Abstract
The results with Corynebacterium glycinophilum AJ-3170 and various mutants from AJ-3170 indicated that l-serine production was almost inversely proportional to l-serine degrading activity. The crude extract of the parental strain, AJ-3170, showed l-serine and l-threonine degrading activities. The 2 activities were completely separated from each other by gel-filtration, indicating that each activity comes from a different enzyme. The l-serine degrading enzyme, l-serine dehydratase (SD), was purified 30-fold from AJ-3170. Molecular weight of SD was 130,000. The enzyme was specific for l-serine, activated slightly by FeCl 2 and inhibited by MnCl 2. The double reciprocal plots of SD rate against substrate concentration gave an upwards-curved line. The value of [S] 0.5 was 35 mM.
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 callDisclaimer: 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.
