Linked Life Data

2529853

Source:http://linkedlifedata.com/resource/pubmed/id/2529853

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1989-11-13
pubmed:abstractText
A tetrameric enzyme form of phosphofructokinase from yeast (called 12 S-enzyme), formed by limited proteolysis of the octameric enzyme in the presence of ATP and by subsequent dissociation in two half-molecules shows sigmoidal kinetics with respect to fructose 6-phosphate and inhibition by ATP. Similar to the native phosphofructokinase, the modified enzyme is also efficiently activated by AMP and fructose 2,6-bisphosphate. Both activators increase the affinity for the substrate fructose 6-phosphate and the respective maximum activity. In contrast to the native phosphofructokinase, however, both AMP and fructose 2,6-bisphosphate change the sigmoidal fructose 6-phosphate velocity curve into a hyperbolic one. AMP and fructose 2,6-bisphosphate decrease the ATP inhibition, probably by modulating the affinity of the allosteric sites to ATP.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0232-766X
pubmed:author
pubmed:issnType
Print
pubmed:volume
48
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
387-92
pubmed:dateRevised
2001-11-2
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Phosphofructokinase from baker's yeast: kinetic properties of a proteolytically modified enzyme.
pubmed:affiliation
Institut für Biochemie, Karl-Marx-Universität Leipzig, DDR.
pubmed:publicationType
Journal Article