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Information on EC 1.3.99.23 - all-trans-retinol 13,14-reductase
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1.3.99.23 all-trans-retinol 13,14-reductaseIUBMB Comments
The reaction is only known to occur in the opposite direction to that given above, with the enzyme being specific for all-trans-retinol as substrate. Neither all-trans-retinoic acid nor 9-cis, 11-cis or 13-cis-retinol isomers are substrates. May play a role in the metabolism of vitamin A.
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
(13,14)-all-trans-retinol saturase, 13,14-dihydroretinol saturase, all-trans-13,14-dihydroretinol saturase, all-trans-retinol:all-trans-13,14-dihydroretinol saturase, retinol saturase, RetSat, RetSat A, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
retinol saturase
RetSat
retinol saturase
regulates retinoid metabolism and sensitivity to oxidative stress
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
all-trans-13,14-dihydroretinol + acceptor = all-trans-retinol + reduced acceptor
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
reduction
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
all-trans-13,14-dihydroretinol:acceptor 13,14-oxidoreductase
The reaction is only known to occur in the opposite direction to that given above, with the enzyme being specific for all-trans-retinol as substrate. Neither all-trans-retinoic acid nor 9-cis, 11-cis or 13-cis-retinol isomers are substrates. May play a role in the metabolism of vitamin A.
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CAS REGISTRY NUMBER
COMMENTARY
149147-14-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-all-trans-13,14-dihydroretinol + acceptor
all-trans-retinol + reduced acceptor
-
retinol saturase catalyzes the saturation of all-trans-retinol to produce (R)-all-trans-13,14-dihydroretinol
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-
r
all-trans-13,14-didehydroretinol + reduced acceptor
all-trans-13,14-dihydro-3,4-didehydroretinol + acceptor
all-trans-13,14-didehydroretinol + reduced acceptor
all-trans-7,8-dihydro-3,4-didehydroretinol + acceptor
-
-
-
?
all-trans-13,14-dihydroretinol + acceptor
all-trans-retinol + reduced acceptor
-
-
-
-
?
all-trans-13,14-dihydroretinol + reduced acceptor
all-trans-13,14-dihydro-3,4-didehydroretinol + acceptor
-
-
-
?
all-trans-3,4-didehydroretinol + reduced acceptor
all-trans-13,14-dihydro-3,4-didehydroretinol + acceptor
all-trans-3,4-didehydroretinol is preferentially converted to all-trans-13,14-dihydro-3,4-didehydroretinol
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-
?
all-trans-7,8-dihydroretinol + reduced acceptor
all-trans-7,8-dihydro-3,4-didehydroretinol + acceptor
-
-
-
?
all-trans-13,14-didehydroretinol + reduced acceptor
all-trans-13,14-dihydro-3,4-didehydroretinol + acceptor
-
preferred product
-
?
all-trans-13,14-didehydroretinol + reduced acceptor
all-trans-13,14-dihydro-3,4-didehydroretinol + acceptor
-
-
-
-
?
all-trans-retinol + reduced acceptor
all-trans-13,14-dihydroretinol + acceptor
-
-
-
?
all-trans-retinol + reduced acceptor
all-trans-13,14-dihydroretinol + acceptor
-
-
-
-
?
all-trans-retinol + reduced acceptor
all-trans-13,14-dihydroretinol + acceptor
-
-
-
-
ir
all-trans-retinol + reduced acceptor
all-trans-13,14-dihydroretinol + acceptor
-
-
-
-
?
all-trans-retinol + reduced acceptor
all-trans-13,14-dihydroretinol + acceptor
-
-
-
?
all-trans-retinol + reduced acceptor
all-trans-13,14-dihydroretinol + acceptor
-
-
-
?
all-trans-retinol + reduced acceptor
all-trans-13,14-dihydroretinol + acceptor
-
-
-
-
?
all-trans-retinol + reduced acceptor
all-trans-7,8-dihydroretinol + acceptor
-
preferred product
-
?
