PMID:6793363
| Citation |
Bürger, E and Görisch, H (1981) Evidence for an essential lysine at the active site of L-histidinol:NAD+ oxidoreductase; a bifunctional dehydrogenase. Eur. J. Biochem. 118:125-30 |
|---|---|
| Abstract |
Histidinol dehydrogenase (EC 1.1.1.23) from Salmonella typhimurium is inhibited by formaldehyde and pyridoxal 5-phosphate (pyridoxal-P). epsilon-Pyridoxyl-lysine is isolated upon acid hydrolysis of pyridoxal-P-treated enzyme reduced by sodium borohydride. In the presence of formylhistidinol and formylhistidine (specific ligands of the enzyme) inactivation of histidinol dehydrogenase by pyridoxal-P is prevented. Extrapolation of the initial part of the inactivation curve caused by pyridoxal-P indicates that modification of two essential lysine residues results in inactivation of the dimeric enzyme. The essential lysine residues appear to participate in the reversible oxidation/reduction reaction converting histidinol to histidinal. |
| Links | |
| Keywords |
Alcohol Oxidoreductases/metabolism; Binding Sites; Formaldehyde/pharmacology; Histidinol/metabolism; Kinetics; Lysine; Protein Binding; Pyridoxal Phosphate/pharmacology; Salmonella typhimurium/enzymology; Spectrophotometry, Ultraviolet |
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