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Your query returned 22 entries. Printable version
EC | 1.1.1.423 | Relevance: 100% | ||||||||||||
Accepted name: | (1R,2S)-ephedrine 1-dehydrogenase | |||||||||||||
Reaction: | (–)-(1R,2S)-ephedrine + NAD+ = (S)-2-(methylamino)-1-phenylpropan-1-one + NADH + H+ | |||||||||||||
Glossary: | (–)-(1R,2S)-ephedrine = (1R,2S)-2-(methylamino)-1-phenylpropan-1-ol (S)-2-(methylamino)-1-phenylpropan-1-one = (S)-methcathinone |
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Other name(s): | EDH; ephedrine dehydrogenase | |||||||||||||
Systematic name: | (–)-(1R,2S)-ephedrine:NAD+ 1-oxidoreductase | |||||||||||||
Comments: | The enzyme, characterized from the bacterium Arthrobacter sp. TS-15, acts on a broad range of different aryl-alkyl ketones, such as haloketones, ketoamines, diketones, and ketoesters. It exhibits a strict enantioselectivity and accepts various types of aryl groups including phenyl-, pyridyl-, thienyl-, and furyl-rings, but the presence of an aromatic ring is essential for the activity. In addition, the presence of a functional group on the alkyl chain, such as an amine, a halogen, or a ketone, is also crucial. When acting on diketones, it catalyses the reduction of only the keto group closest to the ring, with no further reduction to the diol. cf. EC 1.1.1.422, pseudoephedrine dehydrogenase and EC 1.5.1.18, ephedrine dehydrogenase. | |||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||
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EC | 1.1.1.422 | Relevance: 99.3% | ||||||||||||
Accepted name: | pseudoephedrine dehydrogenase | |||||||||||||
Reaction: | (+)-(1S,2S)-pseudoephedrine + NAD+ = (S)-2-(methylamino)-1-phenylpropan-1-one + NADH + H+ | |||||||||||||
Glossary: | (+)-(1S,2S)-pseudoephedrine = (1S,2S)-2-(methylamino)-1-phenylpropan-1-ol (S)-2-(methylamino)-1-phenylpropan-1-one = (S)-methcathinone |
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Other name(s): | PseDH | |||||||||||||
Systematic name: | (+)-(1S,2S)-pseudoephedrine:NAD+ 1-oxidoreductase | |||||||||||||
Comments: | The enzyme, characterized from the bacterium Arthrobacter sp. TS-15, acts on a broad range of different aryl-alkyl ketones, such as haloketones, ketoamines, diketones, and ketoesters. It accepts various types of aryl groups including phenyl-, pyridyl-, thienyl-, and furyl-rings, but the presence of an aromatic ring is essential for the activity. In addition, the presence of a functional group on the alkyl chain, such as an amine, a halogen, or a ketone, is also crucial. The enzyme exhibits a strict anti-Prelog enantioselectivity. When acting on diketones, it catalyses the reduction of only the keto group closest to the ring, with no further reduction to the diol. cf. EC 1.1.1.423, ephedrine dehydrogenase. | |||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||
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EC | 1.5.99.14 | Relevance: 63.4% | ||||||||||||
Accepted name: | 6-hydroxypseudooxynicotine dehydrogenase | |||||||||||||
Reaction: | 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + acceptor + H2O = 1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one + reduced acceptor | |||||||||||||
For diagram of nicotine catabolism by arthrobacter, click here | ||||||||||||||
Glossary: | 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one = 6-hydroxypseudooxynicotine 1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one = 2,6-dihydroxypseudooxynicotine |
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Systematic name: | 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one:acceptor 6-oxidoreductase (hydroxylating) | |||||||||||||
