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Displaying entries 51-100 of 580.
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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 | ||||||||||||||||||
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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, PDB | ||||||||||||||||||
References: |
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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) |
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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, PDB, CAS registry number: 37256-58-9 | ||||||||||||||||||
References: |
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EC | 1.13.11.32 | ||||||||||||||||||
Transferred entry: | 2-nitropropane dioxygenase. Now EC 1.13.12.16, nitronate monooxygenase | ||||||||||||||||||
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 |
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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, PDB, CAS registry number: 199877-10-6 | ||||||||||||||||||
References: |
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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, PDB | ||||||||||||||||||
References: |
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EC | 1.13.11.59 | ||||||||||||||||||
Accepted name: | torulene dioxygenase | ||||||||||||||||||
Reaction: | torulene + O2 = 4′-apo-β,ψ-caroten-4′-al + 3-methylbut-2-enal | ||||||||||||||||||
Glossary: | torulene = 3′,4′-didehydro-β,ψ-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: |
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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: |
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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: |
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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: |
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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, PDB | ||||||||||||||||||
References: |
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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, PDB | ||||||||||||||||||
References: |
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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 |
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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 |
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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: |
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EC | 1.13.12.14 | ||||||||||||||||||
Transferred entry: | chlorophyllide-a oxygenase. Now EC 1.14.13.122, chlorophyllide-a oxygenase | ||||||||||||||||||
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, PDB | ||||||||||||||||||
References: |
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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 |
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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 |
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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: |
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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: |
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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: |
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EC | 1.14.11.19 | ||||||||||||||||||
Transferred entry: | anthocyanidin synthase. Now EC 1.14.20.4, anthocyanidin synthase | ||||||||||||||||||
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 |
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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: |
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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, PDB | ||||||||||||||||||
References: |
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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 |
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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: |
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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 |
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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: |
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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 |
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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 iron(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: |
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EC | 1.14.12.20 | ||||||||||||||||||
Transferred entry: | pheophorbide a oxygenase. Now classified as EC 1.14.15.17, pheophorbide a oxygenase. | ||||||||||||||||||
EC | 1.14.13.41 | ||||||||||||||||||
Transferred entry: | tyrosine N-monooxygenase. Now EC 1.14.14.36, tyrosine N-monooxygenase | ||||||||||||||||||
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, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 134214-78-1 | ||||||||||||||||||
References: |
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EC | 1.14.13.68 | ||||||||||||||||||
Transferred entry: | 4-hydroxyphenylacetaldehyde oxime monooxygenase. Now EC 1.14.14.37, 4-hydroxyphenylacetaldehyde oxime monooxygenase | ||||||||||||||||||
EC | 1.14.13.78 | ||||||||||||||||||
Transferred entry: | ent-kaurene oxidase. Now EC 1.14.14.86, ent-kaurene monooxygenase | ||||||||||||||||||
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 |
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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 iron(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: |
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EC | 1.14.13.88 | ||||||||||||||||||
Transferred entry: | flavanoid 3,5-hydroxylase. Now EC 1.14.14.81, flavanoid 3,5-hydroxylase | ||||||||||||||||||
EC | 1.14.13.101 | ||||||||||||||||||
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: |
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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 | 1.14.13.119 | ||||||||||||||||||
Transferred entry: | 5-epiaristolochene 1,3-dihydroxylase. Now EC 1.14.14.149, 5-epiaristolochene 1,3-dihydroxylase | ||||||||||||||||||
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+ |
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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: |
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EC | 1.14.13.124 | ||||||||||||||||||
Transferred entry: | phenylalanine N-monooxygenase, now classified as EC 1.14.14.40, phenylalanine N-monooxygenase | ||||||||||||||||||
EC | 1.14.13.125 | ||||||||||||||||||
Transferred entry: | tryptophan N-monooxygenase. Now EC 1.14.14.156, tryptophan N-monooxygenase | ||||||||||||||||||
EC | 1.14.13.129 | ||||||||||||||||||
Transferred entry: | β-carotene 3-hydroxylase. Now EC 1.14.15.24, β-carotene 3-hydroxylase. | ||||||||||||||||||
EC | 1.14.13.168 | ||||||||||||||||||
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: |
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EC | 1.14.13.169 | ||||||||||||||||||
Transferred entry: | sphinganine C4-monooxygenase. Now EC 1.14.18.5, sphingolipid C4-monooxygenase | ||||||||||||||||||
EC | 1.14.13.180 | ||||||||||||||||||
Accepted name: | aklavinone 12-hydroxylase | ||||||||||||||||||
Reaction: | aklavinone + NADPH + H+ + O2 = ε-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 ε-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 |
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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, PDB | ||||||||||||||||||
References: |
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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 |
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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 |
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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: |
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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 | 1.14.13.237 | ||||||||||||||||||
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: |
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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 |
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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: |
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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 |
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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: |
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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 |
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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: |
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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 |
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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. |
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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: |
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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 |
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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: |
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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) |
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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: |
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