Active site of human liver aldehyde dehydrogenase.
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.
Abriola
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DP
Center of Alcohol Studies, Busch Campus, Rutgers University, Piscataway, New Jersey 08854.
Fields
R
R
Stein
S
S
MacKerell
A D
AD
Pietruszko
R
R
D000098:Acetophenones / Q000494:pharmacology*; D000444:Aldehyde Dehydrogenase / Q000378:metabolism*; D001665:Binding Sites; D002250:Carbon Radioisotopes; D002851:Chromatography, High Pressure Liquid; D006801:Humans; D007527:Isoenzymes / Q000378:metabolism; D008099:Liver / Q000201:enzymology*; D010446:Peptide Fragments / Q000032:analysis; D014357:Trypsin
D000098:Acetophenones; D002250:Carbon Radioisotopes; D007527:Isoenzymes; D010446:Peptide Fragments; C013190:phenacyl bromide; D000444:Aldehyde Dehydrogenase; D014357:Trypsin