Abstract
O-phosphorylethanolamine ammonia lyase, a new enzyme present in vertebrate liver, has been shown to catalyze the catabolism of O-phosphorylethanolamine to equimolar quantities of ammonia, acetaldehyde, and inorganic phosphate. The enzyme occurs in the soluble fraction of the cell and has been partially purified from rabbit liver. Using 14C O-PE as substrate, the 14C acetaldehyde formed enzymatically was characterized as the 2,4-dinitrophenylhydrazone by infrared spectra and chromatography. Ethanolamine is not a substrate for the enzyme nor does the cobamide coenzyme affect its rate. The Km for O-phosphorylethanolamine was found to be 6.1 × 10 −4M and for pyridoxal phosphate 2.7 × 10 −7M.
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.
