Linked Life Data

8162187

Source:http://linkedlifedata.com/resource/pubmed/id/8162187

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1994-5-20
pubmed:databankReference
pubmed:abstractText
An NADP-dependent constitutive alcohol dehydrogenase that can oxidize hexan-1-ol was detected in several Gram-positive and Gram-negative eubacteria and in two yeasts. The enzyme was purified to homogeneity from Acinetobacter calcoaceticus NCIB 8250 and from Saccharomyces cerevisiae D273-10B. The bacterial enzyme appears to be a tetramer of subunit M(r) 40,300 and the yeast enzyme appears to be a monomer of subunit M(r) 43,500. The N-terminal amino acid sequence of the bacterial enzyme has 34% identity with part of the sequence of a fermentative alcohol dehydrogenase from Escherichia coli. The pI value of the bacterial enzyme was 5.7 and the pH optimum was 10.2. Both the bacterial and yeast enzymes were shown to transfer the pro-R hydrogen to/from NADP(H). The substrate specificities of the two enzymes were similar to each other, both oxidizing primary alcohols and some diols, but not secondary alcohols. The maximum velocities of both enzymes were with pentan-1-ol as substrate and there was very low activity with ethanol; the maximum specificity constants were found with primary alcohols containing six to eight carbon atoms. Neither enzyme was significantly inhibited by metal-binding agents but some thiol-blocking compounds inhibited them. It appears that these two alcohol dehydrogenases, on prokaryotic and one eukaryotic, are structurally, kinetically and functionally different from members of the major known groups of alcohol dehydrogenases.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1350-0872
pubmed:author
pubmed:issnType
Print
pubmed:volume
140 ( Pt 1)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
173-83
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
NADP-dependent alcohol dehydrogenases in bacteria and yeast: purification and partial characterization of the enzymes from Acinetobacter calcoaceticus and Saccharomyces cerevisiae.
pubmed:affiliation
Department of Biochemistry, University of Glasgow, UK.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't