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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
19
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pubmed:dateCreated |
2005-8-22
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pubmed:abstractText |
Mandelate racemase has been studied as a paradigm for enzyme-catalyzed abstraction of a proton from carbon acids with relatively high pKa values. 1,1-Diphenyl-1-hydroxymethylphosphonate is a substrate-intermediate-product analogue and is a modest competitive inhibitor of the enzyme (Ki=1.41+/-0.09 mM), suggesting that simultaneous binding of the two phenyl groups obviates mimicry of the aci-carboxylate function of the intermediate by the phosphonate group.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0960-894X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4342-4
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16039120-Bacterial Proteins,
pubmed-meshheading:16039120-Binding, Competitive,
pubmed-meshheading:16039120-Binding Sites,
pubmed-meshheading:16039120-Enzyme Inhibitors,
pubmed-meshheading:16039120-Ligands,
pubmed-meshheading:16039120-Molecular Structure,
pubmed-meshheading:16039120-Organophosphorus Compounds,
pubmed-meshheading:16039120-Pseudomonas putida,
pubmed-meshheading:16039120-Racemases and Epimerases,
pubmed-meshheading:16039120-Structure-Activity Relationship
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pubmed:year |
2005
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pubmed:articleTitle |
Inhibition of mandelate racemase by the substrate-intermediate-product analogue 1,1-diphenyl-1-hydroxymethylphosphonate.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, Dalhousie University, Halifax, NS, Canada B3H 1X5.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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