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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
|
pubmed:dateCreated |
1993-11-17
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pubmed:abstractText |
Substrate specificity of 3-isopropylmalate dehydrogenase is analyzed using a series of synthetic (2R,3S)-3-alkylmalates. Each analog with hydrogen, methyl, ethyl, isopropyl, isobutyl, tert-butyl, and isoamyl group on C-3 functions as a substrate, implying a broad substrate specificity of the enzyme toward alkylmalates. The incremental binding energy of the isopropyl group of 3-isopropylmalate to the enzyme is estimated to be 3.55 kcal/mol, the rather small value supporting the broad specificity. Although the enzyme shows a broad specificity toward the alkylmalates, it does not show activity with isocitrate which has a negatively charged carboxymethyl group instead of the alkyl groups.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
|
pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
11
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pubmed:volume |
332
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
35-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading | |
pubmed:year |
1993
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pubmed:articleTitle |
Kinetic analysis on the substrate specificity of 3-isopropylmalate dehydrogenase.
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pubmed:affiliation |
Department of Life Science, Tokyo Institute of Technology, Yokohama, Japan.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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