Alcohol dehydrogenase different species

The first step in the complete biodegradation of primary alcohol sulfates seems to be the hydrolysis to yield alcohol. Sulfatases are able to hydrolyze primary alcohol sulfates. Different authors have isolated and used several sulfia-tase enzymes belonging to Pseudomonas species. The alcohol obtained as a result of the hydrolysis, provided that dehydrogenases have been removed to avoid the oxidation of the alcohol, was identified by chromatography and other methods [388-394]. The absence of oxygen uptake in the splitting of different primary alcohol sulfates also confirms the hydrolysis instead of oxidation [395, 396]. The hydrolysis may acidify the medium and stop the bacterial growth in the absence of pH control [397-399]. 

There exists a large literature on enzyme polymorphism and species adaptation (91), but none of it can as yet be interpreted in stereochemical terms. The best-studied species is Drosophila melanogaster, in which the frequency of the two dominant alleles of alcohol dehydrogenase varies with latitude in several continents one of these alleles has a consistently lower Michaelis constant for alcohols than the other (92). The two enzymes have been found to differ by the single substitution of a lysine for... 

Variations in the structures of enzymes within a species can also occur between and within ethnic groups of the same species. For example, a number of different alcohol dehydrogenase isoenzymes have been observed in some Asians. 

In higher organisms, isozymes frequently have different organal distributions (62,66,471). In this respect, the retinal alcohol dehydrogenase was of special interest because of its possible role in conversion of retinene (1,473). The retinal enzyme, however, apparently lacks this capacity and is different from the liver enzyme (81,474). ADH also occurs in other organs outside the liver (62,66,476,476). Different intracellular distributions of isozymes (477) and an isozyme dependency on the culture medium (478) are also known for other species than the Saccharomyces (Section III,A). Completely (Section IV,C 479) or partially (480) ADH-deficient mutants are known in some species. 

Mitochondrial malate dehydrogenase (MDH) from several species has been shown to exist in several enzymically active forms which also appear to be conformational isoenzymes (Kitto et al, 1966, 1970). Kitto et al (1970) showed, in contrast to Epstein and Schechter (1968), that these MDH s were interconvertible in vitro, had the same amino acid compositions and molecular weights, but differed, once reversibly denatured, considerably in their heat stability. Similar interconversion of isoenzymes has also been observed with purified preparations of horse liver alcohol dehydrogenase (Lutstorf and von Wartburg, 1969). The question arises if such conformers are of any physiological or functional significance. It is possible that beeause of their differences in surface charge, the various conformative isoenzymes are differently bound within a cell. 

When a mixture containing AMP (0.5 nmol), ADP (0.2 nmol) and ADP-ribose (1 nmol) is applied to an alcohol dehydrogenase-silica column [see Section 4.2.3(iii)] under isocratic conditions, separation of the three species is achieved on the basis of the different strength of interaction between the silica-immobilized enzyme and the three nucleotides Figure 6) (21). 

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