Linked Life Data

12453632

Source:http://linkedlifedata.com/resource/pubmed/id/12453632

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2002-11-27
pubmed:abstractText
After extraction and purification, the kinetic behavior of the Ca(2+)/calmodulin-dependent protein kinase II (CaM kinase II) from horse brain was investigated as a function of ATP and a synthetic substrate, syntide-2. Both phospho- and dephospho- forms of the enzyme obey a bi-bi random mechanism. The K(M)s for ATP (K(M,ATP)) and syntide-2 (K(M,syntide-2)) were determined as equal to 80 and 30 microM, respectively. However, the maximum reaction yield is decreased by 50% when the enzyme is (auto)phosphorylated. In addition, this phosphorylated form of the enzyme leads to the formation of a totally Ca(2+)-independent state of activity.
pubmed:language
eng
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:author
pubmed:copyrightInfo
Copyright 2002 Société françcaise de biochimie et biologie moléculaire / Editions scientifiques et médicales Elsevier SAS
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
605-10
pubmed:dateRevised
2007-11-15
pubmed:articleTitle
Effect of (auto)phosphorylation on the kinetic behavior of the Ca2+/calmodulin-dependent protein kinase II from horse brain.
pubmed:affiliation
UPRESA no 6022 du CNRS, Génie Enzymatique et Cellulaire, BP 20529, Université de Compiègne, 60205 Compiègne cedex, France.