Linked Life Data

20964

Source:http://linkedlifedata.com/resource/pubmed/id/20964

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1977-12-29
pubmed:abstractText
The pH dependence of the human prostatic acid phosphatase-catalyzed hydrolysis of p-nitrophenyl phosphate and beta-glyceryl phosphate has been studied over a wide range of pH and the values of Km and V calculated with the aid of the Cleland HYPER program. The pH dependence of Km shows the effect of substrate ionization: pK values of 5.6 and 6.4 are observed as for the respective values of free substrates. The pH dependence of both Km and V for each substrate reveals the involvement of an ionizable group in the ES complex which is ascribed to a phosphohistidine-enzyme intermediate. The small deuterium solvent isotope effects which are observed on V are consistent with values observed for solvolysis of phosphoramidates. The measured data for Km indicates limits on burst-titration experiments of prostatic acid phosphatase (orthophosphoric-monoester phosphohydrolase, EC 3.1.3.2).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
484
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
386-97
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
pH dependence and solvent isotope effects in the hydrolysis of phosphomonoesters by human prostatic acid phosphatase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.