Linked Life Data

7024272

Source:http://linkedlifedata.com/resource/pubmed/id/7024272

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
1981-11-22
pubmed:abstractText
Fluoromethylglyoxal in the presence of glutathione has been shown to undergo a novel glyoxalase I-catalyzed product partitioning to S-fluorolactoylglutathione and S-pyruvylglutathione with fluoride elimination. While the partition ratio (fluoride eliminated/total fluoride) was insensitive to pH 5.5-7.5 and concentrations of substrate and glyoxalase I, it was species-dependent. When [1-2H]fluoromethylglyoxal was reacted with glyoxalase I, an increase in the partition ratio and retention of deuterium in the product fluorolactate was observed. This result can only be explained by a selective primary isotope effect on the protonation of an enediol intermediate relative to fluoride elimination.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
256
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9785-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Deuterium isotope effects on the product partitioning of fluoromethylglyoxal by glyoxalase I. Proof of a proton transfer mechanism.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.