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Literature summary for 1.13.11.86 extracted from
- Novel Gene encoding 5-aminosalicylate 1,2-dioxygenase from Comamonas sp. strain QT12 and catalytic properties of the purified enzyme (2018), J. Bacteriol., 200, e00395-17 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| heterologously expressed in Escherichia coli as a His-tagged enzyme | Comamonas thiooxydans |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| G93A | the mutant enzyme shows the ability to oxidize salicylate, the wild-type enzyme shows no activity with salicylate | Comamonas thiooxydans |
| H107A | mutant enzyme shows no enzymatic activity | Comamonas thiooxydans |
| H109A | mutant enzyme shows no enzymatic activity | Comamonas thiooxydans |
| H150A | mutant enzyme shows no enzymatic activity | Comamonas thiooxydans |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 1,10-phenanthroline | 0.01 mM, 89% inhibition | Comamonas thiooxydans |  |
| EDTA | 1 mM, 31% inhibition | Comamonas thiooxydans | |
| SDS | 1 mM, complete inhibition | Comamonas thiooxydans | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.052 | - |
5-Aminosalicylate | pH 8.0, 25°C, wild-type enzyme | Comamonas thiooxydans | |
| 0.823 | - |
gentisate | pH 8.0, 25°C, wild-type enzyme | Comamonas thiooxydans | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| 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 | Comamonas thiooxydans | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 45000 | - |
SDS-PAGE | Comamonas thiooxydans |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5-aminosalicylate + O2 | Comamonas thiooxydans | the enzyme plays an important physiological role in 3-aminobenzoate degradation in Comamonas sp. strain QT12 | (2Z,4E)-4-amino-6-oxohepta-2,4-dienedioate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Comamonas thiooxydans | A0A1V0ELS9 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Comamonas thiooxydans |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 1-hydroxy-2-naphthoate + O2 | oxidized by MabB at a rate less than 1% of that observed for 5-aminosalicylate | Comamonas thiooxydans | (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate | - |
? | |
| 5-aminosalicylate + O2 | the enzyme plays an important physiological role in 3-aminobenzoate degradation in Comamonas sp. strain QT12 | Comamonas thiooxydans | (2Z,4E)-4-amino-6-oxohepta-2,4-dienedioate | - |
? | |
| 5-aminosalicylate + O2 | 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 | Comamonas thiooxydans | (2Z,4E)-4-amino-6-oxohepta-2,4-dienedioate | - |
? | |
| gentisate + O2 | 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 | Comamonas thiooxydans | maleylpyruvate | - |
? | |
| additional information | no activity is detected in reaction with salicylate | Comamonas thiooxydans | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 45000, SDS-PAGE | Comamonas thiooxydans |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| mabB | - |
Comamonas thiooxydans |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 10 | - |
- |
Comamonas thiooxydans |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 10 | 45 | 10°C: maximal activity, 45°C: about 60% of maximal activity | Comamonas thiooxydans |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | 8 | - |
Comamonas thiooxydans |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | 9 | pH 6.5: about 50% of maximal activity, pH 9.0: about 40% of maximal activity | Comamonas thiooxydans |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Comamonas thiooxydans | the enzyme is induced by 3-aminobenzoate or its degradation intermediates | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | the mabB-disrupted mutant loses the ability to grow on 3-aminobenzoate | Comamonas thiooxydans |
| metabolism | the enzyme plays an important physiological role in 3-aminobenzoate degradation in Comamonas sp. strain QT12 | Comamonas thiooxydans |
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