Active site of human liver aldehyde dehydrogenase. [Biochemistry. 1987]

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1: Biochemistry. 1987 Sep 8;26(18):5679-84.Links

Active site of human liver aldehyde dehydrogenase.

Abriola DP, Fields R, Stein S, MacKerell AD Jr, Pietruszko R.

Center of Alcohol Studies, Busch Campus, Rutgers University, Piscataway, New Jersey 08854.

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.

PMID: 3676276 [PubMed - indexed for MEDLINE]

Correlation of loss of activity of human aldehyde dehydrogenase with reaction of bromoacetophenone with glutamic acid-268 and cysteine-302 residues. Partial-sites reactivity of aldehyde dehydrogenase.
Biochem J. 1990 Feb 15; 266(1):179-87.

[Biochem J. 1990]
Bromoacetophenone as an affinity reagent for human liver aldehyde dehydrogenase.
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