Linked Life Data

1567427

Source:http://linkedlifedata.com/resource/pubmed/id/1567427

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1992-5-20
pubmed:abstractText
Previously, we reported the importance of Tyr7 for the catalytic activity of human class Pi glutathione S-transferase [Kong et al. (1992) Biochem. Biophys. Res. Comm., 182, 1122]. As an extension of this study, we investigated the pH dependence of kinetic parameters of the wild-type enzyme and the Y7F mutant. The replacement of Tyr7 with phenylalanine was found to alter the pH dependence of Vmax and Vmax/KmCDNB of the enzyme for conjugation of GSH with 1-chloro-2,4-dinitrobenzene (CDNB). The pKa of the thiol of GSH in the wild-type enzyme-GSH complex was estimated to be about 2.4 pK units lower than that in the Y7F-GSH complex. Tyr7 is thus considered to be important for catalytic activity in lowering the pKa of the thiol of GSH in the enzyme-GSH complex.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
184
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
194-7
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Tyrosine-7 in human class Pi glutathione S-transferase is important for lowering the pKa of the thiol group of glutathione in the enzyme-glutathione complex.
pubmed:affiliation
Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Japan.
pubmed:publicationType
Journal Article