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Literature summary for 1.1.1.50 extracted from

  • Heredia, V.V.; Kruger, R.G.; Penning, T.M.
    Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase (3alpha-HSD or AKR1C9) (2003), Chem. Biol. Interact., 143-144, 393-400.
    View publication on PubMed
Search for more literature for 1.1.1.50

Protein Variants

Protein Variants Comment Organism
F118A site-directed mutagenesis, mutation of a substrate binding residue, altered steroid recognition and kinetics compared to the wild-type enzyme Rattus norvegicus
F129A site-directed mutagenesis, mutation of a substrate binding residue, altered steroid recognition and kinetics compared to the wild-type enzyme, highly reduced activity Rattus norvegicus
L54A site-directed mutagenesis, mutation of a substrate binding residue, altered steroid recognition and kinetics compared to the wild-type enzyme Rattus norvegicus
N306A site-directed mutagenesis, mutation of a substrate binding residue, altered steroid recognition and kinetics compared to the wild-type enzyme Rattus norvegicus
T226A site-directed mutagenesis, mutation of a substrate binding residue, steroid recognition and kinetics are similar to the wild-type enzyme Rattus norvegicus
T24A site-directed mutagenesis, mutation of a substrate binding residue, steroid recognition and kinetics are similar to the wild-type enzyme Rattus norvegicus
W227A site-directed mutagenesis, mutation of a substrate binding residue, altered steroid recognition and kinetics compared to the wild-type enzyme, highly reduced activity and binding of progesterone Rattus norvegicus
Y310A site-directed mutagenesis, mutation of a substrate binding residue, altered steroid recognition and kinetics compared to the wild-type enzyme Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rattus norvegicus enzyme plays a pivotal role in the inactivation of circulating steroid hormones ?
-
 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
 isozyme AKR1C9
-

Reaction

Reaction Comment Organism Reaction ID
a 3alpha-hydroxysteroid + NAD(P)+ = a 3-oxosteroid + NAD(P)H + H+ ordered bi bi kinetic mechanism, catalytic residues are Y55 and H117 Rattus norvegicus
a

Source Tissue

Source Tissue Comment Organism Textmining
liver isozyme AKR1C9 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme plays a pivotal role in the inactivation of circulating steroid hormones Rattus norvegicus ?
-
 ?
additional information wild-type enzyme recognizes only the 3-keto function of steroids, while the substrate binding residue-mutant enzymes show a broader substrate specificity and broader reaction spectra, overview, structure-function study on the basis of the crystal structure, modeling Rattus norvegicus ?
-
 ?
progesterone + NADPH
-
 Rattus norvegicus ?
-
 ?
testosterone + NADPH + H+ substrate binding residues are T24, L54, Y55, H117, F118, F129, T226, W227, N306, and Y310 Rattus norvegicus ?
-
 ?

Subunits

Subunits Comment Organism
More structure-function study on the basis of the crystal structure, modeling Rattus norvegicus

Synonyms

Synonyms Comment Organism
3alpha-HSD
-
 Rattus norvegicus
3alpha-hydroxysteroid dehydrogenase
-
 Rattus norvegicus
AKR1C9
-
 Rattus norvegicus
More enzyme belongs to the aldo-keto reductase AKR superfamily Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Rattus norvegicus