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Literature summary for 1.5.1.38 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
Search for more literature for 1.5.1.38

KM Value [mM]

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

Purification (Commentary)

Purification (Comment) Organism
-
 Vibrio harveyi

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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+
-
 ?
FAD + NADPH + H+ Vmax/KM for riboflavin is 6fold lower compared to Vmax/Km for FMN Vibrio harveyi FADH2 + NADP+
-
 ?
FMN + NADPH + H+
-
 Vibrio harveyi FMNH2 + NADP+
-
 ?
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+
-
 ?
riboflavin + NADPH + H+ Vmax/KM for riboflavin is 13fold lower compared to Vmax/Km for FMN Vibrio harveyi reduced riboflavin + NADP+
-
 ?

Synonyms

Synonyms Comment Organism
NADPH:FMN oxidoreductase
-
 Vibrio harveyi

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
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
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