Abstract
Glutamate decarboxylase (GAD) (EC 4.1.1.15) catalyzes decarboxylation of glutamic acid to produce gammaaminobutyric acid (GABA). A putative gad gene (tk1814) from an archaeon Thermococcus kodakaraensis KOD1 was cloned and transformed into Escherichia coli to produce a bulk amount of recombinant GAD. Activity of the purified GAD was optimal at 90°C and pH 8.0. Optimal concentration of substrate for conversion into gamma-aminobutyric acid by recombinant GAD was 50 mM monosodium glutamate. Recombinant GAD was confirmed to be monomeric, and its activity was greatly inhibited by various salts such as sodium chloride, Tris-HCl, and sodium phosphate. Km, Vmax, and Kcat values were 9.92 mM, 153.8 μmol min−1 mg−1, and 6.613×103 min−1 respectively.
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 the Korean Society for Applied Biological Chemistry
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.
