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Information on EC 1.1.1.315 - 11-cis-retinol dehydrogenase and Organism(s) Bos taurus and UniProt Accession Q27979

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IUBMB Comments
This enzyme, abundant in the retinal pigment epithelium, catalyses the reduction of 11-cis-retinol to 11-cis-retinal while the substrate is bound to the retinal-binding protein . This is a crucial step in the regeneration of 11-cis-retinal, the chromophore of rhodopsin. The enzyme can also accept other cis forms of retinol .
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Bos taurus
UNIPROT: Q27979
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The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
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11-cis-retinol-[retinal-binding-protein]
+
NAD+
=
11-cis-retinal-[retinol-binding-protein]
+
NADH
+
H+
11-cis-retinol-[retinal-binding-protein]
+
=
11-cis-retinal-[retinol-binding-protein]
+
+
Synonyms
11-cis-retinol dehydrogenase, 11-cis-rdh, crad2, atrdh, 11-cis rd, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11-cis RD
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cRDH
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PATHWAY SOURCE
PATHWAYS
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-
SYSTEMATIC NAME
IUBMB Comments
11-cis-retinol:NAD+ oxidoreductase
This enzyme, abundant in the retinal pigment epithelium, catalyses the reduction of 11-cis-retinol to 11-cis-retinal [1] while the substrate is bound to the retinal-binding protein [4]. This is a crucial step in the regeneration of 11-cis-retinal, the chromophore of rhodopsin. The enzyme can also accept other cis forms of retinol [2].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
11-cis-retinol + NAD+
11-cis-retinal + NADH + H+
show the reaction diagram
-
-
-
?
11-cis-retinol-[cellular retinaldehyde binding protein] + NAD+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+
show the reaction diagram
-
-
-
-
?
11-cis-retinol-[cellular retinaldehyde binding protein] + NADP+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADPH + H+
show the reaction diagram
-
-
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
show the reaction diagram
the addition of NADP+ results in more efficient oxidation of all-trans retinol into all-trans retinal, when compared with the addition of NAD+, suggesting that RDH10 prefers NADP as the cofactor. At assay conditions (pH 5.5 and pH 7.6), and NADH or NADPH is used as the cofactor, only a low level of all-trans retinol is generated by RDH10
-
-
r
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
show the reaction diagram
the addition of NADP+ results in more efficient oxidation of all-trans retinol into all-trans retinal, when compared with the addition of NAD+, suggesting that RDH10 prefers NADP as the cofactor. At assay conditions (pH 5.5 and pH 7.6), and NADH or NADPH is used as the cofactor, only a low level of all-trans retinol is generated by RDH10
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-
r
additional information
?
-
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
11-cis-retinol-[cellular retinaldehyde binding protein] + NAD+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+
show the reaction diagram
-
-
-
-
?
11-cis-retinol-[cellular retinaldehyde binding protein] + NADP+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADPH + H+
show the reaction diagram
-
-
-
-
?
additional information
?
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-
cRDH does not react with endogenous all-trans-retinal bound to retinal G protein-coupled receptor RGR but reacts specifically with 11-cis-retinal that is generated by photoisomerization after irradiation of RGR. The reduction of 11-cis-retinal to 11-cis-retinol by cRDH enhances the net photoisomerization of all-trans-retinal bound to RGR
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
additional information
no cofactor: NADP+
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
specific expression
Manually annotated by BRENDA team
low activity
Manually annotated by BRENDA team
low activity
Manually annotated by BRENDA team
low activity
Manually annotated by BRENDA team
low activity
Manually annotated by BRENDA team
low activity
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
RDH10 colocalizes with retinal pigment protein RPE65 and with cellular retinaldehyde-binding protein CRALBP in vivo
Manually annotated by BRENDA team
low activity
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the majority of 11-cis retinol dehydrogenase is associated with the smooth ER in retinal pigment epithelial cells. The enzyme is an integral membrane protein, anchored to membranes by two hydrophobic peptide segments. The catalytic domain of the enzyme is confined to a lumenal compartment and is not present on the cytosolic aspect of membranes
Manually annotated by BRENDA team
associated to membrane, and ssequence displays several potential membrane-spanning segments
Manually annotated by BRENDA team
-
pronounced 11-cis-retinol dehydrogenase activity is associated with both endoplasmic reticulum- and plasma membrane-enriched membrane fractions. In contrast, 11-cis-retinyl ester hydrolase activity is mostly recovered in plasma membrane-enriched fractions, while lecithin retinol acyl transferase LRAT activity is found only in endoplasmic reticulum-enriched membranes
Manually annotated by BRENDA team
-
pronounced 11-cis-retinol dehydrogenase activity is associated with both endoplasmic reticulum- and plasma membrane-enriched membrane fractions. In contrast, 11-cis-retinyl ester hydrolase activity is mostly recovered in plasma membrane-enriched fractions, while lecithin retinol acyl transferase LRAT activity is found only in endoplasmic reticulum-enriched membranes
Manually annotated by BRENDA team
-
pronounced 11-cis-retinol dehydrogenase activity is associated with both endoplasmic reticulum- and plasma membrane-enriched membrane fractions. In contrast, 11-cis-retinyl ester hydrolase activity is mostly recovered in plasma membrane-enriched fractions, while lecithin retinol acyl transferase LRAT activity is found only in endoplasmic reticulum-enriched membranes
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
cRDH is involved in the processing of 11-cis-retinal after irradiation of retinal G protein-coupled receptor RGR opsin and plays a role in the visual cycle
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RDH5_BOVIN
318
0
35037
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
x * 32000, SDS-PAGE
32000
-
x * 32000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 32000, SDS-PAGE
?
