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Literature summary for 1.14.13.1 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)

Cloned (Comment) Organism
expression in Escherichia coli Pseudomonas putida

Crystallization (Commentary)

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

Protein Variants

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

KM Value [mM]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
-
-

Substrates and Products (Substrate)

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