-hydroxylase. Now EC 1.14.15.24, β-carotene 3-hydroxylase.
[EC 1.14.13.129 created 2011, deleted 2017]
 
 
EC 1.14.13.168     
Accepted name: indole-3-pyruvate monooxygenase
Reaction: (indol-3-yl)pyruvate + NADPH + H+ + O2 = (indol-3-yl)acetate + NADP+ + H2O + CO2
For diagram of indoleacetic acid biosynthesis, click here
Glossary: (indol-3-yl)pyruvate = 3-(1H-indol-3-yl)-2-oxopropanoate, (indol-3-yl)acetate = 2-(1H-indol-3-yl)acetate = indole-3-acetate
Other name(s): YUC2 (gene name); spi1 (gene name)
Systematic name: indole-3-pyruvate,NADPH:oxygen oxidoreductase (1-hydroxylating, decarboxylating)
Comments: This plant enzyme, along with EC 2.6.1.99 L-tryptophan—pyruvate aminotransferase, is responsible for the biosynthesis of the plant hormone indole-3-acetate from L-tryptophan.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Mashiguchi, K., Tanaka, K., Sakai, T., Sugawara, S., Kawaide, H., Natsume, M., Hanada, A., Yaeno, T., Shirasu, K., Yao, H., McSteen, P., Zhao, Y., Hayashi, K., Kamiya, Y. and Kasahara, H. The main auxin biosynthesis pathway in Arabidopsis. Proc. Natl. Acad. Sci. USA 108 (2011) 18512–18517. [DOI] [PMID: 22025724]
2.  Zhao, Y. Auxin biosynthesis: a simple two-step pathway converts tryptophan to indole-3-acetic acid in plants. Mol. Plant 5 (2012) 334–338. [DOI] [PMID: 22155950]
[EC 1.14.13.168 created 2012]
 
 
EC 1.14.13.169      
Transferred entry: sphinganine C4-monooxygenase. Now EC 1.14.18.5, sphingolipid C4-monooxygenase
[EC 1.14.13.169 created 2012, deleted 2015]
 
 
EC 1.14.13.180     
Accepted name: aklavinone 12-hydroxylase
Reaction: aklavinone + NADPH + H+ + O2 = &epsilon;-rhodomycinone + NADP+ + H2O
For diagram of aflatoxin biosynthesis, click here
Glossary: aklavinone = methyl (1R,2R,4S)-2-ethyl-2,4,5,7-tetrahydroxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracene-1-carboxylate
&epsilon;-rhodomycinone = methyl (1R,2R,4S)-2-ethyl-2,4,5,7,12-pentahydroxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracene-1-carboxylate
Other name(s): DnrF; RdmE; aklavinone 11-hydroxylase (incorrect)
Systematic name: aklavinone,NADPH:oxygen oxidoreductase (12-hydroxylating)
Comments: The enzymes from the Gram-positive bacteria Streptomyces peucetius and Streptomyces purpurascens participate in the biosynthesis of daunorubicin, doxorubicin and rhodomycins. The enzyme from Streptomyces purpurascens is an FAD monooxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Filippini, S., Solinas, M.M., Breme, U., Schluter, M.B., Gabellini, D., Biamonti, G., Colombo, A.L. and Garofano, L. Streptomyces peucetius daunorubicin biosynthesis gene, dnrF: sequence and heterologous expression. Microbiology 141 (1995) 1007–1016. [DOI] [PMID: 7773378]
2.  Niemi, J., Wang, Y., Airas, K., Ylihonko, K., Hakala, J. and Mantsala, P. Characterization of aklavinone-11-hydroxylase from Streptomyces purpurascens. Biochim. Biophys. Acta 1430 (1999) 57–64. [DOI] [PMID: 10082933]
[EC 1.14.13.180 created 2013]
 
