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Literature summary for 1.7.1.17 extracted from

  • Langer, S.; Nakanishi, S.; Mathes, T.; Knaus, T.; Binter, A.; Macheroux, P.; Mase, T.; Miyakawa, T.; Tanokura, M.; Mack, M.
    The flavoenzyme azobenzene reductase AzoR from Escherichia coli binds roseoflavin mononucleotide (RoFMN) with high affinity and is less active in its RoFMN form (2013), Biochemistry, 52, 4288-4295 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.002
-
4'-(dimethylamino)-azobenzene-2-carboxylic acid cofactor roseoflavin mononucleotide, pH 7.4, 30°C Escherichia coli
0.027
-
4'-(dimethylamino)-azobenzene-2-carboxylic acid cofactor FMN, pH 7.4, 30°C Escherichia coli
0.26
-
NADH cofactor FMN, pH 7.4, 30°C Escherichia coli
0.269
-
NADH cofactor roseoflavin mononucleotide, pH 7.4, 30°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P41407
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4'-(dimethylamino)-azobenzene-2-carboxylic acid + 2 NADH + 2 H+ i.e. methyl red Escherichia coli 2-aminobenzoic acid + N,N-dimethyl-p-phenylenediamine + 2 NAD+
-
?

Synonyms

Synonyms Comment Organism
AzoR
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FMN
-
Escherichia coli
additional information no cofactor: 8-amino-8-demethyl-riboflavin mononucleotide Escherichia coli
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 Escherichia coli