EC |
1.1.1.397 |
Accepted name: |
β-methylindole-3-pyruvate reductase |
Reaction: |
(2S,3R)-2-hydroxy-3-(indol-3-yl)butanoate + NAD+ = (R)-3-(indol-3-yl)-2-oxobutanoate + NADH + H+ |
Glossary: |
(R)-3-(indol-3-yl)-2-oxobutanoate = (R)-β-methylindole-3-pyruvate
(2S,3R)-2-hydroxy-3-(indol-3-yl)butanoate = indolmycenate |
Other name(s): |
ind2 (gene name) |
Systematic name: |
(2S,3R)-2-hydroxy-3-(indol-3-yl)butanoate:NAD+ oxidoreductase |
Comments: |
The enzyme, characterized from the bacterium Streptomyces griseus, participates 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 |
References: |
1. |
Du, Y.L., Alkhalaf, L.M. and Ryan, K.S. In vitro reconstitution of indolmycin biosynthesis reveals the molecular basis of oxazolinone assembly. Proc. Natl. Acad. Sci. USA 112 (2015) 2717–2722. [DOI] [PMID: 25730866] |
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[EC 1.1.1.397 created 2016] |
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EC |
2.1.1.47 |
Accepted name: |
indolepyruvate C-methyltransferase |
Reaction: |
S-adenosyl-L-methionine + (indol-3-yl)pyruvate = S-adenosyl-L-homocysteine + (R)-3-(indol-3-yl)-2-oxobutanoate |
Other name(s): |
ind1 (gene name); indolepyruvate methyltransferase; indolepyruvate 3-methyltransferase; indolepyruvic acid methyltransferase; S-adenosyl-L-methionine:indolepyruvate C-methyltransferase |
Systematic name: |
S-adenosyl-L-methionine:(indol-3-yl)pyruvate C3-methyltransferase |
Comments: |
The enzyme, characterized from the bacterium Streptomyces griseus, is involved in the biosynthesis of the antibacterial drug indolmycin. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 54576-88-4 |
References: |
1. |
Hornemann, U., Speedie, M.K., Hurley, L.H. and Floss, H.G. Demonstration of a C-methylating enzyme in cell free extracts of indolmycin-producing Streptomyces griseus. Biochem. Biophys. Res. Commun. 39 (1970) 594–599. [DOI] [PMID: 5490210] |
2. |
Hornemann, U., Hurley, L.H., Speedie, M.K. and Floss, H.G. The biosynthesis of indolmycin. J. Am. Chem. Soc. 93 (1971) 3028–3035. [PMID: 5095271] |
3. |
Speedie, M.K., Hornemann, U. and Floss, H.G. Isolation and characterization of tryptophan transaminase and indolepyruvate C-methyltransferase. Enzymes involved in indolmycin biosynthesis in Streptomyces griseus. J. Biol. Chem. 250 (1975) 7819–7825. [PMID: 809439] |
4. |
Du, Y.L., Alkhalaf, L.M. and Ryan, K.S. In vitro reconstitution of indolmycin biosynthesis reveals the molecular basis of oxazolinone assembly. Proc. Natl. Acad. Sci. USA 112 (2015) 2717–2722. [DOI] [PMID: 25730866] |
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[EC 2.1.1.47 created 1976, modified 2016] |
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EC |
2.1.1.328 |
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 |
References: |
1. |
Du, Y.L., Alkhalaf, L.M. and Ryan, K.S. In vitro reconstitution of indolmycin biosynthesis reveals the molecular basis of oxazolinone assembly. Proc. Natl. Acad. Sci. USA 112 (2015) 2717–2722. [DOI] [PMID: 25730866] |
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[EC 2.1.1.328 created 2016] |
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