Abstract
Ornithine and α-N-acetylornithine δ-aminotransferases were purified to a homogeneous state from a gramicidin S-producing strain of Bacillus brevis. Ornithine aminotransferase has a molecular weight of about 90,000 and N-acetylornithine aminotransferase has that of about 80,000 on gel filtration, respectively. Both enzymes were composed of two identical subunits. Ornithine aminotransferase is specific for ornithine, and N-acetylornithine aminotransferase is specific for N-acetylornithine as amino donor. Both enzymes used 2-oxoglutarate as amino acceptor.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
More From: Enzymes Dependent on Pyridoxal Phosphate and Other Carbonyl Compounds as Cofactors
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.