Linked Life Data

3611058

Source:http://linkedlifedata.com/resource/pubmed/id/3611058

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
1987-9-4
pubmed:abstractText
The Ca2+-activated, phospholipid-dependent protein kinase C autophosphorylates by an intrapeptide reaction in a mixed micelle system in which the enzyme is a monomer. The rate of autophosphorylation in the micellar system is comparable to that observed in bilayer systems, where the enzyme may exist as an oligomer. Trypsinolysis of the enzyme reveals that both the regulatory and catalytic domains of the molecule are modified by the intrapeptide phosphorylation. Proteolysis of the enzyme to separate the two domains results in loss of ability to autophosphorylate. Furthermore, intact protein kinase C cannot phosphorylate either the cleaved regulatory or catalytic domains. Kinetic and proteolytic analyses suggest that intrapeptide phosphorylation is the predominant, and perhaps only, mechanism by which protein kinase C autophosphorylates. The intrapeptide modification of protein kinase C has intriguing implications for protein structure and regulation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
262
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10185-8
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Protein kinase C autophosphorylates by an intrapeptide reaction.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.