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

BRENDA support

Literature summary for 1.14.13.2 extracted from

  • Ortiz-Maldonado, M.; Gatti, D.; Ballou, D.P.; Massey, V.
    Structure-function correlation of the reaction of reduced nicotinamide analogues with p-hydroxybenzoate hydroxylase substituted with a series of 8-substituted flavins (1999), Biochemistry, 38, 16636-16647.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
-
-

Cofactor

Cofactor Comment Organism Structure
FAD two flavin conformations in the enzyme: the in-position and the out-position. Substrate hydroxylation occurs while the flavin in the enzyme is in the in-conformation. Flavin must move to the out-conformation for proper formation of the charge-transfer complex between NADPH and FAD that is necessary for rapid flavin reduction Pseudomonas aeruginosa
FAD thermodynamic and kinetic constants of the enzyme reconstituted with 8-substituted flavins Pseudomonas aeruginosa