Glutamates 78 and 122 in the active site of saccharopine dehydrogenase contribute to reactant binding and modulate the basicity of the acid-base catalysts

DK Ekanayake, B Andi, KD Bobyk, AH West…

Index: Ekanayake, Devi K.; Andi, Babak; Bobyk, Kostyantyn D.; West, Ann H.; Cook, Paul F. Journal of Biological Chemistry, 2010 , vol. 285, # 27 p. 20756 - 20768

Full Text: HTML

Citation Number: 6

Abstract

Abstract Saccharopine dehydrogenase catalyzes the NAD-dependent oxidative deamination of saccharopine to give l-lysine and α-ketoglutarate. There are a number of conserved hydrophilic, ionizable residues in the active site, all of which must be important to the overall reaction. In an attempt to determine the contribution to binding and rate enhancement of each of the residues in the active site, mutations at each residue are ...