KEGG   ENZYME: 2.1.1.47
Entry
EC 2.1.1.47                 Enzyme                                 
Name
indolepyruvate C-methyltransferase;
ind1 (gene name);
indolepyruvate methyltransferase;
indolepyruvate 3-methyltransferase;
indolepyruvic acid methyltransferase;
S-adenosyl-L-methionine:indolepyruvate C-methyltransferase
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
Sysname
S-adenosyl-L-methionine:(indol-3-yl)pyruvate C3-methyltransferase
Reaction(IUBMB)
S-adenosyl-L-methionine + (indol-3-yl)pyruvate = S-adenosyl-L-homocysteine + (R)-3-(indol-3-yl)-2-oxobutanoate [RN:R01972]
Reaction(KEGG)
R01972;
(other) R01973
Substrate
S-adenosyl-L-methionine [CPD:C00019];
(indol-3-yl)pyruvate [CPD:C00331]
Product
S-adenosyl-L-homocysteine [CPD:C00021];
(R)-3-(indol-3-yl)-2-oxobutanoate [CPD:C21289]
Comment
The enzyme, characterized from the bacterium Streptomyces griseus, is involved in the biosynthesis of the antibacterial drug indolmycin.
History
EC 2.1.1.47 created 1976, modified 2016
Pathway
ec00380  Tryptophan metabolism
ec01100  Metabolic pathways
Orthology
K22590  indolepyruvate C-methyltransferase
Reference
1  [PMID:5490210]
  Authors
Hornemann U, Speedie MK, Hurley LH, Floss HG.
  Title
Demonstration of a C-methylating enzyme in cell free extracts of indolmycin-producing Streptomyces griseus.
  Journal
Biochem Biophys Res Commun 39:594-9 (1970)
DOI:10.1016/0006-291X(70)90245-7
Reference
2  [PMID:5095271]
  Authors
Hornemann U, Hurley LH, Speedie MK, Floss HG
  Title
The biosynthesis of indolmycin.
  Journal
J Am Chem Soc 93:3028-35 (1971)
DOI:10.1021/ja00741a035
Reference
3  [PMID:809439]
  Authors
Speedie MK, Hornemann U, Floss HG
  Title
Isolation and characterization of tryptophan transaminase and indolepyruvate C-methyltransferase. Enzymes involved in indolmycin biosynthesis in Streptomyces  griseus.
  Journal
J Biol Chem 250:7819-25 (1975)
Reference
4  [PMID:25730866]
  Authors
Du YL, Alkhalaf LM, Ryan KS
  Title
In vitro reconstitution of indolmycin biosynthesis reveals the molecular basis of oxazolinone assembly.
  Journal
Proc Natl Acad Sci U S A 112:2717-22 (2015)
DOI:10.1073/pnas.1419964112
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 2.1.1.47
IUBMB Enzyme Nomenclature: 2.1.1.47
ExPASy - ENZYME nomenclature database: 2.1.1.47
BRENDA, the Enzyme Database: 2.1.1.47
CAS: 54576-88-4

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