Linked Life Data

8260493

Source:http://linkedlifedata.com/resource/pubmed/id/8260493

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
51
pubmed:dateCreated
1994-1-25
pubmed:abstractText
Epimers of [gamma-17O]adenosine 5'-O-(3-thiotriphosphate) ([gamma-17O]ATP gamma S) have been used to determine the stereochemistry of Mn2+ coordination to the terminal thiophosphoryl group in complexes of pyruvate kinase, oxalate, ATP gamma S, and Mg2+, Zn2+, Co2+, or Cd2+. The complex of pyruvate kinase with oxalate and ATP binds 2 equiv of divalent cation per active site. The terminal phosphoryl group of ATP in this enzymic complex becomes a chiral center as a result of coordination to both divalent metal ions. Electron paramagnetic resonance (EPR) data for complexes of pyruvate kinase with Rp- or Sp-[gamma-17O]-ATP gamma S, [17O]oxalate, and mixtures of Mn2+ with Mg2+, Zn2+, or Co2+ show that Mn2+ binds selectively at the site defined by coordination to oxalate and the pro-R oxygen of the thiophosphoryl group of ATP gamma S. In mixtures containing Mn2+ and Cd2+ with Tl+ as the monovalent cation, two hybrid complexes form, enzyme-oxalate-MnII-ATP gamma S-CdII and enzyme-oxalate-CdII-ATP gamma S-MnII, as in the analogous complexes with ATP and K+ or Tl+ (Buchbinder, J. L., & Reed, G. H. (1990) Biochemistry 29, 1799-1806). In the enzyme-oxalate-MnII-ATP gamma S-CdII species, Mn2+ binds exclusively to the pro-R oxygen of the thiophosphoryl group. In the enzyme-oxalate-CdII-ATP gamma S-MnII species, Mn2+ binds to the pro-R oxygen (60%) and to the pro-S oxygen (40%).(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
14111-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Stereochemistry of metal ion coordination to the terminal thiophosphoryl group of adenosine 5'-O-(3-thiotriphosphate) at the active site of pyruvate kinase.
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.