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Literature summary for 1.14.13.2 extracted from

  • Ortiz-Maldonado, M.; Entsch, B.; Ballou, D.P.
    Oxygen reactions in p-hydroxybenzoate hydroxylase utilize the H-bond network during catalysis (2004), Biochemistry, 43, 15246-15257.
    View publication on PubMed
Search for more literature for 1.14.13.2

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pseudomonas aeruginosa

Protein Variants

Protein Variants Comment Organism
E49Q mutation enhances the positive charge in the active site of PHBH, rate of hydroxylation is above that of wild-type, the rate of release of product is slower than the rate of return of the flavin to the oxidized state Pseudomonas aeruginosa
E49Q investigation of oxygen half-reaction Pseudomonas aeruginosa
H72N rate of turnover is only about 8% of wild-type enzyme at all pH values Pseudomonas aeruginosa
H72N investigation of oxygen half-reaction Pseudomonas aeruginosa
K297M mutation decreases the positive charge in the active site of PHBH but does not interfere with with the H-bond network, 25fold decrease in the rate of hydroxylation compared to wild-type enzyme Pseudomonas aeruginosa
K297M investigation of oxygen half-reaction Pseudomonas aeruginosa
Y201F investigation of oxygen half-reaction Pseudomonas aeruginosa
Y385F in the oxygen half-reaction, the rate of hydroxylation is 25fold slower than that for the wild-type enzyme at pH 6.5, in contrast to wild-type enzyme there is some formation of H2O2 in the reaction Pseudomonas aeruginosa
Y385F investigation of oxygen half-reaction Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
-
-

Reaction

Reaction Comment Organism Reaction ID
4-hydroxybenzoate + NADPH + H+ + O2 = 3,4-dihydroxybenzoate + NADP+ + H2O rate of formation of the flavin hydroperoxide is not influenced by pH-change. Rate of hydroxylation reaction increases with pH. The H-bond network abstracts the phenolic proton from p-hydroxybenzoate in the transition state of oxygen transfer. Product deprotonation enhances the rate of a specific conformational change required for both product relase and the elimination of water Pseudomonas aeruginosa
a

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
PHBH
-
 Pseudomonas aeruginosa