Histidinol dehydrogenase from salmonella typhimurium and Escherichia coli. Purification, some characteristics and the amino acid sequence around a reactive thiol group.
The purification and some physical properties of histidinol dehydrogenase, L-histidinol-nicotinamide adenine dinucleotide oxido-reductase (EC 1.1.1.23) from either Salmonella typhimurium or Escherichia coli are reported in this paper. Modification of histidinol dehydrogenase with one equivalent of N-(4-dimethylamino-3,5-dinitrophenyl)maleimide at pH 6.8 yields an enzyme that is inactive toward the oxidation of L-histidinol. The modified cysteine residue was located in an acid insoluble tryptic core. The amino acid sequence around the reactive thiol group in S. typhimurium is: Leu-Cys-Gly-Val-Glu-Glu-Ile-Phe, and in E. coli is: Leu-Cys-Gly-Val-Glu-Asp-Val-Phe. These unique sequences show no homology to the reactive thiol groups from some other dehydrogenases.
D000429:Alcohol Oxidoreductases / Q000302:isolation & purification; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001665:Binding Sites; D003545:Cysteine / Q000032:analysis; D004926:Escherichia coli / Q000201:enzymology*; D006641:Histidinol; D007700:Kinetics; D008301:Maleimides; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D012486:Salmonella typhimurium / Q000201:enzymology*; D013045:Species Specificity
D000596:Amino Acids; D008301:Maleimides; D010446:Peptide Fragments; D006641:Histidinol; D000429:Alcohol Oxidoreductases; C021358:histidinol dehydrogenase; D003545:Cysteine