Abstract
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.
MeSH terms
-
Adenosine Monophosphate / metabolism
-
Alcohol Oxidoreductases*
-
Amino Acid Sequence
-
Bacterial Proteins
-
Binding Sites
-
Carbohydrate Dehydrogenases* / genetics*
-
Escherichia coli / enzymology*
-
Escherichia coli Proteins*
-
Hydroxypyruvate Reductase
-
L-Lactate Dehydrogenase
-
Malate Dehydrogenase
-
Molecular Sequence Data
-
NAD / pharmacology
-
Phosphoglycerate Dehydrogenase
-
Plants / enzymology*
-
Pyridoxine / biosynthesis
-
Sequence Homology, Nucleic Acid
Substances
-
Bacterial Proteins
-
Escherichia coli Proteins
-
NAD
-
Adenosine Monophosphate
-
Alcohol Oxidoreductases
-
Carbohydrate Dehydrogenases
-
pdxB protein, E coli
-
L-Lactate Dehydrogenase
-
Glycerate dehydrogenase
-
Malate Dehydrogenase
-
Hydroxypyruvate Reductase
-
Phosphoglycerate Dehydrogenase
-
Pyridoxine