Affiliation:
1. Biological and Chemical Sciences and Engineering, Central Research and Development, E. I. DuPont de Nemours, Inc., Wilmington, Delaware 19880-0328
Abstract
ABSTRACT
Biological oxidation of cyclic ketones normally results in formation of the corresponding dicarboxylic acids, which are further metabolized in the cell.
Rhodococcus ruber
strain SC1 was isolated from an industrial wastewater bioreactor that was able to utilize cyclododecanone as the sole carbon source. A reverse genetic approach was used to isolate a 10-kb gene cluster containing all genes required for oxidative conversion of cyclododecanone to 1,12-dodecanedioic acid (DDDA). The genes required for cyclododecanone oxidation were only marginally similar to the analogous genes for cyclohexanone oxidation. The biochemical function of the enzymes encoded on the 10-kb gene cluster, the flavin monooxygenase, the lactone hydrolase, the alcohol dehydrogenase, and the aldehyde dehydrogenase, was determined in
Escherichia coli
based on the ability to convert cyclododecanone. Recombinant
E. coli
strains grown in the presence of cyclododecanone accumulated lauryl lactone, 12-hydroxylauric acid, and/or DDDA depending on the genes cloned. The cyclododecanone monooxygenase is a type 1 Baeyer-Villiger flavin monooxygenase (FAD as cofactor) and exhibited substrate specificity towards long-chain cyclic ketones (C
11
to C
15
), which is different from the specificity of cyclohexanone monooxygenase favoring short-chain cyclic compounds (C
5
to C
7
).
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
89 articles.
订阅此论文施引文献
订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献