 
EC 1.14.13.181     
Accepted name: 13-deoxydaunorubicin hydroxylase
Reaction: (1) 13-deoxydaunorubicin + NADPH + H+ + O2 = 13-dihydrodaunorubicin + NADP+ + H2O
(2) 13-dihydrodaunorubicin + NADPH + H+ + O2 = daunorubicin + NADP+ + 2 H2O
For diagram of daunorubicin biosynthesis, click here
Glossary: 13-dihydrodaunorubicin = daunorubicinol = (1S,3S)-3,5,12-trihydroxy-3-(1-hydroxyethyl)-10-methoxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracen-1-yl 3-amino-2,3,6-trideoxy-α-L-lyxo-hexopyranoside
13-deoxydaunorubicin = (1S,3S)-3-ethyl-3,5,12-trihydroxy-10-methoxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracen-1-yl 3-amino-2,3,6-trideoxy-α-L-lyxo-hexopyranoside
daunorubicin = (1S,3S)-3-acetyl-3,5,12-trihydroxy-10-methoxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracen-1-yl 3-amino-2,3,6-trideoxy-α-L-lyxo-hexopyranoside
Other name(s): DoxA
Systematic name: 13-deoxydaunorubicin,NADPH:oxygen oxidoreductase (13-hydroxylating)
Comments: The enzymes from the Gram-positive bacteria Streptomyces sp. C5 and Streptomyces peucetius show broad substrate specificity for structures based on an anthracycline aglycone, but have a strong preference for 4-methoxy anthracycline intermediates (13-deoxydaunorubicin and 13-dihydrodaunorubicin) over their 4-hydroxy analogues (13-deoxycarminomycin and 13-dihydrocarminomycin), as well as a preference for substrates hydroxylated at the C-13 rather than the C-14 position.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Walczak, R.J., Dickens, M.L., Priestley, N.D. and Strohl, W.R. Purification, properties, and characterization of recombinant Streptomyces sp. strain C5 DoxA, a cytochrome P-450 catalyzing multiple steps in doxorubicin biosynthesis. J. Bacteriol. 181 (1999) 298–304. [PMID: 9864343]
2.  Dickens, M.L., Priestley, N.D. and Strohl, W.R. In vivo and in vitro bioconversion of &epsilon;-rhodomycinone glycoside to doxorubicin: functions of DauP, DauK, and DoxA. J. Bacteriol. 179 (1997) 2641–2650. [DOI] [PMID: 9098063]
[EC 1.14.13.181 created 2013]
 
 
EC 1.14.13.205      
Transferred entry: long-chain fatty acid ω-monooxygenase. Now EC 1.14.14.80, long-chain fatty acid ω-monooxygenase
[EC 1.14.13.205 created 2015, deleted 2018]
 
 
EC 1.14.13.237     
Accepted name: aliphatic glucosinolate S-oxygenase
Reaction: an ω-(methylsulfanyl)alkyl-glucosinolate + NADPH + H+ + O2 = an ω-(methylsulfinyl)alkyl-glucosinolate + NADP+ + H2O
Glossary: ω-(methylsulfanyl)alkyl-glucosinolate = an ω-(methylsulfanyl)-N-sulfo-alkylhydroximate S-glucoside
Other name(s): ω-(methylthio)alkylglucosinolate S-oxygenase; GS-OX1 (gene name); ω-(methylthio)alkyl-glucosinolate,NADPH:oxygen S-oxidoreductase
Systematic name: ω-(methylsulfanyl)alkyl-glucosinolate,NADPH:oxygen S-oxidoreductase
Comments: The enzyme is a member of the flavin-dependent monooxygenase (FMO) family (cf. EC 1.14.13.8). The plant Arabidopsis thaliana contains five isoforms. GS-OX1 through GS-OX4 are able to catalyse the S-oxygenation independent of chain length, while GS-OX5 is specific for 8-(methylsulfanyl)octyl glucosinolate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hansen, B.G., Kliebenstein, D.J. and Halkier, B.A. Identification of a flavin-monooxygenase as the S-oxygenating enzyme in aliphatic glucosinolate biosynthesis in Arabidopsis. Plant J. 50 (2007) 902–910. [DOI] [PMID: 17461789]
2.  Li, J., Hansen, B.G., Ober, J.A., Kliebenstein, D.J. and Halkier, B.A. Subclade of flavin-monooxygenases involved in aliphatic glucosinolate biosynthesis. Plant Physiol. 148 (2008) 1721–1733. [DOI] [PMID: 18799661]
[EC 1.14.13.237 created 2017]
 
