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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 |
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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 | ||||||||||||||
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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 | ||||||||||||||
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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 | ||||||||||||||
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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 | ||||||||||||||
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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 |
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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 | ||||||||||||||
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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 | ||||||||||||||
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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 |
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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: |
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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 | ||||||||||||||
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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 | ||||||||||||||
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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 |
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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 | ||||||||||||||
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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 | ||||||||||||||
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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 |
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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 | ||||||||||||||
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EC | 1.14.14.158 | ||||||||||||||
Accepted name: | carotenoid ε 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 |
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For diagram of lutein biosynthesis, click here | |||||||||||||||
Other name(s): | CYP97C1; LUT1; CYP97C; carotene ε-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: |
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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 |
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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 | ||||||||||||||
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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] |
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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 | ||||||||||||||
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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] |
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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 | ||||||||||||||
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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 | ||||||||||||||
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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) |
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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-ψ,ψ-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: |
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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) |
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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: |
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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 |
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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: |
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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: |
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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: |
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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: |
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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: |
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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 |
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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: |
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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 |
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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: |
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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: |
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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: |
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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: |
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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: |
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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] |
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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: |
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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 |
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Glossary: | a (4R)-4-hydroxysphinganine-ceramide = a phytoceramide (4R)-4-hydroxysphinganine = phytosphinganine |
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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: |
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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 |
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Glossary: | (9Z,12Z)-octadeca-9,12-dienoyl-[glycerolipid] = linoleoyl-[glycerolipid] (9Z,12Z,15Z)-octadeca-9,12,15-trienoyl-[glycerolipid] = α-linolenoyl-[glycerolipid] |
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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: |
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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 |
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Glossary: | (5Z,11Z,14Z)-icosa-5,11,14-trienoate = sciadonate (5Z,11Z,14Z,17Z)-icosa-5,11,14,17-tetraenoate = juniperonate |
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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: |
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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 | ||||||||||||||
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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 | ||||||||||||||
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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 | ||||||||||||||
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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 |
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Glossary: | camalexin = 3-(thiazol-2-yl)indole (R)-dihydrocamalexate = (4R)-2-(1H-indol-3-yl)-4,5-dihydrothiazole-4-carboxylate |
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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 | ||||||||||||||
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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 |
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Other name(s): | ADS2 (gene name) | ||||||||||||||
Systematic name: | very-long-chain acyl-[glycerolipid],ferrocytochrome b5:oxygen oxidoreductase (ω9,ω8-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 | ||||||||||||||
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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 |
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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 | ||||||||||||||
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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 |
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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: |
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EC | 1.14.99.45 | ||||||||||||||
Transferred entry: | carotene ε-monooxygenase. Now EC 1.14.14.158, carotene ε-monooxygenase | ||||||||||||||
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 | ||||||||||||||
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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: |
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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 |
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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 | ||||||||||||||
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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 |
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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 |
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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 | ||||||||||||||
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EC | 1.16.5.1 | ||||||||||||||
Transferred entry: | ascorbate ferrireductase (transmembrane). Now EC 7.2.1.3, ascorbate ferrireductase (transmembrane) | ||||||||||||||
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: |
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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: |
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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) |
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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 | ||||||||||||||
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