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Literature summary for 1.7.1.6 extracted from

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

Application

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

Cloned(Commentary)

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

Crystallization (Commentary)

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

Inhibitors

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

Localization

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

Organism

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

Reaction

Reaction Comment Organism Reaction ID
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
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
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
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
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
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
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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
balsalazide + NADPH + H+ tautomeric forms of balsalazide occur in solution, reaction mechanism, overview Pseudomonas aeruginosa ? + NADP+
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
olsalazine + NADPH + H+
-
Escherichia coli ? + NADP+
-
?
Orange I + NADPH + H+
-
Bacillus sp. B29 ? + NADP+
-
?
reactive black 5 + NADPH + H+
-
Pseudomonas putida ? + NADP+
-
?

Subunits

Subunits Comment Organism
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

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

Cofactor

Cofactor Comment Organism Structure
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
NADPH
-
Bacillus subtilis
NADPH
-
Escherichia coli
NADPH
-
Cereibacter sphaeroides
NADPH
-
Pseudomonas putida
NADPH
-
Enterococcus faecalis
NADPH
-
Bacillus sp. B29
NADPH
-
Pseudomonas aeruginosa

General Information

General Information Comment Organism
evolution phylogeny of azoreductases, overview Bacillus subtilis
evolution phylogeny of azoreductases, overview Escherichia coli
evolution phylogeny of azoreductases, overview Cereibacter sphaeroides
evolution phylogeny of azoreductases, overview Pseudomonas putida
evolution phylogeny of azoreductases, overview Enterococcus faecalis
evolution phylogeny of azoreductases, overview Bacillus sp. B29
evolution phylogeny of azoreductases, overview Pseudomonas aeruginosa
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
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
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
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
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
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
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
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