Ts. Huang et al., Cloning and characterization of a putative human D-2-hydroxyacid dehydrogenase in chromosome 9q, BIOC BIOP R, 268(2), 2000, pp. 298-301
Citations number
11
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
There is little information on D-isomer-specific dehydrogenases in humans.
Identification of D-2-hydroxy-glutaric aciduria, an inherited metabolic dis
order associated with severe neurological dysfunction, highlights the role
of D-isomers in human metabolism. The possibility of a defect in D-2-hydrox
yglutarate dehydrogenation prompted us to employ E, coli D-2-hydroxyacid de
hydrogenase cDNA to search the human expressed sequence tags database. Two
human EST homologues were retrieved and sequenced. Analysis showed the two
clones were identical with 1258 nucleotides encoding 248 amino acids of the
putative human D-2-hydroxyacid dehydrogenase, It was highly homologous to
bacterial D-2-hydroxyacid dehydrogenases (46%), D-phosphoglycerate dehydrog
enase (38%), and formate dehydrogenase (36%) at the amino acid level. The g
ene is expressed ubiquitously in tissue, most abundantly in liver, and was
mapped to chromosome 9q between markers WI-3028 and WI-93330, To our knowle
dge this is the first cloning and characterization of the cDNA for a human
D-isomer specific NAD(+)-dependent 2-hydroxyacid dehydrogenase. (C) 2000 Ac
ademic Press.