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Literature summary extracted from

  • Palfey, B.A.; Basu, R.; Frederick, K.K.; Entsch, B.; Ballou, D.P.
    Role of protein flexibility in the catalytic cycle of p-hydroxybenzoate hydroxylase elucidated by the Pro293Ser mutant (2002), Biochemistry, 41, 8438-8446.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.13.2 expression in Escherichia coli Pseudomonas aeruginosa

Protein Variants

EC Number Protein Variants Comment Organism
1.14.13.2 P293S mutation decreases the stability of the folded mutant protein compared to the wild-type PHBH Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.13.2 4-hydroxybenzoate + NADPH + O2 Pseudomonas aeruginosa
-
 protocatechuate + NADP+ + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.2 Pseudomonas aeruginosa
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.2 4-hydroxybenzoate + NADPH + O2
-
 Pseudomonas aeruginosa protocatechuate + NADP+ + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.13.2 PHBH
-
 Pseudomonas aeruginosa

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.2 FAD
-
 Pseudomonas aeruginosa
1.14.13.2 NADPH
-
 Pseudomonas aeruginosa