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Regulation of Two Soluble Forms of Brain Glutamate Dehydrogenase Isoproteins by Leucine

Authors
 Jongweon Lee  ;  Jong Eun Lee  ;  Soo Young Choi  ;  Sung-Woo Cho 
Citation
 JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY, Vol.30(5) : 332-336, 1997 
Journal Title
 JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY 
ISSN
 1225-8687 
Issue Date
1997
Abstract
The stimulatory effects of leucine on the activities of two soluble forms of brain glutamate dehydrogenase isoproteins (GDH I and GDH II) have been studied at various conditions. There were significant differences between GDH I and GDH II in their sensitivities to the action of leucine. When the effects of varied leucine concentrations on GDH activities were studied in the direction of reductive amination of 2-oxoglutarate with NADPH as a coenzyme, a marked activation was observed for both isoproteins at leucine concentrations up to 10 mM, whereas both isoproteins showed activation to a lesser extent with NADH as a coenzyme. The stimulatory effects of leucine on GDH activities in the direction of the oxidative deamination of glutamate were also observed, but to a much lesser extent. Leucine relieved the inhibition of GDH I by GTP and this resulted in an increase in the apparent activation by leucine in the presence of GTP. 2-Oxoglutarate was found to give rise to high substrate inhibition and leucine significantly reduced the substrate inhibition in the presence of $200\;{\mu}M$ 수식 이미지 NADH. Thus, the effects of leucine might be composed of a direct effect on the enzyme together with a relief of high substrate inhibition.
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Anatomy (해부학교실) > 1. Journal Papers
Yonsei Authors
Lee, Jong Eun(이종은) ORCID logo https://orcid.org/0000-0001-6203-7413
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/177315
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