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Literature summary for 1.1.1.184 extracted from

  • Zhang, R.; Xu, Y.; Sun, Y.; Nie, Y.; Mu, X.; Li, X.; Zhang, X.C.; Rao, Z.
    Crystallization and preliminary X-ray crystallographic analysis of a carbonyl reductase from Candida parapsilosis (2008), Acta Crystallogr. Sect. F, 64, 252-254.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.184

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Candida parapsilosis

Crystallization (Commentary)

Crystallization (Comment) Organism
apo-enzyme, diffraction to 2.7 A. Enzyme forms a homotetramer with broken 2-2-2 symmetry. In the apo-form, the entrance of the NADPH pocket is blocked by a surface loop Candida parapsilosis

Protein Variants

Protein Variants Comment Organism
additional information site-directed mutagenesis, deletion of the N-terminal 31 residues, catalytic parameters similar to wild-type, decrase in melting temperature Candida parapsilosis
S172A site-directed mutagenesis, decrease of melting temperature compared to wild-type. No catalytic activity Candida parapsilosis
S172T site-directed mutagenesis, decrease of melting temperature compared to wild-type. Catalytic activity similar to wild-type Candida parapsilosis
S67D/H68D site-directed mutagenesis, about 10fold increase and 20fold decrease for NADH and NADPH kcat/KM-value, respectively Candida parapsilosis
V270D site-directed mutagenesis, catalytic acitivity similar to wild-type, mutant forms a dimer Candida parapsilosis
Y187A site-directed mutagenesis, decrease of melting temperature compared to wild-type. No catalytic activity Candida parapsilosis
Y187F site-directed mutagenesis, decrease of melting temperature compared to wild-type. No catalytic activity Candida parapsilosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.59
-
 NADPH wild-type, pH 7.5, 35°C Candida parapsilosis
0.63
-
 NADPH deletion mutant lacking 31 N-terminal amino acids, pH 7.5, 35°C Candida parapsilosis
0.68
-
 NADPH mutant S172T, pH 7.5, 35°C Candida parapsilosis
0.71
-
 NADPH mutant V270D, pH 7.5, 35°C Candida parapsilosis
0.76
-
 NADH mutant S67D/H68D, pH 7.5, 35°C Candida parapsilosis
7.89
-
 NADH wild-type, pH 7.5, 35°C Candida parapsilosis
8.03
-
 NADH deletion mutant lacking 31 N-terminal amino acids, pH 7.5, 35°C Candida parapsilosis
8.45
-
 NADH mutant V270D, pH 7.5, 35°C Candida parapsilosis
8.67
-
 NADH mutant S172T, pH 7.5, 35°C Candida parapsilosis
10.27
-
 NADPH mutant S67D/H68D, pH 7.5, 35°C Candida parapsilosis

Organism

Organism UniProt Comment Textmining
Candida parapsilosis B2KJ46 fragment
-

Purification (Commentary)

Purification (Comment) Organism
recombinant protein Candida parapsilosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-hydroxyacetophenone + NADH + H+
-
 Candida parapsilosis (S)-1-phenyl-1,2-ethanediol + NAD+
-
 ?
2-hydroxyacetophenone + NADPH + H+
-
 Candida parapsilosis (S)-1-phenyl-1,2-ethanediol + NADP+
-
 ?

Subunits

Subunits Comment Organism
tetramer crystallization data Candida parapsilosis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45
-
 melting temperature, mutant Y187A Candida parapsilosis
46
-
 melting temperature, mutant S172A Candida parapsilosis
46
-
 melting temperature, mutant Y187F Candida parapsilosis
48
-
 melting temperature, mutant S172T and N-terminal deletion mutant lacking 31 amino acids Candida parapsilosis
52
-
 melting temperature, wild-type Candida parapsilosis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.13
-
 NADH mutant S172T, pH 7.5, 35°C Candida parapsilosis
1.21
-
 NADPH mutant S67D/H68D, pH 7.5, 35°C Candida parapsilosis
1.22
-
 NADH mutant V270D, pH 7.5, 35°C Candida parapsilosis
1.24
-
 NADH deletion mutant lacking 31 N-terminal amino acids, pH 7.5, 35°C Candida parapsilosis
1.26
-
 NADH mutant S67D/H68D, pH 7.5, 35°C Candida parapsilosis
1.32
-
 NADH wild-type, pH 7.5, 35°C Candida parapsilosis
1.34
-
 NADPH mutant V270D, pH 7.5, 35°C Candida parapsilosis
1.36
-
 NADPH mutant S172T, pH 7.5, 35°C Candida parapsilosis
1.39
-
 NADPH deletion mutant lacking 31 N-terminal amino acids, pH 7.5, 35°C Candida parapsilosis
1.48
-
 NADPH wild-type, pH 7.5, 35°C Candida parapsilosis

Cofactor

Cofactor Comment Organism Structure
NADH NADPH is preferred over NADH Candida parapsilosis
NADP+
-
 Candida parapsilosis
NADPH preferred over NADH Candida parapsilosis