Abstract
The acetyl transacylase activity of the fatty acid synthase from yeast has been investigated using p-nitrophenylthiol acetate. The chromophoric nature of the nitrophenylthiol moiety affords a convenient spectrophotometric assay for the transacylase function as well as a means to investigate the kinetics and the mechanism of this process. A probable kinetic scheme for enzyme catalyzed transacetylation from p-nitrophenylthiol acetate to an acyl acceptor (CoA or N-acetylcysteamine) is proposed and the kinetic constants for acetylation of enzyme and for acetyl transfer to an acceptor were determined. It was also demonstrated that p-nitrophenylthiol acetate can replace acetyl-CoA as a substrate in fatty acid synthesis.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Biochemical and Biophysical Research Communications
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
