1. Biochemical characteristization of propionyl-coenzyme a carboxylase complex of Streptomyces toxytricini.
- Author
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Demirev AV, Khanal A, Hanh NP, Nam KT, and Nam DH
- Subjects
- Acyl Coenzyme A metabolism, Bacterial Proteins genetics, Bacterial Proteins metabolism, Lactones metabolism, Methylmalonyl-CoA Decarboxylase genetics, Protein Subunits genetics, Recombinant Proteins genetics, Recombinant Proteins metabolism, Streptomyces classification, Streptomyces genetics, Substrate Specificity, Methylmalonyl-CoA Decarboxylase metabolism, Protein Subunits metabolism, Streptomyces enzymology
- Abstract
Acyl-CoA carboxylases (ACC) are involved in important primary or secondary metabolic pathways such as fatty acid and/or polyketides synthesis. In the 62 kb fragment of pccB gene locus of Streptomyces toxytricini producing a pancreatic inhibitor lipstatin, 3 distinct subunit genes of presumable propionyl-CoA carboxylase (PCCase) complex, assumed to be one of ACC responsible for the secondary metabolism, were identified along with gene for a biotin protein ligase (Bpl). The subunits of PCCase complex were a subunit (AccA3), P subunit (PccB), and auxiliary ɛ subunit (PccE). In order to disclose the involvement of the PCCase complex in secondary metabolism, some biochemical characteristics of each subunit as well as their complex were examined. In the test of substrate specificity of the PCCase complex, it was confirmed that this complex showed much higher conversion of propionyl-CoA rather than acetyl-CoA. It implies the enzyme complex could play a main role in the production of methylmalonyl-CoA from propionyl-CoA, which is a precursor of secondary polyketide biosynthesis.
- Published
- 2011
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