Abstract
The kinetic properties of L-glutamate: gloxylate transminase have been investigated. Glycine formation was linear with both protein concentration and incubation time. L-glutamate was the most effective amino donor. Optimal concentrations for L-glutamate and glyoxylate were 150–200 mM and 10–20 mM, respectively. Initial velocity studies suggested a ping-pong reaction mechanism with a K m value of 89.90-66.50 mM for L-glutamate and of 12.50-10.75 mM for glyoxylate. A competitive parabolic substrate inhibition by glyoxylate at concentrations greater than 20 mM was observed. A pure linear non-competitive inhibition between glyoxylate and 4,5-dioxovaleric acid (1.1–2.8 mM) was found. We show here that in vivo different enzymes exist for the transamination of glyoxylate and DOVA.
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: Journal of Photochemistry & Photobiology, B: Biology
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.
