Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1990-2-13
pubmed:abstractText
The NADH-dependent hydroxypyruvate reductase from cucumber and the pdxB gene product of E. coli display significant homology to E. coli D-3-phosphoglycerate dehydrogenase. In contrast, these proteins do not display much similarity with other oxidoreductases or with other 2-hydroxyacid dehydrogenases in particular. On the basis of their relatedness and the structure of their substrates, these three enzymes constitute a new family of 2-hydroxyacid dehydrogenases distinct from malate and lactate dehydrogenase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Monophosphate, http://linkedlifedata.com/resource/pubmed/chemical/Alcohol Oxidoreductases, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carbohydrate Dehydrogenases, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Glycerate dehydrogenase, http://linkedlifedata.com/resource/pubmed/chemical/Hydroxypyruvate Reductase, http://linkedlifedata.com/resource/pubmed/chemical/L-Lactate Dehydrogenase, http://linkedlifedata.com/resource/pubmed/chemical/Malate Dehydrogenase, http://linkedlifedata.com/resource/pubmed/chemical/NAD, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoglycerate Dehydrogenase, http://linkedlifedata.com/resource/pubmed/chemical/Pyridoxine, http://linkedlifedata.com/resource/pubmed/chemical/pdxB protein, E coli
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
165
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1371-4
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:2692566-Adenosine Monophosphate, pubmed-meshheading:2692566-Alcohol Oxidoreductases, pubmed-meshheading:2692566-Amino Acid Sequence, pubmed-meshheading:2692566-Bacterial Proteins, pubmed-meshheading:2692566-Binding Sites, pubmed-meshheading:2692566-Carbohydrate Dehydrogenases, pubmed-meshheading:2692566-Escherichia coli, pubmed-meshheading:2692566-Escherichia coli Proteins, pubmed-meshheading:2692566-Hydroxypyruvate Reductase, pubmed-meshheading:2692566-L-Lactate Dehydrogenase, pubmed-meshheading:2692566-Malate Dehydrogenase, pubmed-meshheading:2692566-Molecular Sequence Data, pubmed-meshheading:2692566-NAD, pubmed-meshheading:2692566-Phosphoglycerate Dehydrogenase, pubmed-meshheading:2692566-Plants, pubmed-meshheading:2692566-Pyridoxine, pubmed-meshheading:2692566-Sequence Homology, Nucleic Acid
pubmed:year
1989
pubmed:articleTitle
A new family of 2-hydroxyacid dehydrogenases.
pubmed:affiliation
Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110.
pubmed:publicationType
Journal Article, Comparative Study