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Literature summary for 1.1.1.202 extracted from

  • Ma, C.; Zhang, L.; Dai, J.; Xiu, Z.
    Relaxing the coenzyme specificity of 1,3-propanediol oxidoreductase from Klebsiella pneumoniae by rational design (2010), J. Biotechnol., 146, 173-178.
    View publication on PubMed
Search for more literature for 1.1.1.202

Crystallization (Commentary)

Crystallization (Comment) Organism
homology modeling with cofactors NADH and NADPH Klebsiella pneumoniae

Protein Variants

Protein Variants Comment Organism
D41A mutation for relaxation of the coenzyme specificity, weakens the repulsion between Asp41 and the phosphate group esterified to the 2-hydroxyl group of the ribose at the adenine end of NADPH Klebsiella pneumoniae
D41G mutation for relaxation of the coenzyme specificity, weakens the repulsion between Asp41 and the phosphate group esterified to the 2-hydroxyl group of the ribose at the adenine end of NADPH Klebsiella pneumoniae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.015
-
 NADH wild-type, pH 7.4, 37°C Klebsiella pneumoniae
0.14
-
 NADPH mutant D41G, pH 7.4, 37°C Klebsiella pneumoniae
0.2
-
 NAD+ wild-type, pH 7.4, 37°C Klebsiella pneumoniae
0.48
-
 NAD+ mutant D41G, pH 7.4, 37°C Klebsiella pneumoniae
0.48
-
 NADH mutant D41G, pH 7.4, 37°C Klebsiella pneumoniae
0.97
-
 NADP+ mutant D41G, pH 7.4, 37°C Klebsiella pneumoniae

Organism

Organism UniProt Comment Textmining
Klebsiella pneumoniae Q7WRJ3
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-hydroxypropanal + NADH + H+
-
 Klebsiella pneumoniae propane-1,3-diol + NAD+
-
 r
3-hydroxypropanal + NADPH + H+ NADPH is not substrate for wild-type, but for mutant D41G Klebsiella pneumoniae propane-1,3-diol + NADP+
-
 r
propane-1,3-diol + NAD+
-
 Klebsiella pneumoniae 3-hydroxypropanal + NADH + H+
-
 r
propane-1,3-diol + NADP+ NADP+ is not substrate for wild-type, but for mutant D41G Klebsiella pneumoniae 3-hydroxypropanal + NADPH + H+
-
 r

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
11.83
-
 NADP+ mutant D41G, pH 7.4, 37°C Klebsiella pneumoniae
51.99
-
 NAD+ wild-type, pH 7.4, 37°C Klebsiella pneumoniae
82.33
-
 NAD+ mutant D41G, pH 7.4, 37°C Klebsiella pneumoniae
90.64
-
 NADH wild-type, pH 7.4, 37°C Klebsiella pneumoniae
187.4
-
 NADPH mutant D41G, pH 7.4, 37°C Klebsiella pneumoniae
411.6
-
 NADH mutant D41G, pH 7.4, 37°C Klebsiella pneumoniae

Cofactor

Cofactor Comment Organism Structure
NADH the electrostatic energy is the major force discriminating NADH from NADPH. Residue Asp41 is the key residue responsible for the coenzyme specificity Klebsiella pneumoniae
NADPH no substrate for wild-type, but substrate for mutant D41G Klebsiella pneumoniae

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
12.2
-
 NADP+ mutant D41G, pH 7.4, 37°C Klebsiella pneumoniae
172
-
 NAD+ mutant D41G, pH 7.4, 37°C Klebsiella pneumoniae
260
-
 NAD+ wild-type, pH 7.4, 37°C Klebsiella pneumoniae
858
-
 NADH mutant D41G, pH 7.4, 37°C Klebsiella pneumoniae
1338
-
 NADPH mutant D41G, pH 7.4, 37°C Klebsiella pneumoniae
6043
-
 NADH wild-type, pH 7.4, 37°C Klebsiella pneumoniae