The Enzyme Database

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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]
[EC 1.1.1.397 created 2016]
 
 
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]
[EC 2.1.1.47 created 1976, modified 2016]
 
 
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]
[EC 2.1.1.328 created 2016]
 
 


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