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- W81581036 abstract "Publisher SummaryGlutamate is of major importance in intermediary metabolism serving as an amino donor in the biosynthesis of almost all other amino acids. Glutamate synthase plays a major role in glutamate biosynthesis. Coupled with glutamine synthetase, glutamate synthase provides a pathway for ammonia assimilation at low free ammonia concentrations or whenever nitrogen availability limits growth, during nitrogen fixation in bacteria capable of fixing nitrogen, and in bacteria that lack glutamate dehydrogenase activity. Thus, it seems probable that many ecologically important bacteria utilize glutamate synthase during nitrogen assimilation. Escherichia coli is the only bacterium from which glutamate synthase has been purified to homogeneity. Escherichia coli glutamate synthase is a high-molecular weight multisubunit nonheme iron containing flavoprotein. Available data suggest that the enzyme might be composed of eight subunits, four of each of two types of dissimilar subunits of molecular weights 135,000 and 53,000. In addition, each molecule contains approximately 32 iron atoms, 32 labile sulfide atoms, and 8 noncovalently bound flavin molecules. The role of nonheme iron and labile sulfide in glutamate synthase catalysis remains to be defined, although it seems likely that it is involved in electron transport as has been postulated for other nonheme iron-containing flavoproteins." @default.
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- W81581036 date "1974-01-01" @default.
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- W81581036 title "GLUTAMATE SYNTHASE" @default.
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- W81581036 doi "https://doi.org/10.1016/b978-0-12-515250-1.50017-5" @default.
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