Biochemical properties of glutamate synthase of salt-tolerant Bradyrhizobium sp. strain WR1001

Abstract 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.