Linked Life Data

7827101

Source:http://linkedlifedata.com/resource/pubmed/id/7827101

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-2-23
pubmed:abstractText
The reaction mechanisms of p-nitrophenyl phosphate hydrolysis catalyzed by two rat liver isoenzymes of the low M(r) phosphotyrosine protein phosphatase (AcP1 and AcP2) were compared. Furthermore, the effect of some heterocyclic compounds on their activities were tested. Cyclic GMP and guanosine causes a particularly high activation of the isoenzyme AcP2, whereas its effect on AcP1 is very poor. A study on the mechanism of cyclic GMP activation was carried out. The results suggest that cyclic GMP activates the AcP2 isoenzyme by increasing the rate of the step that leads to the hydrolysis of the covalent enzyme-substrate phosphorylated complex formed during the catalytic process. The physiological significance of cyclic GMP activation of only one of the two isoenzymes (AcP2) remains uncertain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
1243
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
129-35
pubmed:dateRevised
2007-11-19
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Kinetic studies on rat liver low M(r) phosphotyrosine protein phosphatases. The activation mechanism of the isoenzyme AcP2 by cGMP.
pubmed:affiliation
Department of Biochemical Sciences, University of Florence, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't