Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1993-11-17
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
332
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
35-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Kinetic analysis on the substrate specificity of 3-isopropylmalate dehydrogenase.
pubmed:affiliation
Department of Life Science, Tokyo Institute of Technology, Yokohama, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't