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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1993-9-30
|
| pubmed:abstractText |
The mechanism that has been proposed for glyoxalase II [36] is summarized in Figure 3. It involves direct nucleophilic attack of an active-site histidine on the thiol ester substrate to form an acyl-imidazole intermediate which then rapidly hydrolyses. This is consistent with the known susceptibility of thiol esters to aminolysis and with the lability of acyl-imidazoles [47].
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
0300-5127
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
21
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
522-7
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:8359524-Animals,
pubmed-meshheading:8359524-Binding Sites,
pubmed-meshheading:8359524-Humans,
pubmed-meshheading:8359524-Hydrogen-Ion Concentration,
pubmed-meshheading:8359524-Kinetics,
pubmed-meshheading:8359524-Pyruvaldehyde,
pubmed-meshheading:8359524-Substrate Specificity,
pubmed-meshheading:8359524-Thiolester Hydrolases
|
| pubmed:year |
1993
|
| pubmed:articleTitle |
Glyoxalase II: molecular characteristics, kinetics and mechanism.
|
| pubmed:affiliation |
Department of Biochemistry, University of New Mexico School of Medicine, Albuquerque 87131.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review
|