Linked Life Data

161131

Source:http://linkedlifedata.com/resource/pubmed/id/161131

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1980-4-26
pubmed:abstractText
Phosphofructokinase from baker's yeast (Saccharomyces cerevisiae) is an octameric enzyme which exhibits complex allosteric behaviour. In contrast to mammalian phosphofructokinase, the enzyme does not show association-dissociation behaviour. A systematic kinetic investigation at pH 7.2 in dependence on the substrates, fructose 6-phosphate and ATP as well as on the effectors AMP and ADP is presented. The results are interpreted in terms of a structure oriented theoretical model. Because the two state model of Monod, Wyman and Changeux proved to be insufficient for interpretation of the experimental data, it was extended to a four state model in which the basic conformations R and T of the enzyme are split into subconformations R1 and R2 as well as T1 and T2, respectively. It is assumed that fructose 6-phosphate and the adenine nucleotides influence different allosteric equilibria. The model permits a precise quantitative description of the experimental data.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0001-5318
pubmed:author
pubmed:issnType
Print
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1067-79
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Kinetic modelling of yeast phosphofructokinase.
pubmed:publicationType
Journal Article