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PMID: 10606761 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Substrate specificities and 13-cis-retinoic acid inhibition of human, mouse and bovine cis-retinol dehydrogenases.

Biochimica et biophysica acta ·Vol. 1476 ·No. 1 ·2000-01-03 ·Pages 3-8

Gamble MV, Mata NL, Tsin AT, Mertz JR, Blaner WS

Abstract

Recent studies of the human, mouse and bovine genes for 11-cis-retinol dehydrogenase (11cRDH) and human and mouse 9-cis-retinol dehydrogenase (9cRDH) suggest that they are homologs of the same enzyme. This conclusion is inconsistent with earlier literature indicating that 11cRDH is expressed solely in the eye and does not utilize 9-cis-retinol as a substrate. We have compared directly the kinetic properties of recombinant human and mouse 9cRDH with those of bovine 11cRDH for 9-cis- and 11-cis-retinol and investigated the inhibitory properties of 13-cis-retinoic acid on each of these enzymes. Human and mouse 9cRDH and bovine 11cRDH have very similar kinetic properties towards 9-cis- and 11-cis-retinol oxidation and they respond identically to 13-cis-retinoic acid inhibition. Our biochemical data are consistent with the conclusion that 9cRDH and 11cRDH are the same enzyme.

MeSH Terms
Alcohol Oxidoreductases/antagonists & inhibitors Animals Cattle Humans Isotretinoin/pharmacology Kinetics Mice Substrate Specificity Vitamin A/pharmacology
Chemicals
Vitamin A Alcohol Oxidoreductases retinol dehydrogenase retinol dehydrogenase 5 Isotretinoin
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Gamble M V
Institute of Human Nutrition, Columbia University, New York, NY 10032, USA.
Mata N L
Tsin A T
Mertz J R
Blaner W S
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
2000-01-03
Pages
3-8
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
Grants
NIDDK NIH HHS · R01 DK52444 · United States
NIDDK NIH HHS · T32 DK07328 · United States
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