Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.7.1.6 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
Search for more literature for 1.7.1.6

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.002
-
 Methyl red cofactor roseoflavin mononucleotide, pH 7.4, 30°C Escherichia coli
0.027
-
 Methyl red 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
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methyl red + NADH + H+
-
 Escherichia coli ? + NAD+
-
 ?

Synonyms

Synonyms Comment Organism
AzoR
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FMN
-
 Escherichia coli
additional information the flavin mononucleotide analogue 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. The AzoR-roseoflavin mononucleotide holoenzyme complex shows 30% of AzoR-FMN activity in a standard assay Escherichia coli