EC Number | Cloned (Comment) | Organism |
---|---|---|
2.1.1.72 | expressed in Escherichia coli ER2566 cells | Moraxella bovis |
2.1.1.113 | gene mboIIR, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli using the constitutive promoter, PtetA | Moraxella bovis |
2.1.1.113 | gene ncuIM2, DNA and amino acid sequence determination and analysis, expression in Escherichia coli | Moraxella cuniculi |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.1.1.72 | Mg2+ | Mg2+ inhibits methylation activity | Moraxella bovis | |
2.1.1.113 | Ca2+ | - |
Moraxella bovis | |
2.1.1.113 | Ca2+ | slight inhibition | Moraxella cuniculi | |
2.1.1.113 | Mg2+ | - |
Moraxella bovis | |
2.1.1.113 | Mg2+ | slight inhibition | Moraxella cuniculi | |
2.1.1.113 | Mn2+ | - |
Moraxella bovis | |
2.1.1.113 | Mn2+ | strong inhibition | Moraxella cuniculi | |
2.1.1.113 | Zn2+ | - |
Moraxella bovis | |
2.1.1.113 | Zn2+ | strong inhibition | Moraxella cuniculi |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.1.1.113 | 30000 | - |
1 * 30000, about, recombinant enzyme, 1 * 32676, sequence calculation | Moraxella cuniculi |
2.1.1.113 | 30000 | - |
1 * 30000, about, recombinant enzyme, SDS-PAGE, 1 * 32111, sequence calculation | Moraxella bovis |
2.1.1.113 | 32111 | - |
1 * 30000, about, recombinant enzyme, SDS-PAGE, 1 * 32111, sequence calculation | Moraxella bovis |
2.1.1.113 | 32676 | - |
1 * 30000, about, recombinant enzyme, 1 * 32676, sequence calculation | Moraxella cuniculi |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.1.72 | additional information | Moraxella bovis | no detectable activity on the single-stranded form of the phage PhiX174 DNA is observed with M1.MboII, double-stranded DNA is less efficiently methylated than pUC18 DNA | ? | - |
? | |
2.1.1.72 | S-adenosyl-L-methionine + DNA adenine | Moraxella bovis | M1.MboII modifies the last adenine in the recognition sequence 5'-GAAGA-3' to N6-methyladenine | S-adenosyl-L-homocysteine + DNA 6-methyladenine | - |
? | |
2.1.1.113 | S-adenosyl-L-methionine + [DNA]-cytosine | Moraxella bovis | - |
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine | - |
? | |
2.1.1.113 | S-adenosyl-L-methionine + [DNA]-cytosine | Moraxella cuniculi | - |
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.1.1.72 | Moraxella bovis | - |
strain ATCC 10900 | - |
2.1.1.113 | Moraxella bovis | - |
strain ATCC 10900, gene mboIIR | - |
2.1.1.113 | Moraxella cuniculi | - |
strain ATCC 14688, gene ncuIM2 | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.1.1.72 | partial purification using phosphocellulose column chromatography, hydroxylapatite column chromatography, CM-Sephadex gel filtration, and heparin agarose column chromatography | Moraxella bovis |
2.1.1.113 | recombinant M2.MboII 3.6fold to electrophoretic homogeneity using a four-step chromatographic procedure, involving adsorption and hydroxylapatite chromatography followed by hydroophobic interaction and heparin affinity chromatography, from Escherichia coli | Moraxella bovis |
2.1.1.113 | recombinant M2.NcuI 3.6fold to electrophoretic homogeneity using a four-step chromatographic procedure, involving adsorption and hydroxylapatite chromatography followed by hydrophobic interaction and heparin affinity chromatography, from Escherichia coli | Moraxella cuniculi |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.1.1.113 | 3200 | - |
purified recombinant enzyme | Moraxella bovis |
2.1.1.113 | 3200 | - |
purified recombinant enzyme | Moraxella cuniculi |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.1.72 | additional information | no detectable activity on the single-stranded form of the phage PhiX174 DNA is observed with M1.MboII, double-stranded DNA is less efficiently methylated than pUC18 DNA | Moraxella bovis | ? | - |
? | |
2.1.1.72 | S-adenosyl-L-methionine + DNA adenine | M1.MboII modifies the last adenine in the recognition sequence 5'-GAAGA-3' to N6-methyladenine | Moraxella bovis | S-adenosyl-L-homocysteine + DNA 6-methyladenine | - |
? | |
2.1.1.113 | S-adenosyl-L-methionine + [DNA]-cytosine | - |
Moraxella bovis | S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine | - |
? | |
2.1.1.113 | S-adenosyl-L-methionine + [DNA]-cytosine | - |
Moraxella cuniculi | S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine | - |
? | |
2.1.1.113 | S-adenosyl-L-methionine + [DNA]-cytosine | substrate is pNH20 plasmid DNA. M2.MboII modifies the internal cytosine in the recognition sequence 39-CTTCT-59, yielding N4-methylcytosine, and moreover is able to methylate double- and single-stranded DNA, single-stranded DNA is preferred. Determination and analysis of the methylation pattern of M2.MboII, overview | Moraxella bovis | S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine | - |
? | |
2.1.1.113 | S-adenosyl-L-methionine + [DNA]-cytosine | substrate is pNH20 plasmid DNA. M2.NcuI modifies the internal cytosine in the recognition sequence yielding N4-methylcytosine, and moreover is able to methylate double- and single-stranded DNA, single-stranded DNA is preferred. Determination of the methylation position, overview | Moraxella cuniculi | S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.1.1.113 | monomer | 1 * 30000, about, recombinant enzyme, 1 * 32676, sequence calculation | Moraxella cuniculi |
2.1.1.113 | monomer | 1 * 30000, about, recombinant enzyme, SDS-PAGE, 1 * 32111, sequence calculation | Moraxella bovis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.1.1.72 | adenine N6-methyltransferase | - |
Moraxella bovis |
2.1.1.72 | M1.MboII | a type IIS methyltransferase | Moraxella bovis |
2.1.1.113 | M2.MboII | - |
Moraxella bovis |
2.1.1.113 | M2.NcuI | - |
Moraxella cuniculi |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.1.1.113 | 37 | - |
assay at | Moraxella bovis |
2.1.1.113 | 37 | - |
assay at | Moraxella cuniculi |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.1.1.113 | 7 | 8 | - |
Moraxella bovis |
2.1.1.113 | 7 | - |
assay at | Moraxella cuniculi |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.1.1.113 | S-adenosyl-L-methionine | - |
Moraxella bovis | |
2.1.1.113 | S-adenosyl-L-methionine | - |
Moraxella cuniculi |
EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|---|
2.1.1.113 | 0.4 | - |
pH 7.0, 37°C, recombinant enzyme | Moraxella bovis | Mn2+ | |
2.1.1.113 | 0.4 | - |
pH 7.0, 37°C, recombinant enzyme | Moraxella bovis | Zn2+ | |
2.1.1.113 | 4 | - |
pH 7.0, 37°C, recombinant enzyme | Moraxella bovis | Ca2+ | |
2.1.1.113 | 5 | - |
pH 7.0, 37°C, recombinant enzyme | Moraxella bovis | Mg2+ |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.1.1.113 | metabolism | the enzyme is part of the MboII restriction-modification, R-M, system of Moraxella bovis strain ATCC 10900 consisting of a restriction endonuclease gene and two methyltransferase genes | Moraxella bovis |
2.1.1.113 | metabolism | the enzyme is part of the Ncul restriction-modification, R-M, system consisting of a restriction endonuclease gene and two methyltransferase genes | Moraxella cuniculi |