1.7.1.17: FMN-dependent NADH-azoreductase
This is an abbreviated version!
For detailed information about FMN-dependent NADH-azoreductase, go to the full flat file.
Reaction
Synonyms
acpD, AZO, azo-dye reductase, AzoA, AzoR, AzoR1, azoreductase, AzoRo, AzrA, AzrG, flavin-containing oxygen-insensitive azoreductase, FMN dependent azoreductase, FMN-dependent methyl red reductase, FMN-dependent NADH-azo compound oxidoreductase, FMN-dependent NADH-azo reductase, FMN-dependent NADH-azoreductase, FMN-dependent-NADH azoreductase, indigo reductase, NADH-azoreductase
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General Information
General Information on EC 1.7.1.17 - FMN-dependent NADH-azoreductase
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evolution
physiological function
additional information
the enzyme catalyses the initial degradation step of azo dyes, characterized by one or more R1-N=N-R2 bonds
physiological function
the enzyme is responsible for the degradation of azo compounds. Residue Arg59 decides the substrate specificity of AzoR
physiological function
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the enzyme catalyses the initial degradation step of azo dyes, characterized by one or more R1-N=N-R2 bonds
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additional information
AzoR in its reduced form reveals a twisted butterfly bend of the isoalloxazine ring of the FMN cofactor and a rearrangement of solvent molecules. The enzyme performs a conformational change of the isoalloxazine ring and the solvent rearrangement upon reduction
additional information
structure homology modeling. An indigo carmine molecule is modeled into the active site using the molecular docking simulation, and the binding mode of indigo carmine is elucidated. Residue F105 plays a major role in the intersubunit aromatic interaction. Crystal structure analysis, overview
additional information
Bacillus smithii DSM 4216
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structure homology modeling. An indigo carmine molecule is modeled into the active site using the molecular docking simulation, and the binding mode of indigo carmine is elucidated. Residue F105 plays a major role in the intersubunit aromatic interaction. Crystal structure analysis, overview
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