Linked Life Data

6243955

Source:http://linkedlifedata.com/resource/pubmed/id/6243955

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1980-5-23
pubmed:abstractText
2-[(R)-16O,17O,18O]Phospho-D-glycerate has been synthesized and used to determine the stereochemical course of each of the two mechanistic classes of phosphoglycerate mutases. The enzyme from rabbit muscle requires 2,3-bis-phospho-D-glycerate as a cofactor and catalyzes an intermolecular phosphoryl group transfer reaction. The enzyme from wheat germ requires no cofactor and catalyzes an intramolecular transfer of the phosphoryl group. We have shown that the reaction catalyzed by each of these enzymes proceeds with overall retention of the configuration at phosphorus. This stereochemical result is consistent with a double-displacement pathway involving a single phosphorylenzyme, for each of the catalyzed reactions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
738-43
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Phosphoglycerate mutases: stereochemical course of the phosphoryl group transfers catalyzed by the cofactor-dependent enzyme from rabbit muscle and the cofactor-independent enzyme from wheat germ.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.