Linked Life Data

3203404

Source:http://linkedlifedata.com/resource/pubmed/id/3203404

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1989-2-6
pubmed:abstractText
The kinetics of hydrolysis of eight substituted phenyl hippurates by trypsin at pH values 6, 7 and 8 were investigated and the kinetic constants Km, kcat (kcatalysis) and kcat/Km were shown to fit the Hammett equation. The rho (rho) value obtained from the correlation of trypsin binding with this class of esters was compared with that obtained with other serine and cysteine proteases. The rho value for trypsin was similar to that obtained for alpha-chymotrypsin in that both enzymes reveal a pronounced dependence on through resonance (sigma-) in the formation of the Michaelis complex and the acyl-enzyme. It is apparent that through resonance facilitates the leaving of the phenoxy moiety during catalysis in the serine proteases but not in the case of the cysteine or bacterial serine proteases.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0009-2797
pubmed:author
pubmed:issnType
Print
pubmed:volume
68
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13-25
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Trypsin hydrolysis of X-phenyl hippurates.
pubmed:affiliation
Department of Chemistry, Pomona College, Claremont, CA 91711.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.