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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Evidence for an essential lysine at the active site of L-histidinol:NAD+ oxidoreductase; a bifunctional dehydrogenase.

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.[1]

References

  1. Evidence for an essential lysine at the active site of L-histidinol:NAD+ oxidoreductase; a bifunctional dehydrogenase. Bürger, E., Görisch, H. Eur. J. Biochem. (1981) [Pubmed]
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