Isolation and characterization of temperature-sensitive pantothenate kinase (coaA) mutants of Escherichia coli.
Escherichia coli mutants conditionally defective in the conversion of pantothenate to coenzyme A were isolated and characterized. The gene was designated coaA and localized between argEH and rpoB near min 90 of the chromosome. The coaA15(Ts) mutation caused a temperature-sensitive growth phenotype and temperature-dependent inactivation of pantothenate kinase activity assayed both in vivo and in vitro. At 30 degrees C, coaA15(Ts) extracts contained less than 20% of the wild-type pantothenate kinase activity; the kinase had near normal kinetic constants for the substrates ATP and pantothenate and was inhibited by coenzyme A to the same degree as the wild-type enzyme. These data define the coaA gene as the structural gene for pantothenate kinase.
Vallari
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Department of Biochemistry, St. Jude Children's Research Hospital, Memphis, Tennessee 38101.
Rock
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D003065:Coenzyme A / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D005796:Genes; D005798:Genes, Bacterial; D009154:Mutation; D010205:Pantothenic Acid / Q000378:metabolism; D010641:Phenotype; D010766:Phosphorylation; D010770:Phosphotransferases / Q000235:genetics*; D017853:Phosphotransferases (Alcohol Group Acceptor); D013696:Temperature; D014161:Transduction, Genetic; D015091:beta-Alanine / Q000378:metabolism
D015091:beta-Alanine; D010205:Pantothenic Acid; D010770:Phosphotransferases; D017853:Phosphotransferases (Alcohol Group Acceptor); C023088:pantothenate kinase; D003065:Coenzyme A