Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1984-1-7
|
pubmed:abstractText |
Glycerol kinase was found to associate with the hexokinase binding protein. The binding of glycerol kinase has a high specificity as illustrated by the fact that the magnitude of binding was reduced by glycerophosphate and antibodies against the hexokinase binding protein. A possible function of glycerol kinase binding to the mitochondria with respect to metabolic regulation is proposed for the following reasons: (i) Glycerol kinase seems to bind to the same binding protein as hexokinase. (ii) Both kinases were observed to be reversibly bound to the mitochondria in different metabolic situations, i.e., 10% of total cellular activity from both kinases is bound in starved rats whereas no activity of glycerol kinase and 30% of hexokinase become bound in fed rats. (iii) The kinetic properties of the associated glycerol kinase change in an analogous manner to those known for structure-bound hexokinase. (iv) With the binding of glycerol kinase to the mitochondria, it is possible to propose a metabolic pathway for glycerol oxidation to dihydroxyacetone phosphate by a combined action involving the enzyme, glycerol phosphate oxidase, and oxidative phosphorylation.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Dietary Carbohydrates,
http://linkedlifedata.com/resource/pubmed/chemical/Glycerol Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Hexokinase,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases
|
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
|
pubmed:issn |
0006-2944
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
30
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
231-45
|
pubmed:dateRevised |
2009-11-11
|
pubmed:meshHeading |
pubmed-meshheading:6316940-Adenosine Diphosphate,
pubmed-meshheading:6316940-Adenosine Triphosphate,
pubmed-meshheading:6316940-Animals,
pubmed-meshheading:6316940-Carrier Proteins,
pubmed-meshheading:6316940-Dietary Carbohydrates,
pubmed-meshheading:6316940-Fasting,
pubmed-meshheading:6316940-Glycerol Kinase,
pubmed-meshheading:6316940-Hexokinase,
pubmed-meshheading:6316940-Mitochondria, Liver,
pubmed-meshheading:6316940-Oxidation-Reduction,
pubmed-meshheading:6316940-Phosphotransferases,
pubmed-meshheading:6316940-Rats,
pubmed-meshheading:6316940-Rats, Inbred Strains
|
pubmed:year |
1983
|
pubmed:articleTitle |
The binding of glycerol kinase to the outer membrane of rat liver mitochondria: its importance in metabolic regulation.
|
pubmed:publicationType |
Journal Article
|