 
EC 1.14.14.36     
Accepted name: tyrosine N-monooxygenase
Reaction: L-tyrosine + 2 O2 + 2 [reduced NADPH—hemoprotein reductase] = (E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH—hemoprotein reductase] + CO2 + 3 H2O (overall reaction)
(1a) L-tyrosine + O2 + [reduced NADPH—hemoprotein reductase] = N-hydroxy-L-tyrosine + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) N-hydroxy-L-tyrosine + O2 + [reduced NADPH—hemoprotein reductase] = N,N-dihydroxy-L-tyrosine + [oxidized NADPH—hemoprotein reductase] + H2O
(1c) N,N-dihydroxy-L-tyrosine = (E)-[4-hydroxyphenylacetaldehyde oxime] + CO2 + H2O
For diagram of dhurrin biosynthesis, click here
Other name(s): tyrosine N-hydroxylase; CYP79A1
Systematic name: L-tyrosine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme from Sorghum is involved in the biosynthesis of the cyanogenic glucoside dhurrin. In Sinapis alba (white mustard) the enzyme is involved in the biosynthesis of the glucosinolate sinalbin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 159447-19-5
References:
1.  Halkier, B.A. and Møller, B.L. The biosynthesis of cyanogenic glucosides in higher plants. Identification of three hydroxylation steps in the biosynthesis of dhurrin in Sorghum bicolor (L.) Moench and the involvement of 1-ACI-nitro-2-(p-hydroxyphenyl)ethane as an intermediate. J. Biol. Chem. 265 (1990) 21114–21121. [PMID: 2250015]
2.  Sibbesen, O., Koch, B., Halkier, B.A. and Møller, B.L. Cytochrome P-450TYR is a multifunctional heme-thiolate enzyme catalyzing the conversion of L-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench. J. Biol. Chem. 270 (1995) 3506–3511. [DOI] [PMID: 7876084]
3.  Bennett, R.N., Kiddle, G. and Wallsgrove, R.M. Involvement of cytochrome P450 in glucosinolate biosynthesis in white mustard (a biochemical anomaly). Plant Physiol. 114 (1997) 1283–1291. [PMID: 12223771]
4.  Kahn, R.A., Fahrendorf, T., Halkier, B.A. and Møller, B.L. Substrate specificity of the cytochrome P450 enzymes CYP79A1 and CYP71E1 involved in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench. Arch. Biochem. Biophys. 363 (1999) 9–18. [DOI] [PMID: 10049494]
5.  Bak, S., Olsen, C.E., Halkier, B.A. and Møller, B.L. Transgenic tobacco and Arabidopsis plants expressing the two multifunctional sorghum cytochrome P450 enzymes, CYP79A1 and CYP71E1, are cyanogenic and accumulate metabolites derived from intermediates in Dhurrin biosynthesis. Plant Physiol. 123 (2000) 1437–1448. [PMID: 10938360]
6.  Nielsen, J.S. and Møller, B.L. Cloning and expression of cytochrome P450 enzymes catalyzing the conversion of tyrosine to p-hydroxyphenylacetaldoxime in the biosynthesis of cyanogenic glucosides in Triglochin maritima. Plant Physiol. 122 (2000) 1311–1321. [PMID: 10759528]
7.  Busk, P.K. and Møller, B.L. Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants. Plant Physiol. 129 (2002) 1222–1231. [DOI] [PMID: 12114576]
8.  Kristensen, C., Morant, M., Olsen, C.E., Ekstrøm, C.T., Galbraith, D.W., Møller, B.L. and Bak, S. Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome. Proc. Natl. Acad. Sci. USA 102 (2005) 1779–1784. [DOI] [PMID: 15665094]
9.  Clausen, M., Kannangara, R.M., Olsen, C.E., Blomstedt, C.K., Gleadow, R.M., Jørgensen, K., Bak, S., Motawie, M.S. and Møller, B.L. The bifurcation of the cyanogenic glucoside and glucosinolate biosynthetic pathways. Plant J. 84 (2015) 558–573. [DOI] [PMID: 26361733]
[EC 1.14.14.36 created 1992 as EC 1.14.13.41, modified 2001, modified 2005, transferred 2016 to EC 1.14.14.36]
 
