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Information on EC 1.3.99.23 - all-trans-retinol 13,14-reductase and Organism(s) Homo sapiens
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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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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
retsat, retinol saturase, retsat a, 13,14-dihydroretinol saturase, all-trans-13,14-dihydroretinol saturase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
retinol saturase
RetSat
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PATHWAY SOURCE
PATHWAYS
KEGG
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.
CAS REGISTRY NUMBER
COMMENTARY
149147-14-8
-
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
all-trans-13,14-dihydroretinol + FAD
all-trans-retinol + FADH2
-
-
-
?
all-trans-13,14-dihydroretinol + NAD+
all-trans-retinol + NADH + H+
-
-
-
?
all-trans-13,14-dihydroretinol + NADP+
all-trans-retinol + NADPH + H+
-
-
-
?
all-trans-retinol + reduced acceptor
all-trans-13,14-dihydroretinol + acceptor
-
-
-
-
?
all-trans-retinol + reduced acceptor
all-trans-13,14-dihydroretinol + acceptor
-
-
-
-
ir
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
all-trans-13,14-dihydroretinol + FAD
all-trans-retinol + FADH2
-
-
-
?
all-trans-13,14-dihydroretinol + NAD+
all-trans-retinol + NADH + H+
-
-
-
?
all-trans-13,14-dihydroretinol + NADP+
all-trans-retinol + NADPH + H+
-
-
-
?
all-trans-retinol + reduced acceptor
all-trans-13,14-dihydroretinol + acceptor
-
-
-
-
?
all-trans-retinol + reduced acceptor
all-trans-13,14-dihydroretinol + acceptor
-
-
-
-
ir
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
retinol saturase (RetSat) is an NADH/NADPH- or FADH-dependent oxidoreductase
-
additional information
-
retinol saturase (RetSat) is an NADH/NADPH- or FADH-dependent oxidoreductase
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
RetSat is predominantly in the endoplasmic reticulum (ER) where it colocalizes with the ER marker protein disulfide isomerase
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
hepatic RETSAT correlates with obesity and steatosis in humans
physiological function
cellular RetSat protein localizes primarily to the endoplasmic reticulum and catalyzes the conversion of retinol to 13,14-dihydroretinol (13,14-dhretinol), a retinoid metabolite that can act as precursor for the generation of 13,14-dihydroretinoic acid. Retinol saturase coordinates liver metabolism by regulating ChREBP activity. The oxidoreductase retinol saturase (RetSat) is involved in the development of fatty liver. Hepatic RetSat expression correlates with steatosis and serum triglycerides (TGs) in humans. Major transcriptional regulators of RetSat expression include peroxisome proliferator-activated receptor alpha (PPARalpha) and forkhead box O1 (FoxO1) in liver, and PPARgamma in adipose tissue, where RetSat's expression is robustly induced during the differentiation of precursor cells into adipocytes
physiological function
retinol saturase (RetSat) is an oxidoreductase that is expressed in metabolically active tissues and is highly regulated in conditions related to insulin resistance and type 2 diabetes. RetSat has been implicated in adipocyte differentiation, hepatic glucose and lipid metabolism, macrophage function, vision, and the generation of reactive oxygen species (ROS). Function of RetSat and dihydroretinol in retinoid homeostasis, overview. RETSAT expression in liver correlates with obesity, hepatic steatosis, and the expression of carbohydrate response element-binding protein (ChREBP) target genes
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). RETST_HUMAN
610
1
66820
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E34A
-
mutant, mutation within the highly conserved region of the dinucleotide-binding motif
E96A
-
mutant, mutation within the highly conserved region of the dinucleotide-binding motif
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
-
major transcriptional regulators of RetSat are the nuclear peroxisome proliferator-activated receptor alpha (PPARalpha) in organs such as liver and PPARgamma in adipose tissue through a PPAR-response element (PPRE) in intron 1 of the human genes
major transcriptional regulators of RetSat expression include peroxisome proliferator-activated receptor alpha (PPARalpha) and forkhead box O1 (FoxO1) in liver, and PPARgamma in adipose tissue, where RetSat's expression is robustly induced during the differentiation of precursor cells into adipocytes
RetSat mRNA and protein expression is robustly upregulated during the differentiation of white pre-adipocytes of human origin
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
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
enzyme RetSat is a critical regulator of liver metabolism functioning upstream of ChREBP. Pharmacological inhibition of liver RetSat may represent a therapeutic approach for steatosis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
Heidenreich, S.; Witte, N.; Weber, P.; Goehring, I.; Tolkachov, A.; von Loeffelholz, C.; Doecke, S.; Bauer, M.; Stockmann, M.; Pfeiffer, A.F.H.; Birkenfeld, A.L.; Pietzke, M.; Kempa, S.; Muenzner, M.; Schupp, M.
Retinol saturase coordinates liver metabolism by regulating ChREBP activity
Nat. Commun.
8
384
2017
Homo sapiens (Q6NUM9), Homo sapiens, Mus musculus (Q64FW2), Mus musculus C57BL/6J (Q64FW2)
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