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Literature summary extracted from

  • Liu, M.; Lei, B.; Ding, Q.; Lee, J.C.; Tu, S.C.
    Vibrio harveyi NADPH:FMN oxidoreductase: preparation and characterization of the apoenzyme and monomer-dimer equilibrium (1997), Arch. Biochem. Biophys., 337, 89-95.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.30 0.003
-
 NADPH enzyme reconstituted from apoenzyme and 2-thioFMN Vibrio harveyi
1.5.1.30 0.005
-
 FMN
-
 Vibrio harveyi
1.5.1.30 0.007
-
 2-thioFMN enzyme reconstituted from apoenzyme and 2-thioFMN Vibrio harveyi
1.5.1.30 0.011
-
 NADPH
-
 Vibrio harveyi
1.5.1.30 0.025
-
 riboflavin
-
 Vibrio harveyi
1.5.1.38 0.003
-
 NADPH pH 7.0, 23°C, enzyme derivative reconstituted from apoenzyme and 2-thioFMN Vibrio harveyi
1.5.1.38 0.005
-
 FMN pH 7.0, 23°C, native enzyme Vibrio harveyi
1.5.1.38 0.007
-
 2-thioFMN pH 7.0, 23°C, enzyme derivative reconstituted from apoenzyme and 2-thioFMN Vibrio harveyi
1.5.1.38 0.011
-
 NADPH pH 7.0, 23°C, native enzyme Vibrio harveyi
1.5.1.38 0.019
-
 FAD pH 7.0, 23°C, native enzyme Vibrio harveyi
1.5.1.38 0.025
-
 riboflavin pH 7.0, 23°C, native enzyme Vibrio harveyi

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.5.1.30 30000 38000 gel filtration Vibrio harveyi

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.1.30 riboflavin + NADPH Vibrio harveyi
-
 reduced riboflavin + NADP+
-
 ?
1.5.1.38 FMN + NADPH + H+ Vibrio harveyi
-
 FMNH2 + NADP+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.30 Vibrio harveyi
-
-
-
1.5.1.38 Vibrio harveyi
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.30 preparation of apoenzyme Vibrio harveyi
1.5.1.38
-
 Vibrio harveyi

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.30 FMN + NADPH
-
 Vibrio harveyi FMNH2 + NADP+
-
 ?
1.5.1.30 reduced 2-thioFMN + NAD+
-
 Vibrio harveyi ?
-
 r
1.5.1.30 riboflavin + NADPH
-
 Vibrio harveyi reduced riboflavin + NADP+
-
 ?
1.5.1.38 2-thioFMN + NADPH + H+ the holoenzyme reconstituted with 2-thioFMN is catalytically active in using either FMN or 2-thioFMN as a substrate Vibrio harveyi 2-thioFMNH2 + NADP+
-
 ?
1.5.1.38 FAD + NADPH + H+ Vmax/KM for riboflavin is 6fold lower compared to Vmax/Km for FMN Vibrio harveyi FADH2 + NADP+
-
 ?
1.5.1.38 FMN + NADPH + H+
-
 Vibrio harveyi FMNH2 + NADP+
-
 ?
1.5.1.38 FMN + NADPH + H+ the apoenzyme binds one FMN per enzyme monomer with a dissociation constant of 0.2 mM at 23°C. The reconstituted holoenzyme is catalytically as active as the native enzyme. FMN binding results in 87% and 92% of quenching of protein and flavin fluorescence, respectively, indicating a conformational difference between the apoprotein and the holoenzyme. Neither riboflavin nor FAD shows any appreciable binding to the cofactor site of the apoenzyme but both flavins are active substrates for the FMN-containing holoenzyme. The holoenzyme reconstituted with 2-thioFMN is catalytically active in using either FMN or 2-thioFMN as a substrate Vibrio harveyi FMNH2 + NADP+
-
 ?
1.5.1.38 riboflavin + NADPH + H+ Vmax/KM for riboflavin is 13fold lower compared to Vmax/Km for FMN Vibrio harveyi reduced riboflavin + NADP+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.5.1.30 dimer dimerization of native enzyme and apoenzyme, equilibrium ultracentrifugation Vibrio harveyi

Synonyms

EC Number Synonyms Comment Organism
1.5.1.30 NADPH:FMN oxidoreductase
-
 Vibrio harveyi
1.5.1.38 NADPH:FMN oxidoreductase
-
 Vibrio harveyi

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.5.1.38 23
-
 assay at Vibrio harveyi

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.1.38 7
-
 assay at Vibrio harveyi

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.30 2-thio-FMN
-
 Vibrio harveyi
1.5.1.30 FMN no cofactors are FAD and riboflavin Vibrio harveyi
1.5.1.38 2-thio-FMN binds to the cofactor site of the apoenzyme with an affinity similar to that for FMN binding. The holoenzyme reconstituted with 2-thioFMN is catalytically active in using either FMN or 2-thioFMN as a substrate Vibrio harveyi
1.5.1.38 FMN the apoenzyme binds one FMN per enzyme monomer with a dissociation constant of 0.2 mM at 23°C. The reconstituted holoenzyme is catalytically as active as the native enzyme. FMN binding results in 87% and 92% of quenching of protein and flavin fluorescence, respectively, indicating a conformational difference between the apoprotein and the holoenzyme. Neither riboflavin nor FAD shows any appreciable binding to the cofactor site of the apoenzyme but both flavins are active substrates for the FMN-containing holoenzyme Vibrio harveyi