EC 1.1.1.300 - NADP-retinol dehydrogenase

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IntEnz Enzyme Nomenclature
EC 1.1.1.300

Names

Accepted name:
NADP-retinol dehydrogenase
Other names:
all-trans retinal reductase
all-trans-retinol dehydrogenase
NADP(H)-dependent retinol dehydrogenase/reductase
RDH11
RDH12
RDH13
RDH14
retinol dehydrogenase 12
retinol dehydrogenase 14
retinol dehydrogenase [NADP+]
RalR1
PSDR1
Systematic name:
retinol:NADP+ oxidoreductase

Reaction

Comments:

Greater catalytic efficiency in the reductive direction. This observation, and the enzyme's localization at the entrance to the mitochondrial matrix, suggest that it may function to protect mitochondria against oxidative stress associated with the highly reactive retinal produced from dietary β-carotene by EC 1.13.11.63 (β-carotene 15,15'-dioxygenase) [2]. Km-values for NADP+ and NADPH are at least 800-fold lower than those for NAD+ and NADH [1,4]. This enzyme differs from EC 1.1.1.105, retinol dehydrogenase, which prefers NAD+ and NADH.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00060
Structural data: CSA , EC2PDB
Gene Ontology: GO:0052650
UniProtKB/Swiss-Prot: (32) [show] [UniProt]

References

  1. Belyaeva, O. V., Korkina, O. V., Stetsenko, A. V., Kim, T., Nelson, P. S., Kedishvili, N. Y.
    Biochemical properties of purified human retinol dehydrogenase 12 (RDH12): catalytic efficiency toward retinoids and C9 aldehydes and effects of cellular retinol-binding protein type I (CRBPI) and cellular retinaldehyde-binding protein (CRALBP) on the oxidation and reduction of retinoids.
    Biochemistry 44: 7035-7047 (2005). [PMID: 15865448]
  2. Belyaeva, O. V., Korkina, O. V., Stetsenko, A. V., Kedishvili, N. Y.
    Human retinol dehydrogenase 13 (RDH13) is a mitochondrial short-chain dehydrogenase/reductase with a retinaldehyde reductase activity.
    FEBS J. 275: 138-147 (2008). [PMID: 18039331]
  3. Haeseleer, F., Huang, J., Lebioda, L., Saari, J. C., Palczewski, K.
    Molecular characterization of a novel short-chain dehydrogenase/reductase that reduces all-trans-retinal.
    J. Biol. Chem. 273: 21790-21799 (1998). [PMID: 9705317]
  4. Kedishvili, N. Y., Chumakova, O. V., Chetyrkin, S. V., Belyaeva, O. V., Lapshina, E. A., Lin, D. W., Matsumura, M., Nelson, P. S.
    Evidence that the human gene for prostate short-chain dehydrogenase/reductase (PSDR1) encodes a novel retinal reductase (RalR1).
    J. Biol. Chem. 277: 28909-28915 (2002). [PMID: 12036956]

[EC 1.1.1.300 created 2009]