 
EC 1.14.14.37     
Accepted name: 4-hydroxyphenylacetaldehyde oxime monooxygenase
Reaction: (E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH—hemoprotein reductase] + O2 = (S)-4-hydroxymandelonitrile + [oxidized NADPH—hemoprotein reductase] + 2 H2O (overall reaction)
(1a) (E)-4-hydroxyphenylacetaldehyde oxime = (Z)-4-hydroxyphenylacetaldehyde oxime
(1b) (Z)-4-hydroxyphenylacetaldehyde oxime = 4-hydroxyphenylacetonitrile + H2O
(1c) 4-hydroxyphenylacetonitrile + [reduced NADPH—hemoprotein reductase] + O2 = (S)-4-hydroxymandelonitrile + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of dhurrin biosynthesis, click here
Glossary: (S)-4-hydroxymandelonitrile = (2S)-hydroxy(4-hydroxyphenyl)acetonitrile
Other name(s): 4-hydroxybenzeneacetaldehyde oxime monooxygenase; cytochrome P450II-dependent monooxygenase; NADPH-cytochrome P450 reductase (CYP71E1); CYP71E1; 4-hydroxyphenylacetaldehyde oxime,NADPH:oxygen oxidoreductase
Systematic name: (E)-4-hydroxyphenylacetaldehyde oxime,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase
Comments: This cytochrome P-450 (heme thiolate) enzyme is involved in the biosynthesis of the cyanogenic glucoside dhurrin in sorghum. It catalyses three different activities - isomerization of the (E) isomer to the (Z) isomer, dehydration, and C-hydroxylation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  MacFarlane, I.J., Lees, E.M. and Conn, E.E. The in vitro biosynthesis of dhurrin, the cyanogenic glycoside of Sorghum bicolor. J. Biol. Chem. 250 (1975) 4708–4713. [PMID: 237909]
2.  Shimada, M. and Conn, E.E. The enzymatic conversion of p-hydroxyphenylacetaldoxime to p-hydroxymandelonitrile. Arch. Biochem. Biophys. 180 (1977) 199–207. [DOI] [PMID: 193443]
3.  Busk, P.K. and Møller, B.L. Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants. Plant Physiol. 129 (2002) 1222–1231. [DOI] [PMID: 12114576]
4.  Kristensen, C., Morant, M., Olsen, C.E., Ekstrøm, C.T., Galbraith, D.W., Møller, B.L. and Bak, S. Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome. Proc. Natl. Acad. Sci. USA 102 (2005) 1779–1784. [DOI] [PMID: 15665094]
5.  Clausen, M., Kannangara, R.M., Olsen, C.E., Blomstedt, C.K., Gleadow, R.M., Jørgensen, K., Bak, S., Motawie, M.S. and Møller, B.L. The bifurcation of the cyanogenic glucoside and glucosinolate biosynthetic pathways. Plant J. 84 (2015) 558–573. [DOI] [PMID: 26361733]
[EC 1.14.14.37 created 2000 as EC 1.14.13.68, modified 2005, transferred 2016 to EC 1.14.14.37]
 