Comments: | Contains a cytidylyl molybdenum cofactor [3]. The enzyme, which participates in the nicotine degradation pathway, has been characterized from the soil bacterium Arthrobacter nicotinovorans [1,2]. | |||||||||||||
Links to other databases: | BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB | |||||||||||||
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EC | 1.5.1.18 | Relevance: 63.3% | ||||||||||||
Accepted name: | ephedrine dehydrogenase | |||||||||||||
Reaction: | (-)-ephedrine + NAD+ = (R)-2-methylimino-1-phenylpropan-1-ol + NADH + H+ | |||||||||||||
Systematic name: | (-)-ephedrine:NAD+ 2-oxidoreductase | |||||||||||||
Comments: | The product immediately hydrolyses to methylamine and 1-hydroxy-1-phenylpropan-2-one. Acts on a number of related compounds including (-)-sympatol, (+)-pseudoephedrine and (+)-norephedrine. | |||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 73508-06-2 | |||||||||||||
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EC | 3.7.1.19 | Relevance: 54.8% | ||||||||||||
Accepted name: | 2,6-dihydroxypseudooxynicotine hydrolase | |||||||||||||
Reaction: | 1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O = 2,6-dihydroxypyridine + 4-methylaminobutanoate | |||||||||||||
For diagram of nicotine catabolism by arthrobacter, click here | ||||||||||||||
Glossary: | 1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one = 2,6-dihydroxypseudooxynicotine | |||||||||||||
Systematic name: | 1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one hydrolase | |||||||||||||
Comments: | The enzyme, characterized from the soil bacterium Arthrobacter nicotinovorans, participates in nicotine degradation. | |||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | |||||||||||||
References: |
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EC | 1.4.3.24 | |||||||||||||
Transferred entry: | pseudooxynicotine oxidase, now classified as EC 1.4.2.3, pseudooxynicotine dehydrogenase | |||||||||||||
EC | 1.4.2.3 | Relevance: 44.7% | ||||||||||||
Accepted name: | pseudooxynicotine dehydrogenase | |||||||||||||
Reaction: | pseudooxynicotine + H2O + 2 ferricytochrome c = 4-oxo-4-(pyridin-3-yl)butanal + methylamine + 2 ferrocytochrome c + 2 H+ | |||||||||||||
Glossary: | pseudooxynicotine = 4-(methylamino)-1-(pyridin-3-yl)butan-1-one | |||||||||||||
Other name(s): | pnaO (gene name) | |||||||||||||
Systematic name: | 4-(methylamino)-1-(pyridin-3-yl)butan-1-one:c-type cytochrome oxidoreductase (methylamine releasing) | |||||||||||||
Comments: | Contains one non-covalently bound FAD molecule per dimer. This enzyme, characterized from the soil bacteria Pseudomonas sp. HZN6 and Pseudomonas putida S16, is involved in nicotine degradation. | |||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||
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EC | 2.1.1.335 | Relevance: 44.1% | ||||||||||||
Accepted name: | 4-amino-anhydrotetracycline N4-methyltransferase | |||||||||||||
Reaction: | (1) S-adenosyl-L-methionine + 4-amino-4-de(dimethylamino)anhydrotetracycline = S-adenosyl-L-homocysteine + 4-methylamino-4-de(dimethylamino)anhydrotetracycline (2) S-adenosyl-L-methionine + 4-methylamino-4-de(dimethylamino)anhydrotetracycline = S-adenosyl-L-homocysteine + anhydrotetracycline |
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Glossary: | 4-amino-4-de(dimethylamino)anhydrotetracycline = (4S,4aS,12aS)-4-amino-3,10,11,12a-tetrahydroxy-6-methyl-1,12-dioxo-4a,5-dihydro-4H-tetracene-2-carboxamide 4-methylamino-4-de(dimethylamino)anhydrotetracycline = (4S,4aS,12aS)-3,10,11,12a-tetrahydroxy-6-methyl-4-(methylamino)-1,12-dioxo-4a,5-dihydro-4H-tetracene-2-carboxamide anhydrotetracycline = (4S,4aS,12aS)-4-(dimethylamino)-3,10,11,12a-tetrahydroxy-6-methyl-1,12-dioxo-1,4,4a,5,12,12a-hexahydrotetracene-2-carboxamide |
