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
ECTree
1.7.1.17 FMN-dependent NADH-azoreductaseAdvanced search results
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results (Cofactor
Cofactor on EC 1.7.1.17 - FMN-dependent NADH-azoreductase
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COFACTOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
roseoflavin mononucleotide
roseoflavin mononucleotide binds to the AzoR apoenzyme with an even higher affinity compared to that of the natural cofactor FMN. Roseoflavin mononucleotide binding does not affect the overall topology of the enzyme and also does not interfere with dimerization of AzoR. With roseoflavin mononucleotide, the holoenzyme shiws about 30% of wild-type activity
FAD
60% of the activity with FMN. FAD is stably retained in the enzyme molecule without degradation to FMN
FMN
a flavin-containing enzyme the enzyme binds 1 FMN per subunit
FMN
FMN is tightly bound to the protein moiety, and this interaction is essential for the crystallization of AzoR
FMN
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coexistence of at least three FMN-containing components in wild-type AzoR, i.e. FMN emitting at 490 nm, 530 nm and 600 nm, respectively
FMN
residues Trp105, Asn106, Leu107, Gly150, Gly151, Tyr153, Asn121 and Tyr129 are involved in binding the FMN isoalloxazine ring. Residue Trp105 is involved in FMN stabilization and destabilization
FMN
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adding FMN as cofactor significantly improves the azodye-reducing activity of the cytosolic extract
FMN
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adding FMN as cofactor significantly improves the azodye-reducing activity of the cytosolic extract
FMN
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adding FMN as cofactor significantly improves the azodye-reducing activity of the cytosolic extract
FMN
FMN is present in the enzyme as a coenzyme and is not covalently bound to the enzyme
NADH
reaction with NADH is 13fold faster than with NADPH
NADPH
reaction with NADH is 13fold faster than with NADPH
additional information
AzoR utilizes NADH but not NADPH as an electron donor and binds FMN as a flavin cofactor
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additional information
no cofactor: 8-amino-8-demethyl-riboflavin mononucleotide
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