 
EC 1.14.14.40     
Accepted name: phenylalanine N-monooxygenase
Reaction: L-phenylalanine + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = (E)-phenylacetaldoxime + 2 [oxidized NADPH—hemoprotein reductase] + CO2 + 3 H2O (overall reaction)
(1a) L-phenylalanine + [reduced NADPH—hemoprotein reductase] + O2 = N-hydroxy-L-phenylalanine + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) N-hydroxy-L-phenylalanine + [reduced NADPH—hemoprotein reductase] + O2 = N,N-dihydroxy-L-phenylalanine + [oxidized NADPH—hemoprotein reductase] + H2O
(1c) N,N-dihydroxy-L-phenylalanine = (E)-phenylacetaldoxime + CO2 + H2O
Other name(s): phenylalanine N-hydroxylase; CYP79A2 (gene name); CYP79D16 (gene name)
Systematic name: L-phenylalanine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating)
Comments: This cytochrome P-450 (heme-thiolate) enzyme, found in plants, catalyses two successive N-hydroxylations of L-phenylalanine, a committed step in the biosynthesis of benzylglucosinolate and the cyanogenic glucosides (R)-prunasin and (R)-amygdalin. The product of the two hydroxylations, N,N-dihydroxy-L-phenylalanine, is labile and undergoes dehydration followed by decarboxylation, producing 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.  Wittstock, U. and Halkier, B.A. Cytochrome P450 CYP79A2 from Arabidopsis thaliana L. Catalyzes the conversion of L-phenylalanine to phenylacetaldoxime in the biosynthesis of benzylglucosinolate. J. Biol. Chem. 275 (2000) 14659–14666. [DOI] [PMID: 10799553]
2.  Yamaguchi, T., Yamamoto, K. and Asano, Y. Identification and characterization of CYP79D16 and CYP71AN24 catalyzing the first and second steps in L-phenylalanine-derived cyanogenic glycoside biosynthesis in the Japanese apricot, Prunus mume Sieb. et Zucc. Plant Mol. Biol. 86 (2014) 215–223. [DOI] [PMID: 25015725]
[EC 1.14.14.40 created 2011 as EC 1.14.13.124, transferred 2017 to EC 1.14.14.40]
 
 
EC 1.14.14.42     
Accepted name: homomethionine N-monooxygenase
Reaction: an L-polyhomomethionine + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = an (E)-ω-(methylsulfanyl)alkanal oxime + 2 [oxidized NADPH—hemoprotein reductase] + CO2 + 3 H2O (overall reaction)
(1a) an L-polyhomomethionine + [reduced NADPH—hemoprotein reductase] + O2 = an L-N-hydroxypolyhomomethionine + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) an L-N-hydroxypolyhomomethionine + [reduced NADPH—hemoprotein reductase] + O2 = an L-N,N-dihydroxypolyhomomethionine + [oxidized NADPH—hemoprotein reductase] + H2O
(1c) an L-N,N-dihydroxypolyhomomethionine = an (E)-ω-(methylsulfanyl)alkanal oxime + CO2 + H2O
Glossary: homomethionine = (2S)-2-amino-5-(methylsulfanyl)pentanoate
an L-polyhomomethionine = analogs of L-methionine that contain additional methylene groups in the side chain prior to the sulfur atom.
Other name(s): CYP79F1 (gene name); CYP79F2 (gene name)
Systematic name: L-polyhomomethionine,[NADPH—hemoprotein reductase]:oxygen oxidoreductase
Comments: This plant cytochrome P-450 (heme thiolate) enzyme is involved in methionine-derived aliphatic glucosinolates biosynthesis. It catalyses two successive N-hydroxylations, which are followed by dehydration and decarboxylation. CYP79F1 from Arabidopsis thaliana can metabolize mono-, di-, tri-, tetra-, penta-, and hexahomomethionine to their corresponding aldoximes, while CYP79F2 from the same plant can only metabolize penta- and hexahomomethionine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hansen, C.H., Wittstock, U., Olsen, C.E., Hick, A.J., Pickett, J.A. and Halkier, B.A. Cytochrome p450 CYP79F1 from arabidopsis catalyzes the conversion of dihomomethionine and trihomomethionine to the corresponding aldoximes in the biosynthesis of aliphatic glucosinolates. J. Biol. Chem. 276 (2001) 11078–11085. [DOI] [PMID: 11133994]
2.  Chen, S., Glawischnig, E., Jørgensen, K., Naur, P., Jorgensen, B., Olsen, C.E., Hansen, C.H., Rasmussen, H., Pickett, J.A. and Halkier, B.A. CYP79F1 and CYP79F2 have distinct functions in the biosynthesis of aliphatic glucosinolates in Arabidopsis. Plant J. 33 (2003) 923–937. [DOI] [PMID: 12609033]
[EC 1.14.14.42 created 2017]
 