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Other name(s): | oxyT (gene name); ctcO (gene name) | |||||||||||||
Systematic name: | S-adenosyl-L-methionine:(4S,4aS,12aS)-4-amino-3,10,11,12a-tetrahydroxy-6-methyl-1,12-dioxo-4a,5-dihydro-4H-tetracene-2-carboxamide Nα-methyltransferase | |||||||||||||
Comments: | The enzyme, characterized from the bacterium Streptomyces rimosus, participates in the biosynthesis of tetracycline antibiotics. | |||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||
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EC | 1.1.1.332 | Relevance: 43.3% | ||||||||||||
Accepted name: | chanoclavine-I dehydrogenase | |||||||||||||
Reaction: | chanoclavine-I + NAD+ = chanoclavine-I aldehyde + NADH + H+ | |||||||||||||
Glossary: | chanoclavine-I = (1E)-2-methyl-3-[(4R,5R)-4-(methylamino)-1,3,4,5-tetrahydrobenz[cd]indol-5-yl]prop-2-en-1-ol chanoclavine-I aldehyde = (1E)-2-methyl-3-[(4R,5R)-4-(methylamino)-1,3,4,5-tetrahydrobenz[cd]indol-5-yl]prop-2-enal |
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Other name(s): | easD (gene name); fgaDH (gene name) | |||||||||||||
Systematic name: | chanoclavine-I:NAD+ oxidoreductase | |||||||||||||
Comments: | The enzyme catalyses a step in the pathway of ergot alkaloid biosynthesis in certain fungi. | |||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||
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EC | 1.5.3.6 | Relevance: 41.7% | ||||||||||||
Accepted name: | (R)-6-hydroxynicotine oxidase | |||||||||||||
Reaction: | (R)-6-hydroxynicotine + H2O + O2 = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2 (overall reaction) (1a) (R)-6-hydroxynicotine + O2 = 5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol + H2O2 (1b) 5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol + H2O = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one (spontaneous) |
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For diagram of nicotine catabolism by arthrobacter, click here | ||||||||||||||
Glossary: | (R)-6-hydroxynicotine = 5-[(2R)-1-methylpyrrolidin-2-yl]pyridin-2-ol 5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol = 6-hydroxy-N-methylmyosmine 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one = 6-hydroxypseudooxynicotine |
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Other name(s): | D-6-hydroxynicotine oxidase; 6-hydroxy-D-nicotine oxidase | |||||||||||||
Systematic name: | (R)-6-hydroxynicotine:oxygen oxidoreductase | |||||||||||||
Comments: | A flavoprotein (FAD). The enzyme, which participates in nicotine degradation, is specific for (R) isomer of 6-hydroxynicotine, derived from the uncommon (R)-nicotine. The bacterium Arthrobacter nicotinovorans, in which this enzyme was originally discovered, has a different enzyme that catalyses a similar reaction with the (S)-isomer (cf. EC 1.5.3.5, (S)-6-hydroxynicotine oxidase). | |||||||||||||
Links to other databases: | BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37233-46-8 | |||||||||||||
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EC | 1.5.3.5 | Relevance: 40.5% | ||||||||||||
Accepted name: | (S)-6-hydroxynicotine oxidase | |||||||||||||
Reaction: | (S)-6-hydroxynicotine + H2O + O2 = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2 (overall reaction) (1a) (S)-6-hydroxynicotine + O2 = 5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol + H2O2 (1b) 5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol + H2O = 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one (spontaneous) |
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For diagram of nicotine catabolism by arthrobacter, click here | ||||||||||||||
