CONSTITUTIVE NADP-DEPENDENT ALCOHOL-DEHYDROGENASE OF ACINETOBACTER SPSTRAIN HO1-N

An NADP-dependent alcohol dehydrogenase was purified to homogeneity fr om Acinetobacter sp. strain HO1-N. The enzyme appears to be a tetramer of sub-unit M(r) 40,600, and it has kinetic and other properties almo st identical to those of an enzyme previously isolated from Acinetobac ter calcoaceticus strain NCIB 8250. The alcohol dehydrogenases from bo th of these strains of Acinetobacter oxidized primary alcohols. The hi ghest k(cat(app)) values were with alcohols containing from four to ei ght carbon atoms; there was activity up to tetradecan-1-ol, although i t was a poor substrate, but there was no measurable activity with hexa decan-1-ol. The highest specificity constant was found with hexan-1-ol as substrate when the measurements were made in the absence of dioxan , and with decan-1-ol as substrate when assayed in the presence of dio xan. It seems unlikely that this enzyme is involved in the metabolism of wax esters or of long-chain alkanes.