Open AccessBiochemical properties of glutamate synthase of salt‐tolerant Bradyrhizobium sp. strain WR1001
Author(s) -
Hua SuiSheng T.,
Lichens Georgia M.,
Guirao Aleatha,
Tsai Victor Y.
Publication year - 1986
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1986.tb01795.x
Subject(s) - glutamate synthase , glutamate receptor , biochemistry , enzyme , atp synthase , strain (injury) , intracellular , bacteria , chemistry , biology , glutamate dehydrogenase , receptor , genetics , anatomy
Accumulation of high levels of intracellular glutamate was a common response of a variety of bacteria to osmotic stress. We characterized the NADPH‐dependent glutamate synthase (GOGAT) in Bradyrhizobium sp. strain WR1001. This enzyme had a pH optimum in the region of 8.3, as compared to 7.6 for most other Rhizobium strains reported in the literature. The enzyme was not inhibited by the end product, glutamate, in the range 50–200 mM.