Glossary: | (S)-6-hydroxynicotine = 5-[(2S)-1-methylpyrrolidin-2-yl]pyridin-2-ol 1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one = 6-hydroxypseudooxynicotine 5-(N-methyl-4,5-dihydro-1H-pyrrol-2-yl)pyridin-2-ol = 6-hydroxy-N-methylmyosmine |
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Other name(s): | L-6-hydroxynicotine oxidase; 6-hydroxy-L-nicotine oxidase; 6-hydroxy-L-nicotine:oxygen oxidoreductase; nctB (gene name) | |||||||||||||
Systematic name: | (S)-6-hydroxynicotine:oxygen oxidoreductase | |||||||||||||
Comments: | A flavoprotein (FAD). The enzyme, which participates in nicotine degradation, is specific for the (S) isomer of 6-hydroxynicotine. The bacterium Arthrobacter nicotinovorans, in which this enzyme was originally discovered, has a different enzyme that catalyses a similar reaction with the less common (R)-isomer (cf. EC 1.5.3.6, (R)-6-hydroxynicotine oxidase). | |||||||||||||
Links to other databases: | BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-29-4 | |||||||||||||
References: |
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EC | 2.1.1.343 | Relevance: 36.6% | ||||||||||||
Accepted name: | 8-amino-8-demethylriboflavin N,N-dimethyltransferase | |||||||||||||
Reaction: | 2 S-adenosyl-L-methionine + 8-amino-8-demethylriboflavin = 2 S-adenosyl-L-homocysteine + roseoflavin (overall reaction) (1a) S-adenosyl-L-methionine + 8-amino-8-demethylriboflavin = S-adenosyl-L-homocysteine + 8-demethyl-8-(methylamino)riboflavin (1b) S-adenosyl-L-methionine + 8-demethyl-8-(methylamino)riboflavin = S-adenosyl-L-homocysteine + roseoflavin |
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For diagram of roseoflavin biosynthesis, click here | ||||||||||||||
Glossary: | roseoflavin = 8-demethyl-8-(dimethylamino)riboflavin | |||||||||||||
Other name(s): | rosA (gene name) | |||||||||||||
Systematic name: | S-adenosyl-L-methionine:8-amino-8-demethylriboflavin N,N-dimethyltransferase | |||||||||||||
Comments: | The enzyme, characterized from the soil bacterium Streptomyces davawensis, catalyses the last two steps in the biosynthesis of the antibiotic roseoflavin. | |||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | |||||||||||||
References: |
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EC | 2.1.1.61 | Relevance: 36.5% | ||||||||||||
Accepted name: | tRNA 5-(aminomethyl)-2-thiouridylate-methyltransferase | |||||||||||||
Reaction: | S-adenosyl-L-methionine + tRNA containing 5-(aminomethyl)-2-thiouridine = S-adenosyl-L-homocysteine + tRNA containing 5-[(methylamino)methyl]-2-thiouridylate | |||||||||||||
Other name(s): | transfer ribonucleate 5-methylaminomethyl-2-thiouridylate 5-methyltransferase; tRNA 5-methylaminomethyl-2-thiouridylate 5′-methyltransferase; S-adenosyl-L-methionine:tRNA (5-methylaminomethyl-2-thio-uridylate)-methyltransferase; tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase | |||||||||||||
Systematic name: | S-adenosyl-L-methionine:tRNA 5-(aminomethyl)-2-thiouridylate N-methyltransferase | |||||||||||||
Comments: | This enzyme specifically adds the terminal methyl group of 5-[(methylamino)methyl]-2-thiouridylate. | |||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 39391-17-8 | |||||||||||||
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EC | 2.1.1.324 | Relevance: 31.6% | ||||||||||||
Accepted name: | dTDP-4-amino-2,3,4,6-tetradeoxy-D-glucose N,N-dimethyltransferase | |||||||||||||
