Purification, characterization, and physiological function of Bacillus subtilis ornithine transcarbamylase.

AUTOR(ES)

Neway, J O

RESUMO

A procedure was developed for purification of ornithine transcarbamylase (OTCase) to near homogeneity from Bacillus subtilis 168. The purified native enzyme existed as a mixture of dimeric, tetrameric, and hexameric forms, but was converted to the dimer in the presence of 2-mercaptoethanol. The molecular weight of the subunit was 44,000. Some general kinetic properties of the enzyme were described. OTCase was repressed by arginine in growing B. subtilis cells, but the enzyme was induced by arginine at the end of exponential growth. Specific antibodies against the purified OTCase were used to show that the same enzyme was produced under all conditions. These results and studies of a mutant lacking OTCase demonstrated that B. subtilis produced only a single OTCase. OTCase was clearly required for arginine biosynthesis, but the physiological function of OTCase induction by arginine was obscure. OTCase was not induced by, or required for, growth on arginine as a carbon and nitrogen source. Absence of OTCase in a mutant did not alter the yield or arginine content of its spores in comparison to a strain containing OTCase.

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