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

BRENDA support

Literature summary for 1.5.1.30 extracted from

  • Li, X.; Chow, D.C.; Tu, S.C.
    Thermodynamic analysis of the binding of oxidized and reduced FMN cofactor to Vibrio harveyi NADPH-FMN oxidoreductase FRP apoenzyme (2006), Biochemistry, 45, 14781-14787.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Vibrio harveyi
-
-
-

Reaction

Reaction Comment Organism Reaction ID
reduced riboflavin + NADP+ = riboflavin + NADPH + H+ binding of FMN by apoenzyme is noncooperative, exothermic and primarily enthalpy driven with significant conformational changes in enzyme upon binding. The kinetically deduced ping-pong mechanism is supported by measurement of binding affinities of the oxidized and reduced FMN cofoactors Vibrio harveyi