Linked Life Data

6351909

Source:http://linkedlifedata.com/resource/pubmed/id/6351909

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
1983-11-23
pubmed:abstractText
X-ray crystallographic studies indicate that His-51 in alcohol dehydrogenase may participate in a proton relay system during enzymatic catalysis [Eklund, H., Plapp, B. V., Samama, J.-P., & Brändén, C.-I. (1982) J. Biol. Chem. 257, 14349-14358], but there is no direct chemical evidence for this role. Diethyl pyrocarbonate (0.5-2 mM, pH 8, 25 degrees C) rapidly inactivated alcohol dehydrogenase, which was acetimidylated on all accessible lysine residues in order to prevent their modification. The reaction appeared to be specific for histidine residues, and the enzyme could be reactivated with 0.5 M hydroxylamine. The ethoxyformylated enzyme could still bind coenzymes, substrate analogues, and bipyridine, but with decreased affinity. The relationship between enzyme activity and the number of histidine residues modified showed that two histidine residues are modified during inactivation. NADH and isobutyramide significantly reduced the rate of inactivation, and the loss of activity then correlated with the modification of one to two histidine residues. The pH dependence of the inactivation showed the unusually high pK value of 9.6, which we attribute to the ionization of the water bound to zinc in the proton relay system. Although the histidine residue involved in the inactivation has not been identified, we conclude that one histidine residue (probably His-51) is essential for enzymatic activity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
22
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3721-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Involvement of histidine residues in the activity of horse liver alcohol dehydrogenase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.