Retinol dehydrogenase

From Wikipedia, the free encyclopedia

In enzymology, a retinol dehydrogenase (EC 1.1.1.105) is an enzyme that catalyzes the chemical reaction

retinol + NAD⁺ retinal + NADH + H⁺

Thus, the two substrates of this enzyme are retinol and NAD⁺, whereas its 3 products are retinal, NADH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is retinol:NAD+ oxidoreductase. Other names in common use include retinol (vitamin A1) dehydrogenase, MDR, microsomal retinol dehydrogenase, all-trans retinol dehydrogenase, retinal reductase, and retinene reductase. This enzyme participates in retinol metabolism.

[edit] References

• IUBMB entry for 1.1.1.105
• BRENDA references for 1.1.1.105 (Recommended.)
• PubMed references for 1.1.1.105
• PubMed Central references for 1.1.1.105
• Google Scholar references for 1.1.1.105
• Koen AL, Shaw CR (1966). "Retinol and alcohol dehydrogenases in retina and liver". Biochim. Biophys. Acta. 128: 48–54. PMID 5972368. 

[edit] External links

The CAS registry number for this enzyme class is 9033-53-8.

• IUBMB entry for 1.1.1.105

• KEGG entry for 1.1.1.105

• BRENDA entry for 1.1.1.105

• NiceZyme view of 1.1.1.105

• EC2PDB: PDB structures for 1.1.1.105

• PRIAM entry for 1.1.1.105

• PUMA2 entry for 1.1.1.105

• IntEnz: Integrated Enzyme entry for 1.1.1.105

• MetaCyc entry for 1.1.1.105

• Atomic-resolution structures of enzymes belonging to this class

[edit] Gene Ontology (GO) codes

• EGO entry for GO code 0004745: retinol dehydrogenase

• AMIGO entry for GO code 0004745: retinol dehydrogenase