1.5.1.39: FMN reductase [NAD(P)H]
This is an abbreviated version!
For detailed information about FMN reductase [NAD(P)H], go to the full flat file.
Reaction
Synonyms
ChuY, EC 1.5.1.29, EC 1.6.8.1, flavin mononucleotide reductase, FMN reductase, fre, FRG, H2O-forming FOR, LrFOR, NAD(P)H-flavin reductase, NAD(P)H:FMN-oxidoreductase, NADH: FMN oxidoreductase, NADPH-dependent FMN reductase, NfoR, non-specific NAD(P)H-FMN reductase, pden_5119, Red, SsuE, two-component FMN-dependent monooxygenase, water forming NADH: FMN oxidoreductase
ECTree
1.5.1.39 FMN reductase [NAD(P)H]Advanced search results
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results (Inhibitors
Inhibitors on EC 1.5.1.39 - FMN reductase [NAD(P)H]
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
AMP
competitive inhibition against NADH and uncompetitive inhibition against FMN
lumichrome
7,8-dimethylalloxazine, competitive inhibitor versus FMN, and mixed noncompetitive inhibitor with respect to NADH
additional information
the substrate binding order is investigated by carrying out dead-end inhibition studies using lumichrome (7,8-dimethylalloxazine) and AMP as inhibitory analogues of FMN and NADH. Strains Pd9233 and Pd9311 contain aa3-type or cbb3-type cytochrome c oxidase, respectively, as the only terminal oxidase of the respiratory electron transfer chain, the flux capacity through terminal oxidase is reduced in strain Pd9311 compared to strain Pd9233 or wild-type strain, manifested by the much lower specific activity of TMPD oxidase found in the cytoplasmic membrane fraction. The pden_5119 transcript in Pd9311 cells but not in Pd9233 cells is elevated similarly as observed in the wild-type strain growing in the presence of electron transfer inhibitors. Downregulation of terminal oxidase thus indeed results in a similar outcome as chemical inhibition
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additional information
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the substrate binding order is investigated by carrying out dead-end inhibition studies using lumichrome (7,8-dimethylalloxazine) and AMP as inhibitory analogues of FMN and NADH. Strains Pd9233 and Pd9311 contain aa3-type or cbb3-type cytochrome c oxidase, respectively, as the only terminal oxidase of the respiratory electron transfer chain, the flux capacity through terminal oxidase is reduced in strain Pd9311 compared to strain Pd9233 or wild-type strain, manifested by the much lower specific activity of TMPD oxidase found in the cytoplasmic membrane fraction. The pden_5119 transcript in Pd9311 cells but not in Pd9233 cells is elevated similarly as observed in the wild-type strain growing in the presence of electron transfer inhibitors. Downregulation of terminal oxidase thus indeed results in a similar outcome as chemical inhibition
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