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Literature summary extracted from

  • Suzuki, K.; Asao, E.; Nakamura, Y.; Nakamura, M.; Ohnishi, K.; Fukuda, S.
    Overexpression of salicylate hydroxylase and the crucial role of Lys163 as its NADH binding site (2000), J. Biochem., 128, 293-299.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.13.1 expression in Escherichia coli Pseudomonas putida

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.13.1 apoenzyme is crystallized by dialysis method, using ammonium sulfate as the precipitant Pseudomonas putida

Protein Variants

EC Number Protein Variants Comment Organism
1.14.13.1 K163E site directed mutagenesis, Lys163 is involved in the NADH-binding site Pseudomonas putida
1.14.13.1 K163G site directed mutagenesis, Lys163 is involved in the NADH-binding site Pseudomonas putida
1.14.13.1 K163R site directed mutagenesis, Lys163 is involved in the NADH-binding site Pseudomonas putida

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.13.1 additional information
-
 additional information FAD, salicylate and NADH, comparison of wild-type, recombinant and mutant enzyme Pseudomonas putida

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.13.1 45000
-
 recombinant native and mutant protein, expressed in E. coli, SDS-PAGE Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.1 Pseudomonas putida
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.1 salicylate + NADH + H+ + O2
-
 Pseudomonas putida catechol + NAD+ + H2O + CO2
-
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