Characterization of Coturnix quail liver alcohol dehydrogenase enzymes.

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Nussrallah BA, Dam R, Wagner FW

Characterization of Coturnix quail liver alcohol dehydrogenase enzymes.

Biochemistry. 1989 Jul 25;28(15):6245-51.

PubMed ID

2789998 [ View in PubMed

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Abstract

Livers from male or female Coturnix quail possess up to four electrophoretically distinct bands of alcohol dehydrogenase (ADH) activity. Three pyrazole-sensitive bands of enzymatic activity, designated ADH-1, ADH-2, and ADH-3, are cathodic at pH 8.2, and the fourth, ADH-An, is neutral to slightly anodic and insensitive to pyrazole. ADH-2 and ADH-3, and occasionally ADH-1, are present in livers from immature females. The predominant enzyme in immature male livers is ADH-3. At sexual maturity all three pyrazole-sensitive enzymes are present in livers from male birds, and livers from females possess predominantly ADH-3. ADH-2 and ADH-3, purified from female livers, are dimers of 80,000 daltons possessing 4 mol of Zn2+/mol of native protein. Both ADH-2 and ADH-3 were inhibited by 4-methylpyrazole with KI values of 430 and 335 nM, respectively. These values are similar to those of human class I isoenzymes. Neither enzyme oxidized methanol or ethylene glycol, which distinguished them from mammalian pyrazole-sensitive ADH isoenzymes. Both ADH-2 and ADH-3 showed specificity toward hydrophobic primary alcohols and were most active toward benzyl alcohol and n-octanol.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Fomepizole	Alcohol dehydrogenase 1A	Protein	Humans	Yes	Inhibitor	Details