Linked Life Data

2166476

Source:http://linkedlifedata.com/resource/pubmed/id/2166476

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1990-9-7
pubmed:abstractText
Complexes of the oxocation of vanadyl(IV), VO2+, with pyruvate kinase from rabbit muscle have been investigated by steady-state kinetic assays and by EPR spectroscopy. Pyruvate kinase requires 2 eq of divalent cation for activity. VO2+ alone is a poor activator of the normal physiological reaction catalyzed by the enzyme and of the enzyme-catalyzed exchange of the methyl protons of pyruvate with solvent. VO2+ alone is, however, an activator of the enzyme-catalyzed phosphorylation of glycolate by ATP. VO2+ is more effective than Mg2+ in activation of the bicarbonate-dependent ATPase reaction of pyruvate kinase, and in the enzyme-catalyzed hydrolysis of phosphoenolpyruvate. EPR data show that VO2+ binds to the divalent cation site on the protein competitively with respect to Mg2+. The VO2+-enzyme complex has a high affinity for bicarbonate. Direct coordination of pyruvate, oxalate, and glycolate to the enzyme-bound VO2+ has been established by EPR measurements with specifically 17O-labeled forms of these compounds.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
281
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
124-31
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Vanadyl(IV) complexes with pyruvate kinase: activation of the enzyme and electron paramagnetic resonance properties of ternary complexes with the protein.
pubmed:affiliation
Institute for Enzyme Research, Graduate School, University of Wisconsin, Madison 53705.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.