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EC Tree
IUBMB Comments Requires Fe(II). The enzyme, characterized from different bacteria, is a nonheme iron dioxygenase in the bicupin family.
The enzyme appears in viruses and cellular organisms
Synonyms
5-aminosalicylate 1,2-dioxygenase,
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mabB
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5-aminosalicylate + O2 = (2Z,4E)-4-amino-6-oxohepta-2,4-dienedioate
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5-aminosalicylate:oxygen 1,2-oxidoreductase (ring-opening)
Requires Fe(II). The enzyme, characterized from different bacteria, is a nonheme iron dioxygenase in the bicupin family.
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1-hydroxy-2-naphthoate + O2
(3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
oxidized by MabB at a rate less than 1% of that observed for 5-aminosalicylate
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5-aminosalicylate + O2
(2Z,4E)-4-amino-6-oxohepta-2,4-dienedioate
gentisate + O2
maleylpyruvate
the two oxygen atoms incorporated into the product are both from the dioxygen molecule. Both 5-aminosalicylate and gentisate can be converted by MabB. The catalytic efficiency of MabB for 5-aminosalicylate is much higher (about 70fold) than that for gentisate
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additional information
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no activity is detected in reaction with salicylate
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5-aminosalicylate + O2
(2Z,4E)-4-amino-6-oxohepta-2,4-dienedioate
the enzyme plays an important physiological role in 3-aminobenzoate degradation in Comamonas sp. strain QT12
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5-aminosalicylate + O2
(2Z,4E)-4-amino-6-oxohepta-2,4-dienedioate
the two oxygen atoms incorporated into the product are both from the dioxygen molecule. Both 5-aminosalicylate and gentisate can be converted by MabB. The catalytic efficiency of MabB for 5-aminosalicylate is much higher (about 70fold) than that for gentisate
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5-aminosalicylate + O2
(2Z,4E)-4-amino-6-oxohepta-2,4-dienedioate
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the enzyme participates in the metabolism of 5-aminosalicylate
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5-aminosalicylate + O2
(2Z,4E)-4-amino-6-oxohepta-2,4-dienedioate
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the enzyme exhibits no activity with gentisate
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5-aminosalicylate + O2
(2Z,4E)-4-amino-6-oxohepta-2,4-dienedioate
5-aminosalicylate + O2
(2Z,4E)-4-amino-6-oxohepta-2,4-dienedioate
the enzyme plays an important physiological role in 3-aminobenzoate degradation in Comamonas sp. strain QT12
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5-aminosalicylate + O2
(2Z,4E)-4-amino-6-oxohepta-2,4-dienedioate
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the enzyme participates in the metabolism of 5-aminosalicylate
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Fe2+
required for the catalytic activity of the purified enzyme, nonheme iron dioxygenase. The enzyme activity of MabB increases about 2.3fold with the addition of 0.25 mM Fe2+, and 74% enzyme activity is observed when 0.25 mM Fe3+ is added
Fe2+
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Fe2+-dependent enzyme
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1,10-phenanthroline
0.01 mM, 89% inhibition
EDTA
1 mM, 31% inhibition
SDS
1 mM, complete inhibition
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0.052
5-Aminosalicylate
pH 8.0, 25°C, wild-type enzyme
0.823
gentisate
pH 8.0, 25°C, wild-type enzyme
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6.5 - 9
pH 6.5: about 50% of maximal activity, pH 9.0: about 40% of maximal activity
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10 - 45
10°C: maximal activity, 45°C: about 60% of maximal activity
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UniProt
brenda
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brenda
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malfunction
the mabB-disrupted mutant loses the ability to grow on 3-aminobenzoate
metabolism
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the enzyme participates in the metabolism of 5-aminosalicylate
metabolism
the enzyme plays an important physiological role in 3-aminobenzoate degradation in Comamonas sp. strain QT12
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A0A1V0ELS9_9BURK
374
0
41509
TrEMBL
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G93A
the mutant enzyme shows the ability to oxidize salicylate, the wild-type enzyme shows no activity with salicylate
H107A
mutant enzyme shows no enzymatic activity
H109A
mutant enzyme shows no enzymatic activity
H150A
mutant enzyme shows no enzymatic activity
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8
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23°C, 100 mM-Tris/HCl, 20 h, activity is completely abolished
747014
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23
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pH 8.0, 100 mM-Tris/HCl, 20 h, activity is completely abolished
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23°C, pH 8.0, 100 mM-Tris/HCl, 20 h, activity is completely abolished
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heterologously expressed in Escherichia coli as a His-tagged enzyme
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the enzyme is induced by 3-aminobenzoate or its degradation intermediates
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Stolz, A.; Noertemann, B.; Knackmuss, H.J.
Bacterial metabolism of 5-aminosalicylic acid. Initial ring cleavage
Biochem. J.
282
675-680
1992
Pusillimonas noertemannii
brenda
Yu, H.; Zhao, S.; Guo, L.
Novel Gene encoding 5-aminosalicylate 1,2-dioxygenase from Comamonas sp. strain QT12 and catalytic properties of the purified enzyme
J. Bacteriol.
200
e00395-17
2018
Comamonas thiooxydans (A0A1V0ELS9)
brenda
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