Mv. Gamble et al., Substrate specificities and 13-cis-retinoic acid inhibition of human, mouse and bovine cis-retinol dehydrogenases, BBA-PROT ST, 1476(1), 2000, pp. 3-8
Citations number
18
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
Recent studies of the human, mouse and bovine genes for 11-cis-retinol dehy
drogenase (11cRDH) and human and mouse 9-cis-retinol dehydrogenase (9cRDH)
suggest that they are homologs of the same enzyme. This conclusion is incon
sistent with earlier literature indicating that 11cRDH is expressed solely
in the eye and does not utilize 9-cis-retinol as a substrate. We have compa
red directly the kinetic properties of recombinant human and mouse 9cRDH wi
th those of bovine 11cRDH for 9-cis- and 11-cis-retinol and investigated th
e inhibitory properties of 13-cis-retinoic acid on each of these enzymes. H
uman and mouse 9cRDH and bovine 11cRDH have very similar kinetic properties
towards 9-cis- and 11-cis-retinol oxidation and they respond identically t
o 13-cis-retinoic acid inhibition. Our biochemical data are consistent with
the conclusion that 9cRDH and 11cRDH are the same enzyme. (C) 2000 Elsevie
r Science B.V. All rights reserved.