EC 1 - Oxidoreductases
EC 1.1 - Acting on the CH-OH group of donors
EC 1.1.1 - With NAD+ or NADP+ as acceptor
EC 1.1.1.105 - all-trans-retinol dehydrogenase (NAD+)
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 1.1.1.105
Names
Accepted name:
all-trans-retinol dehydrogenase (NAD+)
Other
names:
MDR
all-trans retinol dehydrogenase
microsomal retinol dehydrogenase
retinal reductase
retinene reductase
retinol (vitamin A1) dehydrogenase
retinol dehydrogenase [misleading]
epidermal retinol dehydrogenase 2
SDR16C5 (gene name)
RDH16 (gene name)
all-trans retinol dehydrogenase
microsomal retinol dehydrogenase
retinal reductase
retinene reductase
retinol (vitamin A1) dehydrogenase
retinol dehydrogenase [misleading]
epidermal retinol dehydrogenase 2
SDR16C5 (gene name)
RDH16 (gene name)
Systematic name:
all-trans retinol:NAD+ oxidoreductase
Reactions
-
48488 [IUBMB]+all-trans-retinol--[retinol-binding protein]GENERIC:14428Is ROOT: no
ROOT compound: GENERIC:12119Number of residues: 2all-trans-retinolName origin: UniProt - CHECKED (C)Formula: C20H30O
Charge: 0Position: undefinedChEBI compound status: CHECKED (C)an L-α amino acid residueName origin: UniProt - CHECKED (C)Formula: C2H2NOR
Charge: 0Position: undefinedChEBI compound status: CHECKED (C)NAD+Name origin: UniProt - CHECKED (C)Formula: C21H26N7O14P2
Charge: -1ChEBI compound status: CHECKED (C)=+all-trans-retinal--[retinol-binding protein]GENERIC:14430Is ROOT: no
ROOT compound: GENERIC:12119Number of residues: 2all-trans-retinalName origin: UniProt - CHECKED (C)Formula: C20H28O
Charge: 0Position: undefinedChEBI compound status: CHECKED (C)an L-α amino acid residueName origin: UniProt - CHECKED (C)Formula: C2H2NOR
Charge: 0Position: undefinedChEBI compound status: CHECKED (C)+H+Name origin: UniProt - CHECKED (C)Formula: H
Charge: 1ChEBI compound status: CHECKED (C) -
+all-trans-retinolName origin: UniProt - CHECKED (C)Formula: C20H30O
Charge: 0ChEBI compound status: CHECKED (C)NAD+Name origin: UniProt - CHECKED (C)Formula: C21H26N7O14P2
Charge: -1ChEBI compound status: CHECKED (C)=+all-trans-retinalName origin: UniProt - CHECKED (C)Formula: C20H28O
Charge: 0ChEBI compound status: CHECKED (C)+H+Name origin: UniProt - CHECKED (C)Formula: H
Charge: 1ChEBI compound status: CHECKED (C)
Comments:
The enzyme recognizes all-trans-retinol and all-trans-retinal as substrates and exhibits a strong preference for NAD+/NADH as cofactors. Recognizes the substrate both in free form and when bound to cellular-retinol-binding-protein (CRBP1), but has higher affinity for the bound form [2]. No activity with 11-cis-retinol or 11-cis-retinal (cf. EC 1.1.1.315, 11-cis retinol dehydrogenase). Also active with 3α-hydroxysteroids [2].
Links to other databases
Enzymes and pathways:
NC-IUBMB
,
BRENDA
,
DIAGRAM
,
ERGO
,
ExplorEnz
,
ENZYME@ExPASy
,
KEGG
,
MetaCyc
,
UniPathway
Protein domains and families:
PROSITE:PDOC00060
Gene Ontology:
GO:0004745
CAS Registry Number:
9033-53-8
UniProtKB/Swiss-Prot:
H17B6_BOVIN
H17B6_HUMAN
H17B6_MOUSE
H17B6_RAT
RDH2_RAT
RDH7_MOUSE
RDH7_RAT
RDHE2_HUMAN
RDHE2_MOUSE
References
-
Retinol and alcohol dehydrogenases in retina and liver.Biochim. Biophys. Acta 128: 48-54 (1966). [PMID: 5972368]
-
cDNA cloning and characterization of a new human microsomal NAD+-dependent dehydrogenase that oxidizes all-trans-retinol and 3α-hydroxysteroids.J. Biol. Chem. 273: 19778-19785 (1998). [PMID: 9677409]
-
Identification of the hRDH-E2 gene, a novel member of the SDR family, and its increased expression in psoriatic lesion.Biochem. Biophys. Res. Commun. 297: 1171-1180 (2002). [PMID: 12372410]
-
Biochemical characterization of human epidermal retinol dehydrogenase 2.Chem. Biol. Interact. 178: 182-187 (2009). [PMID: 18926804]
[EC 1.1.1.105 created 1972, modified 2011]