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Literature summary for 1.5.1.38 extracted from

  • Lei, B.; Tu, S.C.
    Mechanism of reduced flavin transfer from Vibrio harveyi NADPH-FMN oxidoreductase to luciferase (1998), Biochemistry, 37, 14623-14629.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
additional information FMN at concentrations over 0.002 mM significantly inhibits the coupled reaction in both light intensity and quantum yield, and shows apparent noncompetitive and competitive inhibition patterns against NADPH and luciferase, respectively. No inhibition of the NADPH oxidation is detected under identical conditions Vibrio harveyi

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information the kinetic mechanism of FRP is changed to a sequential pattern with a Km(FMN) of 0.003 mM and a Km(NADPH) of 0.02 mM in a luciferase-coupled assay measuring light emission Vibrio harveyi
0.008
-
FMN pH 7.0, 23°C, single-enzyme spectrophotometric assay monitoring the NADPH oxidation Vibrio harveyi
0.02
-
NADPH pH 7.0, 23°C, single-enzyme spectrophotometric assay monitoring the NADPH oxidation Vibrio harveyi

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
FMN + NADPH + H+ Vibrio harveyi
-
FMNH2 + NADP+
-
?

Organism

Organism UniProt Comment Textmining
Vibrio harveyi
-
-
-

Reaction

Reaction Comment Organism Reaction ID
FMNH2 + NADP+ = FMN + NADPH + H+ ping-pong kinetic pattern Vibrio harveyi

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
FMN + NADPH + H+
-
Vibrio harveyi FMNH2 + NADP+
-
?

Synonyms

Synonyms Comment Organism
FRP
-
Vibrio harveyi
NADPH-FMN oxidoreductase
-
Vibrio harveyi