DEVIATIONS FROM MICHAELIS-MENTEN BEHAVIOR OF PLANT GLUTAMATE-DEHYDROGENASE WITH AMMONIUM AS VARIABLE SUBSTRATE - Research portal of Justus Liebig University Giessen:

Journal article

DEVIATIONS FROM MICHAELIS-MENTEN BEHAVIOR OF PLANT GLUTAMATE-DEHYDROGENASE WITH AMMONIUM AS VARIABLE SUBSTRATE

Authors list: PAHLICH, E; GERLITZ, C

Publication year: 1980

Pages: 11-13

Journal: Phytochemistry

Volume number: 19

Issue number: 1

ISSN: 0031-9422

eISSN: 1873-3700

DOI Link: https://doi.org/10.1016/0031-9422(80)85004-7

Publisher: Elsevier

Abstract:
A stopped flow kinetic analysis was performed with a homogenous protein fraction of plant (Pisum sativum) glutamate dehydrogenase. The enzyme exerts strong negative cooperativity with ammonium as variable substrate. The limiting initial rate constants for low substrate concentrations, as calculated from the kinetic data, indicate that the catalytic efficiency of the enzyme increases at low ammonium concentrations. From this it becomes evident that the reductive amination reaction is highly adaptive to the ammonium environment.

Citation Styles

Harvard Citation style: PAHLICH, E. and GERLITZ, C. (1980) DEVIATIONS FROM MICHAELIS-MENTEN BEHAVIOR OF PLANT GLUTAMATE-DEHYDROGENASE WITH AMMONIUM AS VARIABLE SUBSTRATE, Phytochemistry, 19(1), pp. 11-13. https://doi.org/10.1016/0031-9422(80)85004-7

APA Citation style: PAHLICH, E., & GERLITZ, C. (1980). DEVIATIONS FROM MICHAELIS-MENTEN BEHAVIOR OF PLANT GLUTAMATE-DEHYDROGENASE WITH AMMONIUM AS VARIABLE SUBSTRATE. Phytochemistry. 19(1), 11-13. https://doi.org/10.1016/0031-9422(80)85004-7

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