KEGG   ENZYME: 2.3.1.289Help
Entry
EC 2.3.1.289                Enzyme                                 

Name
aureothin polyketide synthase system;
aurABC (gene names);
aureothin polyketide synthase complex
Class
Transferases;
Acyltransferases;
Transferring groups other than aminoacyl groups
BRITE hierarchy
Sysname
malonyl-CoA/(S)-methylmalonyl-CoA:4-nitrobenzoyl-CoA (methyl)malonyltransferase (demethylluteothin-forming)
Reaction(IUBMB)
4-nitrobenzoyl-CoA + malonyl-CoA + 4 (S)-methylmalonyl-CoA + 4 NADPH + 4 H+ = demethylluteothin + 5 CO2 + 6 CoA + 4 NADP+ + 3 H2O [RN:R12467]
Reaction(KEGG)
Substrate
4-nitrobenzoyl-CoA [CPD:C22178];
malonyl-CoA [CPD:C00083];
(S)-methylmalonyl-CoA [CPD:C00683];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Product
demethylluteothin [CPD:C22086];
CO2 [CPD:C00011];
CoA [CPD:C00010];
NADP+ [CPD:C00006];
H2O [CPD:C00001]
Comment
This polyketide synthase, characterized from the bacterium Streptomyces thioluteus, generates the backbone of the antibiotic aureothin. It is composed of 4 modules that total 18 domains and is encoded by three genes. The enzyme accepts the unusual starter unit 4-nitrobenzoyl-CoA and extends it by 4 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA. The first module (encoded by aurA) is used twice in an iterative fashion, so that the five Claisen condensation reactions are catalysed by only four modules. The iteration becomes possible by the transfer of the [acp]-bound polyketide intermediate back to the ketosynthase (KS) domain on the opposite polyketide synthase strand (polyketides are homodimeric).
History
EC 2.3.1.289 created 2019
Orthology
K23744  aureothin polyketide synthase system AurA
K23745  aureothin polyketide synthase system AurB
K23746  aureothin polyketide synthase system AurC
Reference
1  [PMID:14700630]
  Authors
He J, Hertweck C.
  Title
Iteration as programmed event during polyketide assembly; molecular analysis of the aureothin biosynthesis gene cluster.
  Journal
Chem Biol 10:1225-32 (2003)
DOI:10.1016/j.chembiol.2003.11.009
  Sequence
Reference
2  [PMID:15812854]
  Authors
He J, Hertweck C
  Title
Functional analysis of the aureothin iterative type I polyketide synthase.
  Journal
Chembiochem 6:908-12 (2005)
Reference
3  [PMID:22799266]
  Authors
Busch B, Ueberschaar N, Sugimoto Y, Hertweck C
  Title
Interchenar retrotransfer of aureothin intermediates in an iterative polyketide synthase module.
  Journal
J Am Chem Soc 134:12382-5 (2012)
Other DBs
ExplorEnz - The Enzyme Database: 2.3.1.289
IUBMB Enzyme Nomenclature: 2.3.1.289
ExPASy - ENZYME nomenclature database: 2.3.1.289
BRENDA, the Enzyme Database: 2.3.1.289

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