Linked Life Data

3360009

Source:http://linkedlifedata.com/resource/pubmed/id/3360009

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1988-5-31
pubmed:abstractText
The zinc ion in the noncatalytic site of human beta 1 beta 1 and beta 1 gamma 1 isozymes of class I alcohol dehydrogenases (EC 1.1.1.1) was specifically replaced by Co(II) ion. The absorption and CD spectra prove that these derivatives contain cobalt bound at the noncatalytic site to the same ligands and in the same coordination geometry as in the corresponding species obtained from the horse liver EE isozyme. These Zn(c)2Co(n)2 human liver alcohol dehydrogenases could be obtained in two ways: (a) by exchange dialysis, (b) by removal of the noncatalytic zinc and subsequent insertion of cobalt(II) ion into the empty site. The human isozymes differ from the horse liver EE enzyme in the possibility of forming stable species lacking the noncatalytic zinc ion. This difference in chemical reactivity of the noncatalytic zinc atom may be related to amino acid changes in the human isozymes, compared to horse liver alcohol dehydrogenase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
173
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
281-5
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
H8Zn(c)2 and Zn(c)2Co(n)2 human liver alcohol dehydrogenase.
pubmed:affiliation
Fachrichtung 14.4-Biochemie, Universität des Saarlandes, Saarbrücken, Federal Republic of Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't