Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.1.2.45 extracted from

  • Eaton, R.W.; Chapman, P.J.
    Bacterial metabolism of naphthalene: Construction and use of recombinant bacteria to study ring cleavage of 1,2-dihydroxynaphthalene and subsequent reactions (1992), J. Bacteriol., 174, 7542-7554.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pseudomonas putida

Inhibitors

Inhibitors Comment Organism Structure
additional information not sensitive to 5 mM EDTA Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Pseudomonas putida Q51947
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.55
-
recombinant enzyme Pseudomonas putida

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(E)-2'-hydroxybenzylidenepyruvate + O2 the equilibrium in this reaction favors cleavage Pseudomonas putida salicylaldehyde + pyruvate
-
r
additional information no activity with trans-benzylidenepyruvate, trans-o-methoxybenzylidenepyruvate or trans-o-hydroxycinnamate. The hydratase-aldolase catalyzes the condensation of pyruvate with several other aromatic aldehydes, including benzaldehyde, to give trans-benzylidenepyruvate. Since benzylidenepyruvate is not a substrate for the enzyme, the reaction is irreversible and can be carried out to completion by using relatively low concentrations of the substrates, benzaldehyde and pyruvate Pseudomonas putida ?
-
?

Synonyms

Synonyms Comment Organism
tHBPA hydratase-aldolase
-
Pseudomonas putida

Cofactor

Cofactor Comment Organism Structure
additional information no cofactor required Pseudomonas putida