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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1975-12-5
|
| pubmed:abstractText |
Human platelet 6-phosphofructokinase (EC 2.7.1.11) shows cooperativity towards Fru-6-P and is allosterically inhibited by high Mg-ATP2- concentrations. No relation could be demonstrated between the cooperativity towards Fru-6-P and the inhibition by Mg-ATP2-. Increasing the concentrations of Mg-ATP2- only raised the apparent Km values for Fru-6-P, but did not change the Hill constants. A possible formation of a Mg-ATP2--enzyme-Fru-6-P complex during catalysis was investigated. Our calculations suggest that such a ternary complex is indeed formed during the reaction.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0006-3002
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
26
|
| pubmed:volume |
397
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
395-404
|
| pubmed:dateRevised |
2004-11-17
|
| pubmed:meshHeading |
pubmed-meshheading:125610-Adenosine Triphosphate,
pubmed-meshheading:125610-Allosteric Regulation,
pubmed-meshheading:125610-Binding Sites,
pubmed-meshheading:125610-Blood Platelets,
pubmed-meshheading:125610-Fructosephosphates,
pubmed-meshheading:125610-Humans,
pubmed-meshheading:125610-Kinetics,
pubmed-meshheading:125610-Magnesium,
pubmed-meshheading:125610-Mathematics,
pubmed-meshheading:125610-Phosphofructokinase-1,
pubmed-meshheading:125610-Protein Binding
|
| pubmed:year |
1975
|
| pubmed:articleTitle |
Human platelet 6-phosphofructokinase. Relation between inhibition by Mg-ATP2-and cooperativity towards fructose 6-phosphate and investigations on the formation of a ternary complex.
|
| pubmed:publicationType |
Journal Article
|