 
EC 1.14.14.43     
Accepted name: (methylsulfanyl)alkanaldoxime N-monooxygenase
Reaction: an (E)-ω-(methylsulfanyl)alkanal oxime + [reduced NADPH—hemoprotein reductase] + glutathione + O2 = an S-[(1E)-1-(hydroxyimino)-ω-(methylsulfanyl)alkyl]-L-glutathione + [oxidized NADPH—hemoprotein reductase] + 2 H2O (overall reaction)
(1a) an (E)-ω-(methylsulfanyl)alkanal oxime + [reduced NADPH—hemoprotein reductase] + O2 = a 1-(methylsulfanyl)-4-aci-nitroalkane + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) a 1-(methylsulfanyl)-4-aci-nitroalkane + glutathione = an S-[(1E)-1-(hydroxyimino)-ω-(methylsulfanyl)alkyl]-L-glutathione + H2O
Glossary: a 1-(methylsulfanyl)-4-aci-nitroalkane = a hydroxyoxo-λ5-azanylidene-ω-(methylsulfanyl)alkane
Other name(s): CYP83A1 (gene name); (methylthio)alkanaldoxime N-monooxygenase; (E)-ω-(methylthio)alkananaldoxime,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating)
Systematic name: (E)-ω-(methylsulfanyl)alkananal oxime,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating)
Comments: This cytochrome P-450 (heme thiolate) enzyme is involved in the biosynthesis of glucosinolates in plants. The enzyme catalyses an N-hydroxylation of the E isomer of ω-(methylsulfanyl)alkanal oximes, forming an aci-nitro intermediate that reacts non-enzymically with glutathione to produce an N-alkyl-thiohydroximate adduct, the committed precursor of glucosinolates. In the absence of a thiol compound, the enzyme is suicidal, probably due to interaction of the reactive aci-nitro intermediate with active site residues.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bak, S., Tax, F.E., Feldmann, K.A., Galbraith, D.W. and Feyereisen, R. CYP83B1, a cytochrome P450 at the metabolic branch point in auxin and indole glucosinolate biosynthesis in Arabidopsis. Plant Cell 13 (2001) 101–111. [PMID: 11158532]
2.  Naur, P., Petersen, B.L., Mikkelsen, M.D., Bak, S., Rasmussen, H., Olsen, C.E. and Halkier, B.A. CYP83A1 and CYP83B1, two nonredundant cytochrome P450 enzymes metabolizing oximes in the biosynthesis of glucosinolates in Arabidopsis. Plant Physiol. 133 (2003) 63–72. [DOI] [PMID: 12970475]
3.  Clausen, M., Kannangara, R.M., Olsen, C.E., Blomstedt, C.K., Gleadow, R.M., Jørgensen, K., Bak, S., Motawie, M.S. and Møller, B.L. The bifurcation of the cyanogenic glucoside and glucosinolate biosynthetic pathways. Plant J. 84 (2015) 558–573. [DOI] [PMID: 26361733]
[EC 1.14.14.43 created 2017]
 
