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Literature summary extracted from

  • Ryan, A.
    Azoreductases in drug metabolism (2017), Br. J. Pharmacol., 174, 2161-2173 .
No PubMed abstract available

Application

EC Number Application Comment Organism
1.7.1.6 drug development azoreductases from enteric bacteria are targets in the development of drugs for the treatment of colon related disorders Bacillus subtilis
1.7.1.6 drug development azoreductases from enteric bacteria are targets in the development of drugs for the treatment of colon related disorders Escherichia coli
1.7.1.6 drug development azoreductases from enteric bacteria are targets in the development of drugs for the treatment of colon related disorders Cereibacter sphaeroides
1.7.1.6 drug development azoreductases from enteric bacteria are targets in the development of drugs for the treatment of colon related disorders Pseudomonas putida
1.7.1.6 drug development azoreductases from enteric bacteria are targets in the development of drugs for the treatment of colon related disorders Enterococcus faecalis
1.7.1.6 drug development azoreductases from enteric bacteria are targets in the development of drugs for the treatment of colon related disorders Bacillus sp. B29
1.7.1.6 drug development azoreductases from enteric bacteria are targets in the development of drugs for the treatment of colon related disorders Pseudomonas aeruginosa

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.7.1.6 phylogenetic tree Bacillus subtilis
1.7.1.6 phylogenetic tree Escherichia coli
1.7.1.6 phylogenetic tree Cereibacter sphaeroides
1.7.1.6 phylogenetic tree Pseudomonas putida
1.7.1.6 phylogenetic tree Enterococcus faecalis
1.7.1.6 phylogenetic tree Bacillus sp. B29
1.7.1.6 phylogenetic tree Pseudomonas aeruginosa

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.7.1.6 structure of balsalazide bound to paAzoR1, PDBs ID 3LT5 Pseudomonas aeruginosa
1.7.1.6 structure of Orange I bound to AzrC, PDBs ID 3W79 Bacillus sp. B29
1.7.1.6 structure of reactive black 5 bound to ppAzoR, PDBs ID 4C14 Pseudomonas putida

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.7.1.6 Cibacron blue a competitive NAD(P)H inhibitor Bacillus sp. B29
1.7.1.6 Cibacron blue a competitive NAD(P)H inhibitor Bacillus subtilis
1.7.1.6 Cibacron blue a competitive NAD(P)H inhibitor Cereibacter sphaeroides
1.7.1.6 Cibacron blue a competitive NAD(P)H inhibitor Enterococcus faecalis
1.7.1.6 Cibacron blue a competitive NAD(P)H inhibitor Escherichia coli
1.7.1.6 Cibacron blue a competitive NAD(P)H inhibitor Pseudomonas aeruginosa
1.7.1.6 Cibacron blue a competitive NAD(P)H inhibitor Pseudomonas putida

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.7.1.6 additional information azoreductases are primarily cytosolic enzymes, but have been shown to be secreted during exposure of bacteria to azo dyes Bacillus subtilis
-
-
1.7.1.6 additional information azoreductases are primarily cytosolic enzymes, but have been shown to be secreted during exposure of bacteria to azo dyes Escherichia coli
-
-
1.7.1.6 additional information azoreductases are primarily cytosolic enzymes, but have been shown to be secreted during exposure of bacteria to azo dyes Cereibacter sphaeroides
-
-
1.7.1.6 additional information azoreductases are primarily cytosolic enzymes, but have been shown to be secreted during exposure of bacteria to azo dyes Pseudomonas putida
-
-
1.7.1.6 additional information azoreductases are primarily cytosolic enzymes, but have been shown to be secreted during exposure of bacteria to azo dyes Enterococcus faecalis
-
-
1.7.1.6 additional information azoreductases are primarily cytosolic enzymes, but have been shown to be secreted during exposure of bacteria to azo dyes Bacillus sp. B29
-
-
1.7.1.6 additional information azoreductases are primarily cytosolic enzymes, but have been shown to be secreted during exposure of bacteria to azo dyes Pseudomonas aeruginosa
-
-

