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Literature summary 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

Crystallization (Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.202 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
1.1.1.202 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.202 0.015
-
 NADH wild-type, pH 7.4, 37°C Klebsiella pneumoniae
1.1.1.202 0.14
-
 NADPH mutant D41G, pH 7.4, 37°C Klebsiella pneumoniae
1.1.1.202 0.2
-
 NAD+ wild-type, pH 7.4, 37°C Klebsiella pneumoniae
1.1.1.202 0.48
-
 NAD+ mutant D41G, pH 7.4, 37°C Klebsiella pneumoniae
1.1.1.202 0.48
-
 NADH mutant D41G, pH 7.4, 37°C Klebsiella pneumoniae
1.1.1.202 0.97
-
 NADP+ mutant D41G, pH 7.4, 37°C Klebsiella pneumoniae

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.202 Klebsiella pneumoniae Q7WRJ3
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.202 3-hydroxypropanal + NADH + H+
-
 Klebsiella pneumoniae propane-1,3-diol + NAD+
-
 r
1.1.1.202 3-hydroxypropanal + NADPH + H+ NADPH is not substrate for wild-type, but for mutant D41G Klebsiella pneumoniae propane-1,3-diol + NADP+
-
 r
1.1.1.202 propane-1,3-diol + NAD+
-
 Klebsiella pneumoniae 3-hydroxypropanal + NADH + H+
-
 r
1.1.1.202 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]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.202 11.83
-
 NADP+ mutant D41G, pH 7.4, 37°C Klebsiella pneumoniae
1.1.1.202 51.99
-
 NAD+ wild-type, pH 7.4, 37°C Klebsiella pneumoniae
1.1.1.202 82.33
-
 NAD+ mutant D41G, pH 7.4, 37°C Klebsiella pneumoniae
1.1.1.202 90.64
-
 NADH wild-type, pH 7.4, 37°C Klebsiella pneumoniae
1.1.1.202 187.4
-
 NADPH mutant D41G, pH 7.4, 37°C Klebsiella pneumoniae
1.1.1.202 411.6
-
 NADH mutant D41G, pH 7.4, 37°C Klebsiella pneumoniae

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.202 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
1.1.1.202 NADPH no substrate for wild-type, but substrate for mutant D41G Klebsiella pneumoniae

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.1.202 12.2
-
 NADP+ mutant D41G, pH 7.4, 37°C Klebsiella pneumoniae
1.1.1.202 172
-
 NAD+ mutant D41G, pH 7.4, 37°C Klebsiella pneumoniae
1.1.1.202 260
-
 NAD+ wild-type, pH 7.4, 37°C Klebsiella pneumoniae
1.1.1.202 858
-
 NADH mutant D41G, pH 7.4, 37°C Klebsiella pneumoniae
1.1.1.202 1338
-
 NADPH mutant D41G, pH 7.4, 37°C Klebsiella pneumoniae
1.1.1.202 6043
-
 NADH wild-type, pH 7.4, 37°C Klebsiella pneumoniae