KEGG   ENZYME: 2.1.1.353
Entry
EC 2.1.1.353                Enzyme                                 

Name
demethylluteothin O-methyltransferase;
aurI (gene name)
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
Sysname
S-adenosyl-L-methionine:demethylluteothin O-methyltransferase
Reaction(IUBMB)
S-adenosyl-L-methionine + demethylluteothin = S-adenosyl-L-homocysteine + luteothin [RN:R12336]
Reaction(KEGG)
R12336
Substrate
S-adenosyl-L-methionine [CPD:C00019];
demethylluteothin [CPD:C22086]
Product
S-adenosyl-L-homocysteine [CPD:C00021];
luteothin [CPD:C22079]
Comment
The enzyme, characterized from the bacterium Streptomyces thioluteus, participates in the biosynthesis of the antibiotic aureothin. An orthologous enzyme in the bacteria Streptomyces orinoci and Streptomyces spectabilis catalyses a similar reaction in the biosynthesis of spectinabilin.
History
EC 2.1.1.353 created 2019
Orthology
K23394  demethylluteothin O-methyltransferase
Reference
1  [PMID:15612710]
  Authors
He J, Muller M, Hertweck C
  Title
Formation of the aureothin tetrahydrofuran ring by a bifunctional cytochrome p450 monooxygenase.
  Journal
J Am Chem Soc 126:16742-3 (2004)
DOI:10.1021/ja046104h
Reference
2  [PMID:16292785]
  Authors
Muller M, He J, Hertweck C
  Title
Dissection of the late steps in aureothin biosynthesis.
  Journal
Chembiochem 7:37-9 (2006)
DOI:10.1002/cbic.200500161
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 2.1.1.353
IUBMB Enzyme Nomenclature: 2.1.1.353
ExPASy - ENZYME nomenclature database: 2.1.1.353
BRENDA, the Enzyme Database: 2.1.1.353

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