-
x * 32000, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
N-terminal 18 amino acids of sequence have the characteristics of a classigal signal sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
alignment of Streptomyces hydrogenans 20beta-hydroxysteroid dehydrogenase with rat retinol dehydrogenase and cow 11-cis retinol dehydrogenase. Lysine64 of the rat enzyme is important in stabilizing binding of 2'-phosphate on NADP+ in two ways: lysine's positively charged side chain has a coulombic attraction to the 2'-phosphate and partially compensates for the negative charge of aspartic acid-38. Cow 11-cis retinol dehydrogenase has threonine61 at the position homologous to lysine64. Threonine61 does not have a stabilizing coulombic interaction with NADP+, nor can threonine61 counteract the repulsive interaction between NADP+ and aspartic acid37 in 11-cis retinol dehydrogenase
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTA289-318
results show that the N-terminal hydrophobic domain is a membrane-anchoring domain
additional information
introduction of a glycosylation site in mutant 11-cis RDH GM71-73 at positions 71-73, residues NIS. Construction of a mutant protein, 11-cis RDH-HA, with a C-terminal extension of 12 amino acid residues consisting of the hemagglutinin antigenic epitope and a glycosylation site. Results suggest that residues 289-310 of 11-cis RDH are a transmembrane domain and that amino acid residues 311-318 are located in the cytosol
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme copurifies with retinal G protein coupled receptor from microsomes
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Cos-1 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mata, N.L.; Tsin, A.T.C.
Distribution of 11-cis LRAT, 11-cis RD and 11-cis REH in bovine retinal pigment epithelium membranes
Biochim. Biophys. Acta
1394
16-22
1998
Bos taurus
Manually annotated by BRENDA team
Wu, B.X.; Chen, Y.; Chen, Y.; Fan, J.; Rohrer, B.; Crouch, R.K.; Ma, J.X.
Cloning and characterization of a novel all-trans retinol short-chain dehydrogenase/reductase from the RPE
Invest. Ophthalmol. Vis. Sci.
43
3365-3372
2002
Bos taurus (Q8HZT6), Bos taurus, Homo sapiens (Q8IZV5), Homo sapiens, Mus musculus (Q8VCH7), Mus musculus
Manually annotated by BRENDA team
Farjo, K.M.; Moiseyev, G.; Takahashi, Y.; Crouch, R.K.; Ma, J.X.
RDH10 has 11-cis-retinol dehydrogenase activity and interacts with visual cycle proteins.
Invest. Ophthalmol. Vis. Sci.
50
5089-5097
2009
Bos taurus (Q8HZT6), Bos taurus, Homo sapiens (Q8IZV5), Homo sapiens
Manually annotated by BRENDA team
Tsigelny, I.; Baker, M.E.
Structures important in NAD(P)(H) specificity for mammalian retinol and 11-cis-retinol dehydrogenases
Biochem. Biophys. Res. Commun.
226
118-127
1996
Bos taurus
Manually annotated by BRENDA team
Simon, A.; Hellman, U.; Wernstedt, C.; Eriksson, U.
The retinal pigment epithelial-specific 11-cis retinol dehydrogenase belongs to the family of short chain alcohol dehydrogenases
J. Biol. Chem.
270
1107-1112
1995
Bos taurus (Q27979)
Manually annotated by BRENDA team
Chen, P.; Lee, T.D.; Fong, H.K.
Interaction of 11-cis-retinol dehydrogenase with the chromophore of retinal G protein-coupled receptor opsin
J. Biol. Chem.
276
21098-21104
2001
Bos taurus
Manually annotated by BRENDA team
Simon, A.; Romert, A.; Gustafson, A.; McCaffery, J.; Eriksson, U.
Intracellular localization and membrane topology of 11-cis retinol dehydrogenase in the retinal pigment epithelium suggest a compartmentalized synthesis of 11-cis retinaldehyde
J. Cell Sci.
112
549-558
1999
Bos taurus (Q27979)
Manually annotated by BRENDA team