Abstract
3-Hexulose phosphate synthase was purified in 94% yield from Methylomonas M15. The enzyme did not form a Schiff-base intermediate with d-ribulose 5-phosphate that could be reduced by NaBH4. However, the enzyme required Mg2+ or Mn2+ ions for activity and was inactivated in the presence of EDTA. The latter is a property of class II aldolases. The enzyme accepted a wide range of other aldehydes in addition to its natural substrate formaldehyde, while d-ribulose 5-phosphate could not be replaced. This makes it an attractive tool for the synthesis of higher sugar phosphates.
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.
