Active site of human liver aldehyde dehydrogenase |
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Authors: | D P Abriola R Fields S Stein A D MacKerell R Pietruszko |
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Affiliation: | Center of Alcohol Studies, Busch Campus, Rutgers University, Piscataway, New Jersey 08854. |
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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. |
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