Reaction: | 2 S-adenosyl-L-methionine + dTDP-4-amino-2,3,4,6-tetradeoxy-α-D-erythro-hexopyranose = 2 S-adenosyl-L-homocysteine + dTDP-α-D-forosamine (overall reaction) (1a) S-adenosyl-L-methionine + dTDP-4-amino-2,3,4,6-tetradeoxy-α-D-erythro-hexopyranose = S-adenosyl-L-homocysteine + dTDP-4-(methylamino)-2,3,4,6-tetradeoxy-α-D-erythro-hexopyranose (1b) S-adenosyl-L-methionine + dTDP-4-(methylamino)-2,3,4,6-tetradeoxy-α-D-erythro-hexopyranose = S-adenosyl-L-homocysteine + dTDP-α-D-forosamine |
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For diagram of dTDP-forosamine biosynthesis, click here | ||||||||||||||
Glossary: | dTDP-α-D-forosamine = dTDP-4-(dimethylamino)-2,3,4,6-tetradeoxy-α-D-erythro-hexopyranose | |||||||||||||
Other name(s): | SpnS; TDP-4-amino-2,3,6-trideoxy-D-glucose N,N-dimethyltransferase | |||||||||||||
Systematic name: | S-adenosyl-L-methionine:dTDP-4-amino-2,3,4,6-tetradeoxy-α-D-erythro-hexopyranose N,N-dimethyltransferase | |||||||||||||
Comments: | The enzyme was isolated from the bacterium Saccharopolyspora spinosa, where it is involved in the biosynthesis of spinosyn A, an active ingredient of several commercial insecticides. | |||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||
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EC | 4.2.1.88 | Relevance: 28.8% | ||||||||||||
Accepted name: | synephrine dehydratase | |||||||||||||
Reaction: | (R)-synephrine = (4-hydroxyphenyl)acetaldehyde + methylamine | |||||||||||||
Glossary: | (R)-synephrine = D-(-)-synephrine = 4-[(1R)-1-hydroxy-2-(methylamino)ethyl]phenol | |||||||||||||
Other name(s): | syringinase | |||||||||||||
Systematic name: | (R)-synephrine hydro-lyase (methylamine-forming) | |||||||||||||
Comments: | Removal of H2O from (R)-synephrine produces a 2,3-enamine, which hydrolyses to the products shown in the reaction above. The enzyme from Arthrobacter synephrinum is highly specific [1]. | |||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 104118-54-9 | |||||||||||||
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EC | 2.1.1.98 | Relevance: 28.2% | ||||||||||||
Accepted name: | diphthine synthase | |||||||||||||
Reaction: | 3 S-adenosyl-L-methionine + 2-[(3S)-3-carboxy-3-aminopropyl]-L-histidine-[translation elongation factor 2] = 3 S-adenosyl-L-homocysteine + diphthine-[translation elongation factor 2] (overall reaction) (1a) S-adenosyl-L-methionine + 2-[(3S)-3-carboxy-3-aminopropyl]-L-histidine-[translation elongation factor 2] = S-adenosyl-L-homocysteine + 2-[(3S)-3-carboxy-3-(methylamino)propyl]-L-histidine-[translation elongation factor 2] (1b) S-adenosyl-L-methionine + 2-[(3S)-3-carboxy-3-(methylamino)propyl]-L-histidine-[translation elongation factor 2] = S-adenosyl-L-homocysteine + 2-[(3S)-3-carboxy-3-(dimethylamino)propyl]-L-histidine-[translation elongation factor 2] (1c) S-adenosyl-L-methionine + 2-[(3S)-3-carboxy-3-(dimethylamino)propyl]-L-histidine-[translation elongation factor 2] = S-adenosyl-L-homocysteine + diphthine-[translation elongation factor 2] |
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For diagram of diphthamide biosynthesis, click here | ||||||||||||||
Glossary: | diphthine = 2-[(3S)-3-carboxy-3-(trimethylamino)propyl]-L-histidine | |||||||||||||
Other name(s): | S-adenosyl-L-methionine:elongation factor 2 methyltransferase (ambiguous); diphthine methyltransferase (ambiguous); S-adenosyl-L-methionine:2-(3-carboxy-3-aminopropyl)-L-histidine-[translation elongation factor 2] methyltransferase; Dph5 (ambiguous) | |||||||||||||
Systematic name: | S-adenosyl-L-methionine:2-[(3S)-3-carboxy-3-aminopropyl]-L-histidine-[translation elongation factor 2] methyltransferase (diphthine-[translation elongation factor 2]-forming) | |||||||||||||
