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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
9-10
|
| pubmed:dateCreated |
1990-2-1
|
| pubmed:abstractText |
The dnaK protein of Escherichia coli has been shown to possess both autophosphorylating and 5'-nucleotidase activities. The dnaK protein has been shown to bind avidly to ATP, but hydrolyzing it slowly. In vitro autophosphorylation occurs at a threonine residue when either ATP or GTP are used as phosphate donors. The extent of autophosphorylation is low; only a few percent of the molecules are phosphorylated. This activity is stimulated at least tenfold in the presence of Ca2+ ions with either ATP or GTP as the donor. The autophosphorylating activity of the mutant dnaK756 protein in the presence or absence of Ca2+ is reduced compared to that of the wild type.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0300-9084
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
71
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1071-7
|
| pubmed:dateRevised |
2000-12-18
|
| pubmed:meshHeading |
pubmed-meshheading:2512998-Amino Acids,
pubmed-meshheading:2512998-Calcium,
pubmed-meshheading:2512998-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:2512998-Escherichia coli,
pubmed-meshheading:2512998-Guanosine Triphosphate,
pubmed-meshheading:2512998-Heat-Shock Proteins,
pubmed-meshheading:2512998-Mutation,
pubmed-meshheading:2512998-Phosphorylation
|
| pubmed:articleTitle |
Biochemical properties of the Escherichia coli dnaK heat shock protein and its mutant derivatives.
|
| pubmed:affiliation |
Department of Cellular, Viral and Molecular Biology, University of Utah Medical Center, Salt Lake City 84132.
|
| pubmed:publicationType |
Journal Article
|