Linked Life Data

8944774

Source:http://linkedlifedata.com/resource/pubmed/id/8944774

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1997-1-13
pubmed:databankReference
pubmed:abstractText
A glutathione-dependent formaldehyde dehydrogenase (class III alcohol dehydrogenase) has been characterized from Arabidopsis thaliana. This plant enzyme exhibits kinetic and molecular properties in common with the class III forms from mammals, with a K(m) for S-hydroxymethylglutathione of 1.4 microM, an anodic electrophoretic mobility (pI: 5.3-5.6) and a cross-reaction with anti-(rat class III alcohol dehydrogenase) antibodies. The enzyme structure, deduced from the cDNA sequence, fits into the complex system of alcohol dehydrogenases and shows that all life forms share the class III protein type. The corresponding mRNA is 1.4 kb and present in all plant organs; a single copy of the gene is found in the genome. The class III structural variability is different from that of the ethanol-active enzyme types in both vertebrates (class I) and plants (class P), although class P conserves more of the class III properties than class I does. Also the enzymatic properties differ between the two ethanol-active classes. Active-site variability and exchanges at essential residues (Leu/Gly57, Asp/Arg115) may explain the distinct kinetics. These patterns are consistent with two different metabolic roles for the ethanol-active enzymes, a more constant function, reduction of acetaldehyde during hypoxia, for class P, and a more variable function, the detoxication of alcohols and participation in metabolic conversions, for class I. A sequence motif, Pro-Xaa-Ile/Val-Xaa-Gly-His-Glu-Xaa-Xaa-Gly, common to all medium-chain alcohol dehydrogenases is defined.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
241
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
849-57
pubmed:dateRevised
2007-7-27
pubmed:meshHeading
pubmed-meshheading:8944774-Alcohol Dehydrogenase, pubmed-meshheading:8944774-Aldehyde Oxidoreductases, pubmed-meshheading:8944774-Amino Acid Sequence, pubmed-meshheading:8944774-Arabidopsis, pubmed-meshheading:8944774-Arabidopsis Proteins, pubmed-meshheading:8944774-Base Sequence, pubmed-meshheading:8944774-Binding Sites, pubmed-meshheading:8944774-Computer Simulation, pubmed-meshheading:8944774-DNA, Complementary, pubmed-meshheading:8944774-Dimerization, pubmed-meshheading:8944774-Gene Library, pubmed-meshheading:8944774-Glutathione Reductase, pubmed-meshheading:8944774-Models, Molecular, pubmed-meshheading:8944774-Molecular Sequence Data, pubmed-meshheading:8944774-Phylogeny, pubmed-meshheading:8944774-Protein Conformation, pubmed-meshheading:8944774-RNA, Plant, pubmed-meshheading:8944774-Sequence Analysis, DNA, pubmed-meshheading:8944774-Sequence Homology, Amino Acid
pubmed:year
1996
pubmed:articleTitle
Arabidopsis formaldehyde dehydrogenase. Molecular properties of plant class III alcohol dehydrogenase provide further insights into the origins, structure and function of plant class p and liver class I alcohol dehydrogenases.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, Spain.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't