Vitamin B 6 -responsive histidine deficiency in mutants of Salmonella typhimurium

Abstract

A mutant of Salmonella typhimurium LT-2 that requires either vitamin B(6) or histidine for growth was found to synthesize vitamin B(5) in amounts comparable to the parent strain, but to be deficient in imidazoleacetol phosphate transaminase (L-histidinolphosphate: 2-oxoglutarate aminotransferase, EC 2.6.1.9), an enzyme required for histidine biosynthesis. The mutant apotransaminase required a 50-fold higher concentration of pyridoxal 5'-phosphate for half-maximum activation than the corresponding wild-type enzyme; the fully activated mutant enzyme also displays a much lower maximum rate of catalysis than the enzyme from the parent strain. Such mutational changes in bacteria resemble those in certain vitamin B(6)-responsive genetic diseases in man and provide useful experimental material for the study of factors involved in coenzyme binding and enzymatic catalysis.