Biochemical Characteristization of Propionyl-Coenzyme A Carboxylase Complex of Streptomyces toxytricini

Title
Biochemical Characteristization of Propionyl-Coenzyme A Carboxylase Complex of Streptomyces toxytricini
Author(s)
남두현데미레프아타나스아나미까 커널[아나미까 커널]응엔 판 기우 한[응엔 판 기우 한]남경태[남경태]
Keywords
ACETYL-COA CARBOXYLASE; COELICOLOR A3(2); POSTTRANSLATIONAL MODIFICATION; LIPASE INHIBITOR; ACYL-COENZYME; LIPSTATIN; PROTEINS; BIOTINYLATION; BIOSYNTHESIS; GENE
Issue Date
201106
Publisher
MICROBIOLOGICAL SOCIETY KOREA
Citation
JOURNAL OF MICROBIOLOGY, v.49, no.3, pp.407 - 412
Abstract
Acyl-CoA carboxylases (ACC) are involved in important primary or secondary metabolic pathways such as fatty acid and/or polyketides synthesis. In the 6.2 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), beta subunit (PccB), and auxiliary c 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.
URI
http://hdl.handle.net/YU.REPOSITORY/25116http://dx.doi.org/10.1007/s12275-011-1122-1
ISSN
1225-8873
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약학대학 > 약학부 > Articles
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