Linked Life Data

1835381

Source:http://linkedlifedata.com/resource/pubmed/id/1835381

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1991-12-12
pubmed:abstractText
The steady state kinetics of 6-phosphofructo-1-kinase was determined in a cell-free extract obtained from a yeast mutant (DFY 250) and compared with the kinetic properties of the enzyme of a wild-type strain (DFY 1). 6-Phosphofructo-1-kinase from the DFY 250 strain shows a complex kinetic behaviour, which is qualitatively similar to, but quantitatively different from, that of normal yeast 6-phosphofructo-1-kinase. The mutant enzyme has a lower affinity to its activators fructose 6-phosphate, fructose 2,6-bisphosphate and AMP. The inhibiting effect of ATP on the mutant 6-phosphofructo-1-kinase is substantially weaker than on the wild-type enzyme. A complex interaction between fructose 6-phosphate and fructose 2,6-bisphosphate at the 6-phosphofructo-1-kinase from strain DFY 250 is reflected by a remarkable substrate inhibition by fructose 6-phosphate even at saturating fructose 2,6-bisphosphate. The kinetic data were fitted to different variants of the Monod-Wyman-Changeux model by nonlinear regression analysis. It turned out that the influence of fructose 6-phosphate, ATP, AMP and fructose 2,6-bisphosphate on the activity of 6-phosphofructo-1-kinase from wild-type and DFY 250 strain could be described by rate equations of essentially the same structure.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0232-766X
pubmed:author
pubmed:issnType
Print
pubmed:volume
50
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
239-50
pubmed:dateRevised
2001-11-2
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Kinetics of 6-phosphofructo-1-kinase from a yeast mutant.
pubmed:affiliation
Institute of Biochemistry, University of Leipzig, FRG.
pubmed:publicationType
Journal Article