Comments: | This archaeal enzyme produces the trimethylated product diphthine, which is converted into diphthamide by EC 6.3.1.14, diphthine—ammonia ligase. Different from the eukaryotic enzyme, which produces diphthine methyl ester (cf. EC 2.1.1.314). In the archaeon Pyrococcus horikoshii the enzyme acts on His600 of elongation factor 2. | |||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 114514-25-9 | |||||||||||||
References: |
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EC | 1.1.1.283 | Relevance: 28% | ||||||||||||
Accepted name: | methylglyoxal reductase (NADPH) | |||||||||||||
Reaction: | (S)-lactaldehyde + NADP+ = 2-oxopropanal + NADPH + H+ | |||||||||||||
Glossary: | 2-oxopropanal = methylglyoxal |
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Other name(s): | lactaldehyde dehydrogenase (NADP+); GRE2 (gene name); methylglyoxal reductase (NADPH-dependent); lactaldehyde:NADP+ oxidoreductase | |||||||||||||
Systematic name: | (S)-lactaldehyde:NADP+ oxidoreductase | |||||||||||||
Comments: | The enzyme from the yeast Saccharomyces cerevisiae catalyses the reduction of a keto group in a number of compounds, forming enantiopure products. Among the substrates are methylglyoxal (which is reduced to (S)-lactaldehyde) [1,2], 3-methylbutanal [3], hexane-2,5-dione [4] and 3-chloro-1-phenylpropan-1-one [5]. The enzyme differs from EC 1.1.1.78, methylglyoxal reductase (NADH), which is found in mammals, by its cosubstrate requirement, reaction direction, and enantiomeric preference. | |||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 78310-66-4 | |||||||||||||
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EC | 1.5.3.2 | Relevance: 27.1% | ||||||||||||
Accepted name: | N-methyl-L-amino-acid oxidase | |||||||||||||
Reaction: | an N-methyl-L-amino acid + H2O + O2 = an L-amino acid + formaldehyde + H2O2 | |||||||||||||
Other name(s): | N-methylamino acid oxidase; demethylase | |||||||||||||
Systematic name: | N-methyl-L-amino-acid:oxygen oxidoreductase (demethylating) | |||||||||||||
Comments: | A flavoprotein. | |||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9029-23-6 | |||||||||||||
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EC | 2.1.1.328 | Relevance: 26.7% | ||||||||||||
Accepted name: | N-demethylindolmycin N-methyltransferase | |||||||||||||
Reaction: | S-adenosyl-L-methionine + N-demethylindolmycin = S-adenosyl-L-homocysteine + indolmycin | |||||||||||||
Glossary: | indolmycin = (5S)-5-[(1R)-1-(indol-3-yl)ethyl]-2-(methylamino)-1,3-oxazolin-4(5H)-one | |||||||||||||
Other name(s): | ind7 (gene name) | |||||||||||||
Systematic name: | S-adenosyl-L-methionine:N-demethylindolmycin N-methyltransferase | |||||||||||||
Comments: | The enzyme, characterized from the bacterium Streptomyces griseus, catalyses the ultimate reaction in the biosynthesis of indolmycin, an antibacterial drug that inhibits the bacterial tryptophan—tRNA ligase (EC 6.1.1.2). | |||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||
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EC | 2.4.1.360 | Relevance: 24.7% | ||||||||||||
Accepted name: | 2-hydroxyflavanone C-glucosyltransferase | |||||||||||||
Reaction: | UDP-α-D-glucose + a 2′-hydroxy-β-oxodihydrochalcone = UDP + a 3′-(β-D-glucopyranosyl)-2′-hydroxy-β-oxodihydrochalcone | |||||||||||||
Glossary: | 2′-hydroxy-β-oxodihydrochalcone = 1-(2-hydroxyphenyl)-3-phenypropan-1,3-dione 3′-(β-D-glucopyranosyl)-2′-hydroxy-β-oxodihydrochalcone = 1-(3-(β-D-glucopyranosyl)-2-hydroxyphenyl)-3-phenylpropan-1,3-dione |
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Other name(s): | OsCGT | |||||||||||||
Systematic name: | UDP-α-D-glucose:2′-hydroxy-β-oxodihydrochalcone C6/8-β-D-glucosyltransferase | |||||||||||||
