Abstract
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.
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Yoshimune, K., Hirayama, A. & Moriguchi, M. 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. Biotechnol Lett 27, 1325–1328 (2005). https://doi.org/10.1007/s10529-005-0480-3
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DOI: https://doi.org/10.1007/s10529-005-0480-3