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Information on EC 1.1.1.105 - all-trans-retinol dehydrogenase (NAD+)

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EC Tree
IUBMB 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 . No activity with 11-cis-retinol or 11-cis-retinal (cf. EC 1.1.1.315, 11-cis retinol dehydrogenase). Also active with 3alpha-hydroxysteroids .
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This record set is specific for:
UNIPROT: O75462
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
all-trans-retinol-[cellular-retinol-binding-protein]
+
=
all-trans-retinal-[cellular-retinol-binding-protein]
+
+
Synonyms
rdh, rdh12, rdh10, dhrs9, retinal reductase, rodh-4, retinol dehydrogenase 12, rdh16, retinol dehydrogenase 10, sdr16c5, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
RoDH-4
RoDH-4 belongs to the group of short-chain dehydrogenase/reductases that are active toward two types of substrates, retinoids and 3alpha-hydroxysteroids
all-trans retinol dehydrogenase
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dehydrogenase, retinol
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MDR
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microsomal retinol dehydrogenase
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P32
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retinal reductase
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retinene reductase
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retinol dehydrogenase (vitamin A1)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
all-trans retinol:NAD+ oxidoreductase
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 3alpha-hydroxysteroids [2].
CAS REGISTRY NUMBER
COMMENTARY hide
9033-53-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
behaves as an integral membrane protein, RoDH-4 contains four potential membrane-spanning domains
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CRLF1_HUMAN
422
0
46302
Swiss-Prot
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTAM1-Y13
truncated RoDH-4 that lacks the first thirteen amino acids of the N-terminal segment is partially active and exhibits the apparent Km value for androsterone similar to that of the wild-type enzyme, truncated mutant behaves as an integral membrane protein
DELTAS295-L317
removal of 23 N-terminal hydrophobic amino acids results in significant loss of activity and a 14fold increase in the apparent Km value, truncated mutant behaves as an integral membrane protein
DELTAY291-L317
removal of the C-terminal 27 amino acid segment results in about 600fold increase in the apparent Km value, truncated mutant behaves as an integral membrane protein
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Belyaeva, O.V.; Chetyrkin, S.V.; Kedishvili, N.Y.
Characterization of truncated mutants of human microsomal short-chain dehydrogenase/reductase RoDH-4
Chem. Biol. Interact.
143-144
279-287
2003
Homo sapiens (O75462), Homo sapiens
Manually annotated by BRENDA team