Isolation and partial characterization of a mutant of Escherichia coli lacking pyridine nucleotide transhydrogenase. |
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Authors: | K J Zahl C Rose R L Hanson |
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Affiliation: | Department of Biochemistry, Columbia University, New York, New York 10032 USA |
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Abstract: | A mutant of Escherichia coli lacking pyridine nucleotide transhydrogenase (EC 1.6.1.1) was isolated by assaying activity in clones of cells mutagenized with N-methyl-N′-nitro-N-nitrosoguanidine. The mutant is missing both energy-independent and energy-dependent transhydrogenase, but has normal NADH dehydrogenase and ATPase activities. Compared to the parental strain, the mutant has normal growth rates with glucose, glycerol, or succinate aerobically and with glucose or glycerol plus fumarate anaerobically. The aerobic growth yield with limiting glucose concentrations is also normal. These growth properties indicate that the enzyme is not an essential source of NADPH or ATP in vivo. |
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