Active Site of Human Liver Aldehyde Dehydrogenase

Biochemistry. 1987 Sep 8;26(18):5679-84. doi: 10.1021/bi00392a015.

Abstract

Bromoacetophenone (2-bromo-1-phenylethanone) functions as an affinity reagent for human aldehyde dehydrogenase (EC 1.2.1.3) and has been found specifically to label a unique tryptic peptide in the enzyme. Amino-terminal sequence analysis of the labeled peptide after purification by two different procedures revealed the following sequence: Val-Thr-Leu-Glu-Leu-Gly-Gly-Lys. Radioactivity was found to be associated with the glutamate residue, which was identified as Glu-268 by reference to the known amino acid sequence. This paper constitutes the first identification of an active site of aldehyde dehydrogenase.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acetophenones / pharmacology*
  • Aldehyde Dehydrogenase / metabolism*
  • Binding Sites
  • Carbon Radioisotopes
  • Chromatography, High Pressure Liquid
  • Humans
  • Isoenzymes / metabolism
  • Liver / enzymology*
  • Peptide Fragments / analysis
  • Trypsin

Substances

  • Acetophenones
  • Carbon Radioisotopes
  • Isoenzymes
  • Peptide Fragments
  • phenacyl bromide
  • Aldehyde Dehydrogenase
  • Trypsin