Dual-substrate Specificity Short Chain Retinol Dehydrogenases from the Vertebrate Retina

Autor: Yoshikazu Imanishi, Peter S. Nelson, Geeng Fu Jang, Masazumi Matsumura, Krzysztof Palczewski, C.A.G.G. Driessen, Françoise Haeseleer
Rok vydání: 2002
Předmět:
genetic structures
medicine.drug_class
Molecular Sequence Data
Dehydrogenase
Biology
Retinol dehydrogenase
Biochemistry
Retina
Article
Substrate Specificity
Mice
chemistry.chemical_compound
medicine
Animals
Humans
Amino Acid Sequence
experimenteel en klinisch onderzoek en behandeling. [Erfelijke en verworven vitreo-retinale aandoeningen]
Retinoid
Molecular Biology
In Situ Hybridization
Phylogeny
Alcohol dehydrogenase
chemistry.chemical_classification
Molecular Structure
Retinol
Stereoisomerism
Retinal
Haplorhini
Mechanism of the visual process and cellular aging
Cell Biology
NAD
Recombinant Proteins
Alcohol Oxidoreductases
medicine.anatomical_structure
Enzyme
chemistry
Het visuele mechanisme en cellulaire veroudering
Retinaldehyde
biology.protein
Cattle
experimental and clinical research and treatment. [Hereditary and acquired vitreo-retinal disorders]
Carrier Proteins
Sequence Alignment
NADP
Zdroj: Journal of Biological Chemistry, 277, 45537-46
Journal of Biological Chemistry, 277, 47, pp. 45537-46
ISSN: 0021-9258
Popis: Contains fulltext : 185315.pdf (Publisher’s version ) (Open Access) Retinoids are chromophores involved in vision, transcriptional regulation, and cellular differentiation. Members of the short chain alcohol dehydrogenase/reductase superfamily catalyze the transformation of retinol to retinal. Here, we describe the identification and properties of three enzymes from a novel subfamily of four retinol dehydrogenases (RDH11-14) that display dual-substrate specificity, uniquely metabolizing all-trans- and cis-retinols with C(15) pro-R specificity. RDH11-14 could be involved in the first step of all-trans- and 9-cis-retinoic acid production in many tissues. RDH11-14 fill the gap in our understanding of 11-cis-retinal and all-trans-retinal transformations in photoreceptor (RDH12) and retinal pigment epithelial cells (RDH11). The dual-substrate specificity of RDH11 explains the minor phenotype associated with mutations in 11-cis-retinol dehydrogenase (RDH5) causing fundus albipunctatus in humans and engineered mice lacking RDH5. Furthermore, photoreceptor RDH12 could be involved in the production of 11-cis-retinal from 11-cis-retinol during regeneration of the cone visual pigments. These newly identified enzymes add new elements to important retinoid metabolic pathways that have not been explained by previous genetic and biochemical studies.
Databáze: OpenAIRE
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