Molecular characterization of the non-biotin-containing subunit of 3-methylcrotonyl-CoA carboxylase
AL McKean, J Ke, J Song, P Che, S Achenbach… - Journal of Biological …, 2000 - jbc.org
The biotin enzyme, 3-methylcrotonyl-CoA carboxylase (MCCase)(3-methylcrotonyl-CoA:
carbon-dioxide ligase (ADP-forming), EC 6.4. 1.4), catalyzes a pivotal reaction required for
both leucine catabolism and isoprenoid metabolism. MCCase is a heteromeric enzyme
composed of biotin-containing (MCC-A) and non-biotin-containing (MCC-B) subunits.
Although the sequence of the MCC-A subunit was previously determined, the primary
structure of the MCC-B subunit is unknown. Based upon sequences of biotin enzymes that …
carbon-dioxide ligase (ADP-forming), EC 6.4. 1.4), catalyzes a pivotal reaction required for
both leucine catabolism and isoprenoid metabolism. MCCase is a heteromeric enzyme
composed of biotin-containing (MCC-A) and non-biotin-containing (MCC-B) subunits.
Although the sequence of the MCC-A subunit was previously determined, the primary
structure of the MCC-B subunit is unknown. Based upon sequences of biotin enzymes that …
