Human liver alcohol dehydrogenase (ADH) isoenzymes beta 1 beta 1, gamma 1 gamma 1 from Caucasian individuals with 'typical' ADH and beta 2 beta 2-Bern from Caucasian individuals with 'atypical' phenotype differed in their susceptibility to anions. At pH 7.0 beta 1 beta 1 and gamma 1 gamma 1 were more active in Tris-HCl buffer than in sodium phosphate buffer but less active in Hepes-NaOH and Mops-NaOH. beta 2 beta 2-Bern showed the same activity in all these buffers. At pH 7.0 and at low concentrations (50-100 mM) chloride activated the ethanol oxidation by beta 1 beta 1 and gamma 1 gamma 1, whereas sulfate showed no effect. At anion concentrations above 100 mM all isoenzymes were inhibited. At pH 10.5 beta 1 beta 1 and gamma 1 gamma 1 were not activated. Measuring the acetaldehyde reduction, no comparable activation by chloride was observed; all three isoenzymes were inhibited, at significantly lower anion concentrations. These anion effects can be correlated with the different primary structures of the isoenzymes around the active site and the coenzyme binding site.
Interacting selectively and non-covalently with a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
Human liver alcohol dehydrogenase (ADH) isoenzymes beta 1 beta 1, gamma 1 gamma 1 from Caucasian individuals with 'typical' ADH and beta 2 beta 2-Bern from Caucasian individuals with 'atypical' phenotype differed in their susceptibility to anions. At pH 7.0 beta 1 beta 1 and gamma 1 gamma 1 were more active in Tris-HCl buffer than in sodium phosphate buffer but less active in Hepes-NaOH and Mops-NaOH. beta 2 beta 2-Bern showed the same activity in all these buffers. At pH 7.0 and at low concentrations (50-100 mM) chloride activated the ethanol oxidation by beta 1 beta 1 and gamma 1 gamma 1, whereas sulfate showed no effect. At anion concentrations above 100 mM all isoenzymes were inhibited. At pH 10.5 beta 1 beta 1 and gamma 1 gamma 1 were not activated. Measuring the acetaldehyde reduction, no comparable activation by chloride was observed; all three isoenzymes were inhibited, at significantly lower anion concentrations. These anion effects can be correlated with the different primary structures of the isoenzymes around the active site and the coenzyme binding site.
There are 7 different ADH's isozymes in human: three belongs to class-I: alpha, beta, and gamma, one to class-II: pi, one to class-III: chi, one to class-IV: ADH7 and one to class-V: ADH6.
A reference proteome is a set of protein sequences derived from a complete proteome which constitutes a defined standard for a particular user community. Reference proteomes are manually defined according to a number of criteria. They cover the proteomes of well- studied model organisms and other proteomes of interest for biomedical and biotechnological research. Reference proteomes have been selected to provide broad coverage of the tree of life, and constitute a representative cross-section of the taxonomic diversity to be found within UniProtKB.
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