Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.1.300 extracted from

  • Gallego, O.; Belyaeva, O.V.; Porte, S.; Ruiz, F.X.; Stetsenko, A.V.; Shabrova, E.V.; Kostereva, N.V.; Farres, J.; Pares, X.; Kedishvili, N.Y.
    Comparative functional analysis of human medium-chain dehydrogenases, short-chain dehydrogenases/reductases and aldo-keto reductases with retinoids (2006), Biochem. J., 399, 101-109.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
-
Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.18
-
all-trans-retinol 37°C Homo sapiens
0.3
-
all-trans-retinal 37°C Homo sapiens

Localization

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

Organism

Organism UniProt Comment Textmining
Homo sapiens Q8TC12
-
-

Purification (Commentary)

Purification (Comment) Organism
purified to homogeneity Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
all-trans-retinol + NADP+ more efficient in the reductive direction Homo sapiens all-trans-retinal + NADPH + H+
-
r
additional information the enzymes utilizes retinol bound to cellular retinol binding protein type I at a much lower rate than free retinol Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
RDH11
-
Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.00012
-
all-trans-retinal 37°C Homo sapiens
0.0006
-
all-trans-retinol 37°C Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NADP+ preferred cofactor Homo sapiens
NADPH preferred cofactor Homo sapiens