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