A new family of 2-hydroxyacid dehydrogenases

Biochem Biophys Res Commun. 1989 Dec 29;165(3):1371-4. doi: 10.1016/0006-291x(89)92755-1.

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.

Publication types

  • Comparative Study

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