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

BRENDA support

Literature summary for 1.14.13.2 extracted from

  • Frederick, K.K.; Palfey, B.A.
    Kinetics of proton-linked flavin conformational changes in p-hydroxybenzoate hydroxylase (2005), Biochemistry, 44, 13304-13314.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
H72N disruption of proton-transfer network, kinetic analysis Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa P20586
-
-

Reaction

Reaction Comment Organism Reaction ID
4-hydroxybenzoate + NADPH + H+ + O2 = 3,4-dihydroxybenzoate + NADP+ + H2O kinetic scheme of reductive half-reaction, flavin movement can occur in the presence or absence of NADPH, but NADPH stimulates movement to the reactive conformation required for hydride transfer Pseudomonas aeruginosa

Cofactor

Cofactor Comment Organism Structure
FAD
-
Pseudomonas aeruginosa
NADPH
-
Pseudomonas aeruginosa