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Information on EC 1.1.1.300 - NADP-retinol dehydrogenase and Organism(s) Oryctolagus cuniculus and UniProt Accession Q9GKX2

for references in articles please use BRENDA:EC1.1.1.300
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EC Tree
IUBMB 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 beta-carotene by EC 1.13.11.63 (beta-carotene 15,15'-dioxygenase) . 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.
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Oryctolagus cuniculus
UNIPROT: Q9GKX2
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The taxonomic range for the selected organisms is: Oryctolagus cuniculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
prrdh, retinol dehydrogenase 11, retinol dehydrogenase 8, ralr1, nrdrb1, mrdh11, nadp(h)-dependent retinol dehydrogenase/reductase, photoreceptor retinol dehydrogenase, rdh14, retinol dehydrogenase-10, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
all-trans retinal reductase
-
peroxisomal NADP(H)-dependent retinol dehydrogenase-reductase
-
retinal reductase
-
retinol dehydrogenase [NADP+]
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
retinol:NADP+ oxidoreductase
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 beta-carotene by EC 1.13.11.63 (beta-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.
CAS REGISTRY NUMBER
COMMENTARY hide
90033-53-8
cf. EC 1.1.1.105
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
all-trans-retinal + NADPH + H+
all-tans-retinol + NADP+
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
all-trans-retinal + NADPH + H+
all-tans-retinol + NADP+
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene harbours two initiation sites, one of which encodes a 279 and the other a 260 amino acids protein
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DHRS4_RABIT
260
0
27430
Swiss-Prot
Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
2 * 27000, SDS-PAGE, native mass by gel filtration
27368
2 * 27368, MALDI-TOF MS, native mass by gel filtration
27430
2 * 27430, calculated from the deduced amino acid sequence, native mass by gel filtration
60000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Du, K.; Liu, G.F.; Xie, J.P.; Song, X.H.; Li, R.; Liang, B.; Huang, D.Y.
A 27.368 kDa retinal reductase in New Zealand white rabbit liver cytosol encoded by the peroxisomal retinol dehydrogenase-reductase cDNA: purification and characterization of the enzyme
Biochem. Cell Biol.
85
209-217
2007
Oryctolagus cuniculus (Q9GKX2), Oryctolagus cuniculus
Manually annotated by BRENDA team