|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0001480,
umls-concept:C0004083,
umls-concept:C0019472,
umls-concept:C0086418,
umls-concept:C0449432,
umls-concept:C0678594,
umls-concept:C1167622,
umls-concept:C1179435,
umls-concept:C1524073,
umls-concept:C1548799,
umls-concept:C1705248,
umls-concept:C2587213
|
|
pubmed:issue |
11
|
|
pubmed:dateCreated |
1999-12-14
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
Hexokinase I sets the pace of glycolysis in the brain, catalyzing the ATP-dependent phosphorylation of glucose. The catalytic properties of hexokinase I are dependent on product inhibition as well as on the action of phosphate. In vivo, a large fraction of hexokinase I is bound to the mitochondrial outer membrane, where the enzyme adopts a tetrameric assembly. The mitochondrion-bound hexokinase I is believed to optimize the ATP/ADP exchange between glucose phosphorylation and the mitochondrial oxidative phosphorylation reactions.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Nov
|
|
pubmed:issn |
0969-2126
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
15
|
|
pubmed:volume |
7
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
1427-37
|
|
pubmed:dateRevised |
2006-11-15
|
|
pubmed:meshHeading |
pubmed-meshheading:10574795-Adenosine Triphosphate,
pubmed-meshheading:10574795-Amino Acid Sequence,
pubmed-meshheading:10574795-Binding Sites,
pubmed-meshheading:10574795-Catalysis,
pubmed-meshheading:10574795-Cell Membrane,
pubmed-meshheading:10574795-Crystallography, X-Ray,
pubmed-meshheading:10574795-Glucose,
pubmed-meshheading:10574795-Glucose-6-Phosphate,
pubmed-meshheading:10574795-Hexokinase,
pubmed-meshheading:10574795-Humans,
pubmed-meshheading:10574795-Models, Molecular,
pubmed-meshheading:10574795-Molecular Sequence Data,
pubmed-meshheading:10574795-Protein Binding,
pubmed-meshheading:10574795-Protein Conformation,
pubmed-meshheading:10574795-Protein Folding,
pubmed-meshheading:10574795-Recombinant Proteins,
pubmed-meshheading:10574795-Sequence Homology, Amino Acid
|
|
pubmed:year |
1999
|
|
pubmed:articleTitle |
Binding of non-catalytic ATP to human hexokinase I highlights the structural components for enzyme-membrane association control.
|
|
pubmed:affiliation |
Dipartimento di Fisica - INFM, Centro Biotecnologie Avanzate - IST, Universita' di Genova, Genova, 10. I-16132, Italy.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
