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

BRENDA support

Literature summary for 1.14.13.2 extracted from

  • Entsch, B.; Palfey, B.A.; Ballou, D.P.; Massey, V.
    Catalytic function of tyrosine residues in para-hydroxybenzoate hydroxylase as determined by the study of site-directed mutants (1991), J. Biol. Chem., 266, 17341-17349.
    View publication on PubMed
Search for more literature for 1.14.13.2

Cloned(Commentary)

Cloned (Comment) Organism
expression of mutant enzymes Y201F and Y385F in Escherichia coli Pseudomonas aeruginosa

Protein Variants

Protein Variants Comment Organism
Y201F less than 6% of the activity of the wild-type enzyme. Reduction of FAD by NADPH is slower by 10fold, when the mutant enzyme-4-hydroxybenzoate complex reacts with oxygen, a long-lived flavin-C(4a)-hydroperoxide is observed, which slowly eliminates H2O2 with very little hydroxylation Pseudomonas aeruginosa
Y385F less than 6% of the activity of the wild-type enzyme. Reduction of FAD by NADPH is slower by 100fold, the mutant enzyme reacts with oxygen to form 25% oxidized enzyme and 75% flavin hydroperoxide, which successfully hydroxylates the substrate. The mutant also hydroxylates the product 3,4-dihydroxybenzoate to form gallic acid Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-hydroxybenzoate + NADPH + O2
-
 Pseudomonas aeruginosa protocatechuate + NADP+ + H2O
-
 ?
additional information mutant enzyme Y385F hydroxylates 3,4-dihydroxybenzoate to form gallic acid Pseudomonas aeruginosa ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.36
-
 4-hydroxybenzoate mutant enzyme Y385F Pseudomonas aeruginosa
0.42
-
 4-hydroxybenzoate mutant enzyme Y201F Pseudomonas aeruginosa
5.7
-
 4-hydroxybenzoate wild-type enzyme Pseudomonas aeruginosa