Organism

EC Number Organism UniProt Comment Textmining
1.7.1.6 Bacillus sp. B29 C0STY1
-
-
1.7.1.6 Bacillus subtilis
-
-
-
1.7.1.6 Cereibacter sphaeroides
-
-
-
1.7.1.6 Enterococcus faecalis
-
-
-
1.7.1.6 Escherichia coli
-
-
-
1.7.1.6 Pseudomonas aeruginosa Q9I5F3
-
-
1.7.1.6 Pseudomonas putida
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.7.1.6 N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ = 4-(dimethylamino)azobenzene + 2 NADPH + 2 H+ the catalytic reaction requires tautomerisation of the azo compound to a quinoneimine and provides a unifying mechanism for the reduction of azo substrates by azoreductases Bacillus subtilis
a
1.7.1.6 N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ = 4-(dimethylamino)azobenzene + 2 NADPH + 2 H+ the catalytic reaction requires tautomerisation of the azo compound to a quinoneimine and provides a unifying mechanism for the reduction of azo substrates by azoreductases Cereibacter sphaeroides
a
1.7.1.6 N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ = 4-(dimethylamino)azobenzene + 2 NADPH + 2 H+ the catalytic reaction requires tautomerisation of the azo compound to a quinoneimine and provides a unifying mechanism for the reduction of azo substrates by azoreductases Pseudomonas putida
a
1.7.1.6 N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ = 4-(dimethylamino)azobenzene + 2 NADPH + 2 H+ the catalytic reaction requires tautomerisation of the azo compound to a quinoneimine and provides a unifying mechanism for the reduction of azo substrates by azoreductases Enterococcus faecalis
a
1.7.1.6 N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ = 4-(dimethylamino)azobenzene + 2 NADPH + 2 H+ the catalytic reaction requires tautomerisation of the azo compound to a quinoneimine and provides a unifying mechanism for the reduction of azo substrates by azoreductases Bacillus sp. B29
a
1.7.1.6 N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ = 4-(dimethylamino)azobenzene + 2 NADPH + 2 H+ the catalytic reaction requires tautomerisation of the azo compound to a quinoneimine and provides a unifying mechanism for the reduction of azo substrates by azoreductases Pseudomonas aeruginosa
a
1.7.1.6 N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ = 4-(dimethylamino)azobenzene + 2 NADPH + 2 H+ the catalytic reaction requires tautomerisation of the azo compound to a quinoneimine and provides a unifying mechanism for the reduction of azo substrates by azoreductases, mechanism for azoreduction by FMN-dependent azoreductases, overview. N5 of FMN accepts a hydride during oxidation of NAD(P)H and donates it upon reduction of the substrate Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.1.6 balsalazide + NADPH + H+ tautomeric forms of balsalazide occur in solution, reaction mechanism, overview Pseudomonas aeruginosa ? + NADP+
-
 ?
1.7.1.6 additional information in general, the substrates of azoreductases do not make many specific hydrophilic interactions, which explains the ability of the active site to accommodate a range of hydrophobic substrates Bacillus subtilis ?
-
 ?
1.7.1.6 additional information in general, the substrates of azoreductases do not make many specific hydrophilic interactions, which explains the ability of the active site to accommodate a range of hydrophobic substrates Escherichia coli ?
-
 ?
1.7.1.6 additional information in general, the substrates of azoreductases do not make many specific hydrophilic interactions, which explains the ability of the active site to accommodate a range of hydrophobic substrates Cereibacter sphaeroides ?
-
 ?
1.7.1.6 additional information in general, the substrates of azoreductases do not make many specific hydrophilic interactions, which explains the ability of the active site to accommodate a range of hydrophobic substrates Pseudomonas putida ?
-
 ?
1.7.1.6 additional information in general, the substrates of azoreductases do not make many specific hydrophilic interactions, which explains the ability of the active site to accommodate a range of hydrophobic substrates Enterococcus faecalis ?
-
 ?
1.7.1.6 additional information in general, the substrates of azoreductases do not make many specific hydrophilic interactions, which explains the ability of the active site to accommodate a range of hydrophobic substrates Bacillus sp. B29 ?
-
 ?
1.7.1.6 additional information in general, the substrates of azoreductases do not make many specific hydrophilic interactions, which explains the ability of the active site to accommodate a range of hydrophobic substrates Pseudomonas aeruginosa ?
-
 ?
1.7.1.6 olsalazine + NADPH + H+
-
 Escherichia coli ? + NADP+
-
 ?
1.7.1.6 Orange I + NADPH + H+
-
 Bacillus sp. B29 ? + NADP+
-
 ?
1.7.1.6 reactive black 5 + NADPH + H+
-
 Pseudomonas putida ? + NADP+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.7.1.6 homodimer homodimeric flavodoxin fold of ecAzoR. The active sites of the enzyme are situated at the dimer interface and are formed by residues from both monomers. One molecule of flavin is bound within each active site and is required for activity Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.7.1.6 AzoR
-
 Escherichia coli
1.7.1.6 azoreductase
-
 Bacillus subtilis
1.7.1.6 azoreductase
-
 Escherichia coli
1.7.1.6 azoreductase
-
 Cereibacter sphaeroides
1.7.1.6 azoreductase
-
 Pseudomonas putida
1.7.1.6 azoreductase
-
 Enterococcus faecalis
1.7.1.6 azoreductase
-
 Bacillus sp. B29
1.7.1.6 azoreductase
-
 Pseudomonas aeruginosa
1.7.1.6 AzrC
-
 Bacillus sp. B29
1.7.1.6 bsAzoR
-
 Bacillus subtilis
1.7.1.6 class 1 azoreductase
-
 Escherichia coli
1.7.1.6 class 1 azoreductase
-
 Enterococcus faecalis
1.7.1.6 class 1 azoreductase
-
 Pseudomonas aeruginosa
1.7.1.6 class 2 azoreductase
-
 Bacillus subtilis
1.7.1.6 class 2 azoreductase
-
 Cereibacter sphaeroides
1.7.1.6 class 2 azoreductase
-
 Bacillus sp. B29
1.7.1.6 ecAzoR
-
 Escherichia coli
1.7.1.6 efAzoR
-
 Enterococcus faecalis
1.7.1.6 flavin-dependent azoreductase
-
 Escherichia coli
1.7.1.6 paAzoR1
-
 Pseudomonas aeruginosa
1.7.1.6 PpAzoR
-
 Pseudomonas putida
1.7.1.6 rsAzoR
-
 Cereibacter sphaeroides

