| Title |
Biochemical Characteristization of Propionyl-Coenzyme A Carboxylase Complex of Streptomyces toxytricini |
| Author |
Atanas V. Demirev, Anamika Khanal, Nguyen Phan Kieu Hanh, Kyung Tae Nam, and Doo Hyun Nam* |
| Address |
Faculty of Pharmacy, Yeungnam University, Gyongsan 712-749, Republic of Korea |
| Bibliography |
Journal of Microbiology, 49(3),407-412, 2011,
|
| DOI |
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| Key Words |
propionyl-CoA carboxylase, biotin protein ligase, AccA3, PccB, Bpl, lipstatin, Streptomyces toxytricini |
| 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 α subunit (AccA3), β subunit (PccB), and auxiliary ε 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. |
