Linked Life Data

12210547

Source:http://linkedlifedata.com/resource/pubmed/id/12210547

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2002-9-4
pubmed:abstractText
Two methanol dehydrogenases (MDHs), MDH1 and MDH2, were purified from a marine methylotroph, Methylophaga sp. strain 1. Both enzymes had very similar properties, including the same native molecular weight, sizes of subunits and substrate specificity. The N-terminal amino acid sequence of the alpha-subunit of MDH2 differed from that of MDH1 by having a histidine residue at a highly conserved glutamate position, but both sequences showed approximately 50% homology to the alpha-subunits of other MDHs. MDH1 had higher specific activity than MDH2 with respect to methanol and ethanol as a substrate. The two enzymes did not appear to be isoforms but that either MDH1 or MDH2 could be a mutant arising from spontaneous mutation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0233-111X
pubmed:author
pubmed:issnType
Print
pubmed:volume
42
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
238-45
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Purification and characterization of two forms of methanol dehydrogenases from a marine methylotroph.
pubmed:affiliation
Department of Biological Sciences and Research Center for Proteineous Materials, Chosun University, Gwangju 501-759, Republic of Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't