Premium
Properties of glutamate dehydrogenase from Beta vulgaris
Author(s) -
NESSELHUT TH.,
HARNISCHFEGER G.
Publication year - 1980
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1980.tb02673.x
Subject(s) - nad+ kinase , glutamate dehydrogenase , substrate (aquarium) , oxidoreductase , glutamate receptor , chemistry , enzyme , biochemistry , beta (programming language) , stereochemistry , biology , ecology , receptor , computer science , programming language
Glutamate‐NAD oxidoreductase, E.C. 1.4.1.3 (GDH), from seedlings of Beta vulgaris cv. Rota, Jahnsch Peragis Comp., was enzymatically characterized. This enzyme with molecular weight of 2.6 × 10 5 has a pH optimum of around 8 for animation of α‐KGA and around 9.5 for the desamination of glutamate. The apparent K m for α‐KGA is 6.7 × 10 −4 M , for NH 3 2.5 × 10 −3 M , for NADH 3.2 × 10 −5 M and for NAADPH 5.5 × 10 −4 M . NAD 1 inhibits the reaction non‐competitively when NADPH serves as substrate. The apparent K 1 is 4.5 × 10 −4 M . The data are discussed on relation to the properties of GDH from other plant sources.