Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli BL21-Gold(DE3)pLysS cells | Pigmentiphaga kullae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.001 | - |
NADPH | pH 6.8, 45°C | Pigmentiphaga kullae | |
0.003 | - |
Orange I | using NADPH as proton donor, at pH 6.8, 45°C | Pigmentiphaga kullae | |
0.0086 | - |
NADH | pH 6.8, 45°C | Pigmentiphaga kullae | |
0.17 | - |
Orange I | using NADH as proton donor, at pH 6.8, 45°C | Pigmentiphaga kullae |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
21300 | - |
calculated from amino acid sequence | Pigmentiphaga kullae |
22000 | - |
SDS-PAGE and gel filtration | Pigmentiphaga kullae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pigmentiphaga kullae | D5HN83 | - |
- |
Pigmentiphaga kullae K24, ATCC BAA-795 | D5HN83 | - |
- |
Purification (Comment) | Organism |
---|---|
phenyl Sepharose column chromatography and HiPrep SP XL column chromatography | Pigmentiphaga kullae |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
2.9 | - |
crude extract, using Orange I as the substrate with NADH as proton donor, pH 6.8, 45°C | Pigmentiphaga kullae |
10.1 | - |
purified enzyme, using Orange I as the substrate with NADH as proton donor, pH 6.8, 45°C | Pigmentiphaga kullae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Methyl Red, Amaranth, Ponceau BS, Ponceau S, Orange II, Orange G, Megneson II, 1-(4-nitrophenylazo)-2-naphthol, and 4-(4-nitrophenylazo)-resorcinol are not reduced by AzoB | Pigmentiphaga kullae | ? | - |
? | |
additional information | Methyl Red, Amaranth, Ponceau BS, Ponceau S, Orange II, Orange G, Megneson II, 1-(4-nitrophenylazo)-2-naphthol, and 4-(4-nitrophenylazo)-resorcinol are not reduced by AzoB | Pigmentiphaga kullae K24, ATCC BAA-795 | ? | - |
? | |
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ | - |
Pigmentiphaga kullae | 4-(dimethylamino)azobenzene + 2 NADPH + 2 H+ | - |
? | |
N,N-dimethyl-1,4-phenylenediamine + aniline + 2 NADP+ | - |
Pigmentiphaga kullae K24, ATCC BAA-795 | 4-(dimethylamino)azobenzene + 2 NADPH + 2 H+ | - |
? | |
Orange I + NADH | both NADH and NADPH can be used as an electron donor for its activity with 4-(4-hydroxy-1-naphthylazo)benzenesulfonic acid (Orange I) as substrate | Pigmentiphaga kullae | ? | - |
? | |
Orange I + NADH | both NADH and NADPH can be used as an electron donor for its activity with 4-(4-hydroxy-1-naphthylazo)benzenesulfonic acid (Orange I) as substrate | Pigmentiphaga kullae K24, ATCC BAA-795 | ? | - |
? | |
Orange I + NADPH | both NADH and NADPH can be used as an electron donor for its activity with 4-(4-hydroxy-1-naphthylazo)benzenesulfonic acid (Orange I) as substrate | Pigmentiphaga kullae | ? | - |
? | |
Orange I + NADPH | both NADH and NADPH can be used as an electron donor for its activity with 4-(4-hydroxy-1-naphthylazo)benzenesulfonic acid (Orange I) as substrate | Pigmentiphaga kullae K24, ATCC BAA-795 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 22000, SDS-PAGE and gel filtration | Pigmentiphaga kullae |
Synonyms | Comment | Organism |
---|---|---|
AzoB | - |
Pigmentiphaga kullae |
azoreductase | - |
Pigmentiphaga kullae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
45 | - |
for activity of the enzyme with Orange I | Pigmentiphaga kullae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
for activity of the enzyme with Orange I, in 50 mM Sorensen's phosphate buffer | Pigmentiphaga kullae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | AzoB belongs to the flavin-free azoreductase group | Pigmentiphaga kullae | |
NADH | when NADPH serves as the electron donor, the activity of the enzyme is 63% higher than that when NADH is used | Pigmentiphaga kullae | |
NADPH | when NADPH serves as the electron donor, the activity of the enzyme is 63% higher than that when NADH is used | Pigmentiphaga kullae |