Evidence for two distinct pyruvate kinase genes in Escherichia coli K-12 |
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Authors: | A Garrido-Pertierra R A Cooper |
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Affiliation: | 1. Institute of Physiology, Georgian SSR Academy of Sciences, Gogua str. 14, Tbilisi 60, 380060 USSR;2. Institute of Molecular Biology, USSR Academy of Sciences, Vavilov str. 32, Moscow, V-334, 117984, USSR |
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Abstract: | A strain of Escherichia coli K-12 defective in pyruvate kinase F has been produced. The existence of this mutant, in conjunction with earlier results, strongly suggests that the two pyruvate kinases in this bacterium are distinct forms and not interconvertible. Either form of pyruvate kinase appeared to be equally effective in the glycolytic conversion of phosphoenolpyruvate to pyruvate. Genes specifying pyruvate kinase A and pyruvate kinase F were present on the small F-prime F506 and the locus for pyruvate kinase F was found to be at minute 36.5 on the E. coli genetic map. |
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Keywords: | 3′-Deoxy-3′-aminonucleoside 5′-triphosphate Terminator RNA synthesis DNA-dependent RNA polymerase 3′-deoxy-3′-aminonucleoside 5′-monophosphates with adenine, guanine, uracil and cytosine bases CpA cytidilyl-(3′ → 5′)-adenosine C(3′NH)pA 3′-deoxy-3′-aminocytidilyl-(3′ → 5′)-adenosine |
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