IUBMB Enzyme Nomenclature

EC 2.1.1.353

Accepted name: demethylluteothin O-methyltransferase

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

For diagram of reaction click here.

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, ExplorEnz, KEGG, MetaCyc, CAS registry number:

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]


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