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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
1997-1-15
|
| pubmed:abstractText |
D-Lactate dehydrogenases (D-LDHs) and L-lactate dehydrogenases (L-LDHs) catalyze a reaction differing only in the chirality of the product. Both enzymes utilize the same kind of amino acid side chains in substrate binding and catalysis. Models based on D-LDH-related enzymes propose that these side chains assume identical roles in both enzymes with their active sites related by a simple geometrical relationship such as a mirror plane.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
0969-2126
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
4
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
437-47
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8740366-Binding Sites,
pubmed-meshheading:8740366-Crystallography, X-Ray,
pubmed-meshheading:8740366-L-Lactate Dehydrogenase,
pubmed-meshheading:8740366-Lactobacillus,
pubmed-meshheading:8740366-Models, Molecular,
pubmed-meshheading:8740366-Oxidoreductases,
pubmed-meshheading:8740366-Protein Conformation,
pubmed-meshheading:8740366-Sequence Homology, Amino Acid
|
| pubmed:year |
1996
|
| pubmed:articleTitle |
Insights into substrate binding by D-2-ketoacid dehydrogenases from the structure of Lactobacillus pentosus D-lactate dehydrogenase.
|
| pubmed:affiliation |
Department of Biochemistry, University of Toronto, Ontario, Canada.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|