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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
|
| pubmed:dateCreated |
1995-1-23
|
| pubmed:abstractText |
The configuration and conformation of a compound are critical factors that determine whether it can be accepted by an enzyme as a substrate or not. We have examined enzyme-catalyzed decarboxylation of some alpha-substituted malonic acids and proposed that the syn-periplanar conformation is required for the substrates to be bound to the active site of the enzyme. Theoretical calculation of potential energy surfaces also supports the conclusion from experimental results.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0968-0896
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
2
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
469-75
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8000869-Alcaligenes,
pubmed-meshheading:8000869-Carboxy-Lyases,
pubmed-meshheading:8000869-Magnetic Resonance Spectroscopy,
pubmed-meshheading:8000869-Malonates,
pubmed-meshheading:8000869-Models, Molecular,
pubmed-meshheading:8000869-Molecular Conformation,
pubmed-meshheading:8000869-Polarography,
pubmed-meshheading:8000869-Substrate Specificity,
pubmed-meshheading:8000869-Thermodynamics
|
| pubmed:year |
1994
|
| pubmed:articleTitle |
Effect of conformation of the substrate on enzymatic decarboxylation of alpha-arylmalonic acid.
|
| pubmed:affiliation |
Department of Chemistry, Keio University, Yokohama, Japan.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|