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.1.6 FMN a flavin-dependent azoreductase, FMN is anchored by a series of sequence-independent hydrogen bonds to a structural motif referred to as the FMN binding cradle. One molecule of flavin is bound within each active site and is required for activity Escherichia coli
1.7.1.6 NADPH
-
 Bacillus subtilis
1.7.1.6 NADPH
-
 Escherichia coli
1.7.1.6 NADPH
-
 Cereibacter sphaeroides
1.7.1.6 NADPH
-
 Pseudomonas putida
1.7.1.6 NADPH
-
 Enterococcus faecalis
1.7.1.6 NADPH
-
 Bacillus sp. B29
1.7.1.6 NADPH
-
 Pseudomonas aeruginosa

General Information

EC Number General Information Comment Organism
1.7.1.6 evolution phylogeny of azoreductases, overview Bacillus subtilis
1.7.1.6 evolution phylogeny of azoreductases, overview Escherichia coli
1.7.1.6 evolution phylogeny of azoreductases, overview Cereibacter sphaeroides
1.7.1.6 evolution phylogeny of azoreductases, overview Pseudomonas putida
1.7.1.6 evolution phylogeny of azoreductases, overview Enterococcus faecalis
1.7.1.6 evolution phylogeny of azoreductases, overview Bacillus sp. B29
1.7.1.6 evolution phylogeny of azoreductases, overview Pseudomonas aeruginosa
1.7.1.6 additional information active site structure of ecAzoR, overview. The active sites of the enzyme are situated at the dimer interface and are formed by residues from both monomers. One molecule of flavin is bound within each active site and is required for activity Escherichia coli
1.7.1.6 physiological function bacterial azoreductases are associated with the activation of two classes of drug, azo drugs for the treatment of inflammatory bowel disease and nitrofuran antibiotics, mechanism of reduction of azo compounds, overview Bacillus subtilis
1.7.1.6 physiological function bacterial azoreductases are associated with the activation of two classes of drug, azo drugs for the treatment of inflammatory bowel disease and nitrofuran antibiotics, mechanism of reduction of azo compounds, overview Escherichia coli
1.7.1.6 physiological function bacterial azoreductases are associated with the activation of two classes of drug, azo drugs for the treatment of inflammatory bowel disease and nitrofuran antibiotics, mechanism of reduction of azo compounds, overview Cereibacter sphaeroides
1.7.1.6 physiological function bacterial azoreductases are associated with the activation of two classes of drug, azo drugs for the treatment of inflammatory bowel disease and nitrofuran antibiotics, mechanism of reduction of azo compounds, overview Pseudomonas putida
1.7.1.6 physiological function bacterial azoreductases are associated with the activation of two classes of drug, azo drugs for the treatment of inflammatory bowel disease and nitrofuran antibiotics, mechanism of reduction of azo compounds, overview Enterococcus faecalis
1.7.1.6 physiological function bacterial azoreductases are associated with the activation of two classes of drug, azo drugs for the treatment of inflammatory bowel disease and nitrofuran antibiotics, mechanism of reduction of azo compounds, overview Bacillus sp. B29
1.7.1.6 physiological function bacterial azoreductases are associated with the activation of two classes of drug, azo drugs for the treatment of inflammatory bowel disease and nitrofuran antibiotics, mechanism of reduction of azo compounds, overview Pseudomonas aeruginosa