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2.1.1.353

Accepted name:

demethylluteothin O-methyltransferase

Reaction:

S-adenosyl-L-methionine + demethylluteothin = S-adenosyl-L-homocysteine + luteothin

Glossary:

luteothin = 2-[(3E,5E)-3,5-dimethyl-6-(4-nitrophenyl)hexa-3,5-dien-1-yl]-6-methoxy-3,5-dimethyl-4H-pyran-4-one
aureothin = 2-methoxy-3,5-dimethyl-6-[(2R,4Z)-4-[(2E)-2-methyl-3-(4-nitrophenyl)prop-2-en-1-ylidene]oxolan-2-yl]-4H-pyran-4-one
spectinabilin = neoaureothin = 2-methoxy-3,5-dimethyl-6-[(2R,4Z)-4-[(2E,4E,6E)-2,4,6-trimethyl-7-(4-nitrophenyl)hepta-2,4,6-trien-1-ylidene]oxolan-2-yl]-4H-pyran-4-one

Other name(s):

aurI (gene name)

Systematic name:

S-adenosyl-L-methionine:demethylluteothin O-methyltransferase

Comments:

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.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	He, J., Muller, M. and Hertweck, C. Formation of the aureothin tetrahydrofuran ring by a bifunctional cytochrome P450 monooxygenase. J. Am. Chem. Soc. 126 (2004) 16742–16743. [PMID: 15612710]
2.	Muller, M., He, J. and Hertweck, C. Dissection of the late steps in aureothin biosynthesis. ChemBioChem 7 (2006) 37–39. [PMID: 16292785]

[EC 2.1.1.353 created 2019]

2.3.1.289

Accepted name:

aureothin polyketide synthase system

Reaction:

4-nitrobenzoyl-CoA + malonyl-CoA + 4 (S)-methylmalonyl-CoA + 4 NADPH + 4 H⁺ = demethylluteothin + 5 CO₂ + 6 CoA + 4 NADP⁺ + 3 H₂O

Glossary:

demethylluteothin = nordeoxyaureothin = 2-[(3E,5E)-3,5-dimethyl-6-(4-nitrophenyl)hexa-3,5-dien-1-yl]-6-hydroxy-3,5-dimethyl-4H-pyran-4-one
aureothin = 2-methoxy-3,5-dimethyl-6-[(2R,4Z)-4-[(2E)-2-methyl-3-(4-nitrophenyl)prop-2-en-1-ylidene]oxolan-2-yl]-4H-pyran-4-one

Other name(s):

aurABC (gene names); aureothin polyketide synthase complex

Systematic name:

malonyl-CoA/(S)-methylmalonyl-CoA:4-nitrobenzoyl-CoA (methyl)malonyltransferase (demethylluteothin-forming)

Comments:

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).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	He, J. and Hertweck, C. Iteration as programmed event during polyketide assembly; molecular analysis of the aureothin biosynthesis gene cluster. Chem. Biol. 10 (2003) 1225–1232. [PMID: 14700630]
2.	He, J. and Hertweck, C. Functional analysis of the aureothin iterative type I polyketide synthase. ChemBioChem 6 (2005) 908–912. [PMID: 15812854]
3.	Busch, B., Ueberschaar, N., Sugimoto, Y. and Hertweck, C. Interchenar retrotransfer of aureothin intermediates in an iterative polyketide synthase module. J. Am. Chem. Soc. 134 (2012) 12382–12385. [PMID: 22799266]

[EC 2.3.1.289 created 2019]