A metal ion as a cofactor attenuates substrate inhibition in the enzymatic production of a high concentration of D-glutamate using N-acyl-D-glutamate amidohydrolase.
N-Acyl-D-glutamate amidohydrolase (D-AGase) was inhibited by 94 % when 1 mol/l N-acetyl-DL-glutamate was used as a substrate. The addition of 1 mM Co2+ stabilized D-AGase. Moreover, the substrate inhibition was weakened to 88% with the addition of 0.4 mM Co2+ to the reaction mixture. Although D-AGase is a zinc-metalloenzyme, the addition of Zn2+ from 0.01 to 10 mM did not increase the D-glutamic acid production in the saturated substrate. Under optimal conditions, 0.38 M D-glutamic acid was obtained from N-acyl-DL-glutamate with 100% of the theoretical yield after 48 h.
Yoshimune
Kazuaki
K
Department of Applied Chemistry, Faculty of Engineering, Oita University, Dannoharu 700, 870-1192, Oita, Japan.
Hirayama
Ai
A
Moriguchi
Mitsuaki
M
D000421:Alcaligenes / Q000201:enzymology*; D000581:Amidohydrolases / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D003035:Cobalt / Q000737:chemistry*; D003067:Coenzymes / Q000737:chemistry*; D018698:Glutamic Acid / Q000737:chemistry*; D007477:Ions / Q000737:chemistry; D015032:Zinc / Q000737:chemistry*
D001426:Bacterial Proteins; D003067:Coenzymes; D007477:Ions; D003035:Cobalt; D018698:Glutamic Acid; D000581:Amidohydrolases; C070988:N-acyl-D-glutamate deacylase; D015032:Zinc