Comments: | The enzyme has been characterized in Oryza sativa (rice), various Citrus spp., Glycine max (soybean), and Fagopyrum esculentum (buckwheat). Flavanone substrates require a 2-hydroxy group. The meta-stable flavanone substrates such as 2-hydroxynaringenin exist in an equilibrium with open forms such as 1-(4-hydroxyphenyl)-3-(2,4,6-trihydroxyphenyl)propane-1,3-dione, which are the actual substrates for the glucosyl-transfer reaction (see EC 1.14.14.162, flavanone 2-hydroxylase). The enzyme can also act on dihydrochalcones. The enzymes from citrus plants can catalyse a second C-glycosylation reaction at position 5. | |||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | |||||||||||||
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EC | 1.3.1.100 | Relevance: 23.9% | ||||||||||||
Accepted name: | chanoclavine-I aldehyde reductase | |||||||||||||
Reaction: | dihydrochanoclavine-I aldehyde + NADP+ = chanoclavine-I aldehyde + NADPH + H+ | |||||||||||||
For diagram of fumigaclavin alkaloid biosynthesis, click here | ||||||||||||||
Glossary: | chanoclavine-I aldehyde = (1E)-2-methyl-3-[(4R,5R)-4-(methylamino)-1,3,4,5-tetrahydrobenz[cd]indol-5-yl]prop-2-enal | |||||||||||||
Other name(s): | FgaOx3; easA (gene name) | |||||||||||||
Systematic name: | chanoclavine-I aldehyde:NAD+ oxidoreductase | |||||||||||||
Comments: | Contains FMN. The enzyme participates in the biosynthesis of fumigaclavine C, an ergot alkaloid produced by some fungi of the Trichocomaceae family. The enzyme catalyses the reduction of chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde. This hydrolyses spontaneously to form 6,8-dimethyl-6,7-didehydroergoline, which is converted to festuclavine by EC 1.5.1.44, festuclavine dehydrogenase. | |||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | |||||||||||||
References: |
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EC | 2.1.1.390 | Relevance: 17.5% | ||||||||||||
Accepted name: | gentamicin X2 methyltransferase | |||||||||||||
Reaction: | gentamicin X2 + 2 S-adenosyl-L-methionine + reduced acceptor = geneticin + 5′-deoxyadenosine + L-methionine + S-adenosyl-L-homocysteine + oxidized acceptor (overall reaction) (1a) S-adenosyl-L-methionine + cob(I)alamin = S-adenosyl-L-homocysteine + methylcob(III)alamin (1b) methylcob(III)alamin + gentamicin X2 + S-adenosyl-L-methionine = cob(III)alamin + geneticin + 5′-deoxyadenosine + L-methionine (1c) cob(III)alamin + reduced acceptor = cob(I)alamin + oxidized acceptor |
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Glossary: | geneticin = G418 = (1R,2S,3S,4R,6S)-4,6-diamino-3-{[3-deoxy-4-C-methyl-3-(methylamino)-β-L-arabinopyranosyl]oxy}-2-hydroxycyclohexyl 2-amino-2,7-dideoxy-D-glycero-α-D-gluco-heptopyranoside | |||||||||||||
Other name(s): | genK (gene name); gntK (gene name); gentamicin C-methyltransferase (ambiguous) | |||||||||||||
Systematic name: | S-adenosyl-L-methionine:gentamicin X2 C6′-methyltransferase | |||||||||||||
Comments: | The enzyme, isolated from the bacterium Micromonospora echinospora, has a single [4Fe-4S] cluster per monomer. It is a radical S-adenosyl-L-methionine (SAM) enzyme with a methylcob(III)alamin cofactor. The enzyme uses two molecues of SAM for the reaction. One molecule forms a 5′-deoxyadenosyl radical, while the other is used to methylate the cobalamin cofactor. It catalyses methylation of the 6′-carbon of gentamicin X2 (GenX2) to produce genetricin (G418) during the biosynthesis of gentamicins. The 6′-pro-R-hydrogen atom of GenX2 is stereoselectively abstracted by the 5′-deoxyadenosyl radical and methylation occurs with retention of configuration at C6′. The regeneration of cob(I)alamin from cob(III)alamin is carried out with an as yet unidentified electron donor. | |||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | |||||||||||||
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