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Literature summary for 1.1.1.105 extracted from

  • Takahashi, Y.; Moiseyev, G.; Farjo, K.; Ma, J.X.
    Characterization of key residues and membrane association domains in retinol dehydrogenase 10 (2009), Biochem. J., 419, 113-122.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.105

Cloned(Commentary)

Cloned (Comment) Organism
expressed in COS-1 cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
G43A/G47A/G49A the triple mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level Homo sapiens
K214A the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level Homo sapiens
K214R the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level Homo sapiens
N169A the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level Homo sapiens
N169D the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level Homo sapiens
S197A mutant retains significant enzymatic activities, although lower than that of wild type enzyme Homo sapiens
S197C the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level Homo sapiens
S197G mutant retains significant enzymatic activities, although lower than that of wild type enzyme Homo sapiens
S197T the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level Homo sapiens
S197V the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level Homo sapiens
Y210A the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level Homo sapiens
Y210F the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0015
-
 NADPH wild type enzyme, in 100 mM sodium phosphate, pH 7.4 Homo sapiens
0.0041
-
 all-trans-retinol wild type enzyme, in 100 mM sodium phosphate, pH 7.4 Homo sapiens
0.027
-
 NADP+ wild type enzyme, in 100 mM sodium phosphate, pH 7.4 Homo sapiens
0.036
-
 NAD+ wild type enzyme, in 100 mM sodium phosphate, pH 7.4 Homo sapiens
0.11
-
 NADH wild type enzyme, in 100 mM sodium phosphate, pH 7.4 Homo sapiens
0.57
-
 all-trans-retinal wild type enzyme, in 100 mM sodium phosphate, pH 7.4 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Homo sapiens 16020
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
 SDS-PAGE Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q8IZV5
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
all-trans-retinal + NADH + H+ wild type RDH10 catalyzes both oxidation of all-trans retinol and reduction of all-trans retinal in vitro. On cultured cells, however, oxidation is the favored reaction catalyzed by RDH10. Homo sapiens all-trans-retinol + NAD+
-
 ?
all-trans-retinal-[cellular-retinol-binding-protein] + NADPH + H+
-
 Homo sapiens all-trans-retinol-[cellular-retinol-binding-protein] + NADP+
-
 ?
all-trans-retinol-[cellular-retinol-binding-protein] + NADP+
-
 Homo sapiens all-trans-retinal-[cellular-retinol-binding-protein] + NADPH + H+
-
 r

Synonyms

Synonyms Comment Organism
RDH10
-
 Homo sapiens
retinol dehydrogenase 10
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NADH the enzyme has higher affinity for NADH than for NADPH Homo sapiens
NADPH the enzyme has lower affinity for NADPH than for NADH Homo sapiens