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In mutant cells ofEscherichia coli missing the particulatel -α-glycerophosphate (l -α-GP) dehydrogenase necessary for aerobic growth on glycerol orl -αGP, a soluble, flavine-dependentl -α-GP dehydrogenase supports normal anaerobic growth rates on either of the two substrates with fumarate or nitrate as exogenous hydrogen acceptor. In an experiment in which glycerol served as the carbon source and nitrate as the acceptor, the growth of such a mutant was arrested upon the admission of air, whereas the growth of wild-type cells continued smoothly. Mutant cells lacking the solublel -α-GP dehydrogenase, but possessing the particulate enzyme, can grow at normal rates aerobically on glycerol andl -α-GP or anaerobically on these compounds with nitrate, but not fumarate, as the hydrogen acceptor. Double mutants lacking both of the dehydrogenases fail to show significant growth on either glycerol orl -α-GP under any condition. Mutations affecting the anaerobic dehydrogenase (glpA locus) are situated at about minute 43 of the Taylor map, just clockwise beyondglpT , and show cotransduction withpurF (1.5%),glpT (91%), andnalA (50%). The anaerobic dehydrogenase is a member of theglp regulon as judged by its inducibility byl -α-GP and by its constitutive formation in strains ofglpR c genotype. The level of the anaerobic dehydrogenase is about the same in cells grown either aerobically or anaerobically with nitrate serving as a terminal hydrogen acceptor. With fumarate as terminal acceptor, the level is elevated several fold.

Anaerobic l -α-Glycerophosphate Dehydrogenase of Escherichia coli: Its Genetic Locus and Its Physiological Role