all-trans-retinol + reduced acceptor
all-trans-7,8-dihydroretinol + acceptor
-
all-trans-7,8-dihydroretinol is the preferred product
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-all-trans-13,14-dihydroretinol + acceptor
all-trans-retinol + reduced acceptor
-
retinol saturase catalyzes the saturation of all-trans-retinol to produce (R)-all-trans-13,14-dihydroretinol
-
-
r
all-trans-13,14-dihydroretinol + acceptor
all-trans-retinol + reduced acceptor
-
-
-
-
?
all-trans-retinol + reduced acceptor
all-trans-13,14-dihydroretinol + acceptor
-
-
-
-
?
all-trans-retinol + reduced acceptor
all-trans-13,14-dihydroretinol + acceptor
-
-
-
-
ir
all-trans-retinol + reduced acceptor
all-trans-13,14-dihydroretinol + acceptor
-
-
-
-
?
all-trans-retinol + reduced acceptor
all-trans-13,14-dihydroretinol + acceptor
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
a short hairpin RNA targeting retinol saturase strongly protects cells from tert-butylhydroperoxide and H2O2 by specifically reducing the expression of retinol saturase
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Congenital Abnormalities
Identification of genes related to beak deformity of chickens using digital gene expression profiling.
Insulin Resistance
Integration of heterogeneous expression data sets extends the role of the retinol pathway in diabetes and insulin resistance.
Metabolic Syndrome
Retinol saturase coordinates liver metabolism by regulating ChREBP activity.
Obesity, Abdominal
Quercetin Ameliorates Gut Microbiota Dysbiosis That Drives Hypothalamic Damage and Hepatic Lipogenesis in Monosodium Glutamate-Induced Abdominal Obesity.
Sarcoma
Case Report: Exome sequencing reveals recurrent RETSAT mutations and a loss-of-function POLDIP2 mutation in a rare undifferentiated tongue sarcoma.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
pluripotent embryonal carcinoma cells with high enzyme mRNA level, quantitative real-time PCR expression analysis
brenda
additional information
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
retinol signaling plays an important role in the establishment and maintenance of cellular phenotype in embryonic and adult vertebrate tissues. all-trans-Retinoic acid functions as the activating ligand for a family of ligand-activated transcription factors, the retinoic acid receptors, which form heterodimers with the retinoid X receptors to regulate gene transcription. Through its activation of the receptors, all-trans-retinoic acid regulates the expression of over 500 protein-coding genes
physiological function
-
RetSat is required for adipocyte differentiation in the 3T3-L1 cell culture model, analysis of the mechanism involved in this putative proadipogenic effect of RetSat, overview. RetSat-null mice have normal levels of retinol and retinyl palmitate in liver, serum, and adipose tissue, but, in contrast to wild-type mice, are deficient in the production of all-trans-13,14-dihydroretinol from dietary vitamin A. Despite accumulating more fat, RetSat-null mice maintained on either low-fat or high-fat diets gain weight and have similar rates of food intake as age- and gender-matched wild-type control littermates, ablation of RetSat does not result in alterations in total body weight gain but could still affect the relative composition and size of adipose stores, phenotype, overview
additional information
additional information
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RetSat deficiency leads to up-regulation of PPARgamma and PPARgamma target expression
additional information
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the mouse pluripotent P-19 cell metabolizes retinol to all-trans-retinoic acid, analysis of expression of enzymes in the cell involved in the pathway, overview
Show AA Sequence and Transmembrane Helices (108 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60000
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E34A
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mutant, mutation within the highly conserved region of the dinucleotide-binding motif
E96A
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mutant, mutation within the highly conserved region of the dinucleotide-binding motif
E34A
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mutant, mutation within the highly conserved region of the dinucleotide-binding motif
E96A
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mutant, mutation within the highly conserved region of the dinucleotide-binding motif
additional information
-
