Structural and mechanistic similarities of 6-phosphogluconate and 3- hydroxyisobutyrate dehydrogenases reveal a new enzyme family, the 3- hydroxyacid dehydrogenases

John W. Hawes, Edwin T. Harper, David W. Crabb, Robert A. Harris

Research output: Contribution to journalArticlepeer-review

35 Scopus citations

Abstract

Rat 3-hydroxyisobutyrate dehydrogenase exhibits significant amino acid sequence homology with 6-phosphogluconate dehydrogenase, D-phenylserine dehydrogenase from Pseudomonas syringae, and a number of hypothetical proteins encoded by genes of microbial origin. Key residues previously proposed to have roles in substrate binding and catalysis in sheep 6- phosphogluconate dehydrogenase are highly conserved in this entire family of enzymes. Site-directed mutagenesis, chemical modification, and substrate specificity studies were used to compare possible mechanistic similarities of 3-hydroxyisobutyrate dehydrogenase with 6-phosphogluconate dehydrogenase. The data suggest that 3-hydroxyisobutyrate and 6-phosphogluconate dehydrogenases may comprise, in part, a previously unrecognized family of 3-hydroxyacid dehydrogenases.

Original languageEnglish (US)
Pages (from-to)263-267
Number of pages5
JournalFEBS Letters
Volume389
Issue number3
DOIs
StatePublished - Jul 8 1996

Keywords

  • 3-Hydroxyisobutyrate
  • 6-Phosphogluconate
  • Dehydrogenase
  • Pyridoxal phosphate

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Fingerprint Dive into the research topics of 'Structural and mechanistic similarities of 6-phosphogluconate and 3- hydroxyisobutyrate dehydrogenases reveal a new enzyme family, the 3- hydroxyacid dehydrogenases'. Together they form a unique fingerprint.

Cite this