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Literature summary for 1.7.1.6 extracted from

  • Chen, H.; Feng, J.; Kweon, O.; Xu, H.; Cerniglia, C.
    Identification and molecular characterization of a novel flavin-free NADPH preferred azoreductase encoded by azoB in Pigmentiphaga kullae K24 (2010), BMC Biochem., 11, 13.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21-Gold(DE3)pLysS cells Pigmentiphaga kullae

KM Value [mM]

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 [Da] Molecular Weight Maximum [Da] Comment Organism
21300
-
calculated from amino acid sequence Pigmentiphaga kullae
22000
-
SDS-PAGE and gel filtration Pigmentiphaga kullae

Organism

Organism UniProt Comment Textmining
Pigmentiphaga kullae D5HN83
-
-
Pigmentiphaga kullae K24, ATCC BAA-795 D5HN83
-
-

Purification (Commentary)

Purification (Comment) Organism
phenyl Sepharose column chromatography and HiPrep SP XL column chromatography Pigmentiphaga kullae

Specific Activity [micromol/min/mg]

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 and Products (Substrate)

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

Subunits Comment Organism
monomer 1 * 22000, SDS-PAGE and gel filtration Pigmentiphaga kullae

Synonyms

Synonyms Comment Organism
AzoB
-
Pigmentiphaga kullae
azoreductase
-
Pigmentiphaga kullae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
for activity of the enzyme with Orange I Pigmentiphaga kullae

pH Optimum

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

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