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Literature summary for 1.1.1.50 extracted from

  • Chang, Y.H.; Wang, C.Z.; Chiu, C.C.; Chuang, L.Y.; Hwang, C.C.
    Contributions of active site residues to cofactor binding and catalysis of 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase (2010), Biochim. Biophys. Acta, 1804, 235-241.
    View publication on PubMed
Search for more literature for 1.1.1.50

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Comamonas testosteroni

Protein Variants

Protein Variants Comment Organism
K159A decrease in the catalytic constant by 56fold and increase in the dissociation constant by 75fold. The enzyme-bound NADH decreases the fluorescence anisotropy value in the decreasing order WT, N86A, Y155F, K159A, indicating an increase in the mobility of the bound NADH for the mutants. Hydrogen bonding with the hydroxyl group of nicotinamide ribose by K159 and Y155 is important to maintain the orientation of NADH and contributes greatly to the transition-state binding energy to facilitate the catalysis Comamonas testosteroni
K159A decrease in catalytic constant and increase in the dissociation constant. The enzyme-bound NADH decreases the fluorescence anisotropy value in the decreasing order WT, N86A, Y155F, K159A, indicating an increase in the mobility of the bound NADH for the mutants. Hydrogen bonding with the hydroxyl group of nicotinamide ribose by residues K159 and Y155 is important to maintain the orientation of NADH and contributes greatly to the transition-state binding energy to facilitate the catalysis. Residue N86 is important for stabilizing the position of K159 Comamonas testosteroni
N86A decrease in the catalytic constant by 37fold and increase in the dissociation constant by 8fold. The enzyme-bound NADH decreases the fluorescence anisotropy value in the decreasing order WT, N86A, Y155F, K159A, indicating an increase in the mobility of the bound NADH for the mutants. Residue N86 is important for stabilizing the position of K159 Comamonas testosteroni
N86A decrease in catalytic constant and increase in the dissociation constant. The enzyme-bound NADH decreases the fluorescence anisotropy value in the decreasing order WT, N86A, Y155F, K159A, indicating an increase in the mobility of the bound NADH for the mutants. Hydrogen bonding with the hydroxyl group of nicotinamide ribose by residues K159 and Y155 is important to maintain the orientation of NADH and contributes greatly to the transition-state binding energy to facilitate the catalysis. Residue N86 is important for stabilizing the position of K159 Comamonas testosteroni
Y155F decrease in the catalytic constant by 220fold and increase in the dissociation constant by 3fold. The enzyme-bound NADH decreases the fluorescence anisotropy value in the decreasing order WT, N86A, Y155F, K159A, indicating an increase in the mobility of the bound NADH for the mutants. Hydrogen bonding with the hydroxyl group of nicotinamide ribose by K159 and Y155 is important to maintain the orientation of NADH and contributes greatly to the transition-state binding energy to facilitate the catalysis Comamonas testosteroni
Y155F decrease in catalytic constant and increase in the dissociation constant. The enzyme-bound NADH decreases the fluorescence anisotropy value in the decreasing order WT, N86A, Y155F, K159A, indicating an increase in the mobility of the bound NADH for the mutants Comamonas testosteroni

Inhibitors

Inhibitors Comment Organism Structure
NADH
-
 Comamonas testosteroni

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0012
-
 5alpha-androstan-3,17-dione wild-type, pH 7.5, 25°C Comamonas testosteroni
0.0012
-
 5beta-androstane-3,17-dione wild-type, pH 7.5, 25°C Comamonas testosteroni
0.0022
-
 5alpha-androstan-3,17-dione mutant N86A, pH 7.5, 25°C Comamonas testosteroni
0.0022
-
 5beta-androstane-3,17-dione mutant N86A, pH 7.5, 25°C Comamonas testosteroni
0.004
-
 NADH wild-type, pH 7.5, 25°C Comamonas testosteroni
0.005
-
 5alpha-androstan-3,17-dione mutant Y155F, pH 7.5, 25°C Comamonas testosteroni
0.005
-
 5beta-androstane-3,17-dione mutant Y155F, pH 7.5, 25°C Comamonas testosteroni
0.007
-
 5alpha-androstan-3,17-dione mutant K159A, pH 7.5, 25°C Comamonas testosteroni
0.007
-
 5beta-androstane-3,17-dione mutant K159A, pH 7.5, 25°C Comamonas testosteroni
0.01
-
 NADH mutant N86A, pH 7.5, 25°C Comamonas testosteroni
0.029
-
 NADH mutant Y155F, pH 7.5, 25°C Comamonas testosteroni

Organism

Organism UniProt Comment Textmining
Comamonas testosteroni P80702
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5alpha-androstan-3,17-dione + NADH + H+
-
 Comamonas testosteroni androsterone + NAD+
-
 ?
5beta-androstane-3,17-dione + NADH + H+
-
 Comamonas testosteroni 5beta-androstan-3alpha-ol-17-one + NAD+
-
 ?

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Comamonas testosteroni

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0034
-
 NADH wild-type, pH 7.5, 25°C, steady-state kinetic study Comamonas testosteroni
0.004
-
 NADH mutant Y155F, pH 7.5, 25°C, steady-state kinetic study Comamonas testosteroni
0.0057
-
 NADH mutant Y155F, pH 7.5, 25°C, product inhibition study Comamonas testosteroni
0.006
-
 NADH wild-type, pH 7.5, 25°C, product inhibition study Comamonas testosteroni
0.01
-
 NADH mutant N86A, pH 7.5, 25°C, steady-state kinetic study Comamonas testosteroni
0.033
-
 NADH mutant N86A, pH 7.5, 25°C, product inhibition study Comamonas testosteroni
0.161
-
 NADH mutant K159A, pH 7.5, 25°C, product inhibition study Comamonas testosteroni
0.585
-
 NADH mutant K159A, pH 7.5, 25°C, steady-state kinetic study Comamonas testosteroni

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.0034
-
 wild-type, pH 7.5, 25°C Comamonas testosteroni NADH
0.004
-
 mutant Y155F, pH 7.5, 25°C Comamonas testosteroni NADH
0.01
-
 mutant N86A, pH 7.5, 25°C Comamonas testosteroni NADH
0.585
-
 mutant K159A, pH 7.5, 25°C Comamonas testosteroni NADH