Linked Life Data

566117

Source:http://linkedlifedata.com/resource/pubmed/id/566117

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1978-8-14
pubmed:abstractText
Rabbit muscle pyruvate kinase has been shown to catalyze the decarboxylation of oxalacetate (Creighton, D.J. and Rose, I.A. (1976) J. Biol. Chem. 251, 61). Noncovalent and covalent modifiers of the enzyme have been used to assess whether the decarboxylase and kinase reactions take place at a common site. Phosphoenol-alpha-ketobutyrate, an analog of the substrate phosphoenol-pyruvate, inhibits decarboxylase and kinase competitively and with nearly identical Ki values (5.7 micron and 4.8 micron, respectively). Oxalate, an analog of enol-pyruvate, inhibits each competitively and with similar Ki values (11 micron and 4.7 micron, respectively). Both activities are lost in parallel upon reaction with dithionitrobenzoate, which is active-site specific. These results indicate that the two activities share a common site on the enzyme. But, effects of the following modifiers suggest that different amino acid residues at that site participate in the two reactions: phenylalanine inhibition and fructose 1,6-bisphosphate activation are more effective with the decarboxylase; iodoacetamide preferentially inactivates decarboxylase while trinitrobenzenesulfonate preferentially inactivates kinase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
523
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
358-67
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
The active site of rabbit muscle pyruvate kinase. Evidence for a site common to the oxalacetate decarboxylase and pyruvate kinase reactions.
pubmed:publicationType
Journal Article