 
EC 1.14.14.45     
Accepted name: aromatic aldoxime N-monooxygenase
Reaction: (1) (E)-indol-3-ylacetaldehyde oxime + [reduced NADPH—hemoprotein reductase] + glutathione + O2 = S-[(E)-N-hydroxy(indol-3-yl)acetimidoyl]-L-glutathione + [oxidized NADPH—hemoprotein reductase] + 2 H2O (overall reaction)
(1a) (E)-indol-3-ylacetaldehyde oxime + [reduced NADPH—hemoprotein reductase] + O2 = 1-(1H-indol-3-yl)-2-aci-nitroethane + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) 1-(1H-indol-3-yl)-2-aci-nitroethane + glutathione = S-[(E)-N-hydroxy(indol-3-yl)acetimidoyl]-L-glutathione + H2O (spontaneous)
(2) (E)-phenylacetaldehyde oxime + [reduced NADPH—hemoprotein reductase] + glutathione + O2 = S-[(Z)-N-hydroxy(phenyl)acetimidoyl]-L-glutathione + [oxidized NADPH—hemoprotein reductase] + 2 H2O (overall reaction)
(2a) (E)-phenylacetaldehyde oxime + [reduced NADPH—hemoprotein reductase] + O2 = 1-aci-nitro-2-phenylethane + [oxidized NADPH—hemoprotein reductase] + H2O
(2b) 1-aci-nitro-2-phenylethane + glutathione = S-[(Z)-N-hydroxy(phenyl)acetimidoyl]-L-glutathione + H2O (spontaneous)
Other name(s): CYP83B1 (gene name)
Systematic name: (E)-indol-3-ylacetaldoxime,[reduced NADPH—hemoprotein reductase],glutathione:oxygen oxidoreductase (oxime-hydroxylating)
Comments: This cytochrome P-450 (heme thiolate) enzyme is involved in the biosynthesis of glucosinolates in plants. The enzyme catalyses the N-hydroxylation of aromatic aldoximes derived from L-tryptophan, L-phenylalanine, and L-tyrosine, forming an aci-nitro intermediate that reacts non-enzymically with glutathione to produce an N-alkyl-thiohydroximate adduct, the committed precursor of glucosinolates. In the absence of glutathione, the enzyme is suicidal, probably due to interaction of the reactive aci-nitro compound with catalytic residues in the active site.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bak, S., Tax, F.E., Feldmann, K.A., Galbraith, D.W. and Feyereisen, R. CYP83B1, a cytochrome P450 at the metabolic branch point in auxin and indole glucosinolate biosynthesis in Arabidopsis. Plant Cell 13 (2001) 101–111. [PMID: 11158532]
2.  Naur, P., Petersen, B.L., Mikkelsen, M.D., Bak, S., Rasmussen, H., Olsen, C.E. and Halkier, B.A. CYP83A1 and CYP83B1, two nonredundant cytochrome P450 enzymes metabolizing oximes in the biosynthesis of glucosinolates in Arabidopsis. Plant Physiol. 133 (2003) 63–72. [DOI] [PMID: 12970475]
3.  Geu-Flores, F., Møldrup, M.E., Böttcher, C., Olsen, C.E., Scheel, D. and Halkier, B.A. Cytosolic γ-glutamyl peptidases process glutathione conjugates in the biosynthesis of glucosinolates and camalexin in Arabidopsis. Plant Cell 23 (2011) 2456–2469. [DOI] [PMID: 21712415]
[EC 1.14.14.45 created 2017]
 
 


Data © 2001–2022 IUBMB
Web site © 2005–2022 Andrew McDonald