generation of RetSat-/- mice, phenotype in comparison to wild-type mice, overview
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into the Xho I site of pCDNA4/TO and expressed in T-REx-293 cells, cloned into the vector pCRII-TOPO
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in adipocytes down-regulated in obesity
incubation of mature adipocytes with pioglitazone or the non-thiazolidinedione ligand GW7845 increases RetSat mRNA expression, peroxisome proliferator activated receptor gamma, PPARgamma, is required for RetSat expression in mature adipocytes
incubation of mature adipocytes with pioglitazone or the non-thiazolidinedione ligand GW7845 increases RetSat mRNA expression, peroxisome proliferator activated receptor gamma, PPARgamma, is required for RetSat expression in mature adipocytes
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incubation of mature adipocytes with pioglitazone or the non-thiazolidinedione ligand GW7845 increases RetSat mRNA expression, peroxisome proliferator activated receptor gamma, PPARgamma, is required for RetSat expression in mature adipocytes
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
the mouse pluripotent P-19 cell metabolizes retinol to atRA and thus can be used in a cell-based screen for disruptors of the pathway. The disruption of the pathway is easily detected and quantitated, the P-19 cell provides an in vitro model system for identifying and exploring the mechanism of action of chemicals that interfere with the critical cellular pathway
medicine
additional information
medicine
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RetSat plays an important role in the biology of adipocytes, where it favors normal differentiation, yet is reduced in the obese state, RetSat is thus a novel target for therapeutic intervention in metabolic disease
medicine
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RetSat plays an important role in the biology of adipocytes, where it favors normal differentiation, yet is reduced in the obese state, RetSat is thus a novel target for therapeutic intervention in metabolic disease
additional information
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conserved function but altered specificity of RetSat in vertebrates
additional information
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conserved function but altered specificity of RetSat in vertebrates
additional information
conserved function but altered specificity of RetSat in vertebrates
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Moise, A.R.; Kuksa, V.; Imanishi, Y.; Palczewski, K.
Identification of all-trans-retinol:all-trans-13,14-dihydroretinol saturase
J. Biol. Chem.
279
50230-50242
2004
Mus musculus (Q64FW2), Mus musculus
brenda
Moise, A.R.; Kuksa, V.; Blaner, W.S.; Baehr, W.; Palczewski, K.
Metabolism and transactivation activity of 13,14-dihydroretinoic acid
J. Biol. Chem.
280
27815-27825
2005
Mus musculus
brenda
Moise, A.R.; Isken, A.; Dominguez, M.; Lera, A.R.; Lintig, J.; Palczewski, K.
Specificity of zebrafish retinol saturase: formation of all-trans-13,14-dihydroretinol and all-trans-7,8-dihydroretinol
Biochemistry
46
1811-1820
2007
Danio rerio, Danio rerio (Q5BLE8), Mus musculus
brenda
Nagaoka-Yasuda, R.; Matsuo, N.; Perkins, B.; Limbaeck-Stokin, K.; Mayford, M.
An RNAi-based genetic screen for oxidative stress resistance reveals retinol saturase as a mediator of stress resistance
Free Radic. Biol. Med.
43
781-788
2007
Mus musculus (Q64FW2)
brenda
Moise, A.R.; Alvarez, S.; Dominguez, M.; Alvarez, R.; Golczak, M.; Lobo, G.P.; von Lintig, J.; de Lera, A.R.; Palczewski, K.
Activation of retinoic acid receptors by dihydroretinoids
Mol. Pharmacol.
76
1228-1237
2009
Homo sapiens
brenda
Schupp, M.; Lefterova, M.I.; Janke, J.; Leitner, K.; Cristancho, A.G.; Mullican, S.E.; Qatanani, M.; Szwergold, N.; Steger, D.J.; Curtin, J.C.; Kim, R.J.; Suh, M.J.; Suh, M.; Albert, M.R.; Engeli, S.; Gudas, L.J.; Lazar, M.A.
Retinol saturase promotes adipogenesis and is downregulated in obesity
Proc. Natl. Acad. Sci. USA
106
1105-1110
2009
Homo sapiens, Mus musculus
brenda
Moise, A.R.; Lobo, G.P.; Erokwu, B.; Wilson, D.L.; Peck, D.; Alvarez, S.; Dominguez, M.; Alvarez, R.; Flask, C.A.; de Lera, A.R.; von Lintig, J.; Palczewski, K.
Increased adiposity in the retinol saturase-knockout mouse
FASEB J.
24
1261-1270
2010
Mus musculus
brenda
Chen, Y.; Reese, D.H.
The retinol signaling pathway in mouse pluripotent P19 cells
J. Cell. Biochem.
112
2865-2872
2011
Mus musculus
brenda
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