EC Number | Application | Comment | Organism |
---|---|---|---|
3.2.2.16 | drug development | the enzyme is a potential target for specific antibiotics | Helicobacter pylori |
EC Number | Cloned (Comment) | Organism |
---|---|---|
3.2.2.16 | expressed in Escherichia coli BL21(DE3) cells | Helicobacter pylori |
3.2.2.16 | gene mnqB, expression of recombinant His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) | Helicobacter pylori |
3.2.2.30 | expressed in Escherichia coli BL21(DE3) cells | Helicobacter pylori |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.2.2.16 | purified recombinant wild-type and mutant enzymes, sitting drop vapour diffusion method, mixing of 50 mg/ml protein in 10 mM Tris-HCl, pH 8.0, with 4.0 M NaH2PO4/K2HPO4, pH 7.0, using a 1:1 ratio of protein to mother liquor, X-ray diffraction structure determination and analysis at 1.65-2.11 A resolution, molecular replacement. for the mutant enzymess th following crystallization slutions are used: for E14Q 0.1 M HEPES, pH 7.5, 25% PEG 3350, 0.2 M NaCl, for D199N 0.1 M bis-Tris, pH 5.5, 25% PEG 3350, 0.2 M MgCl2 x 6H2O, and for D199A 0.1 M bis-Tris, pH 6.5, 25% PEG 3350, 0.2 M Li2SO4 xH2O | Helicobacter pylori |
3.2.2.16 | sitting drop vapor diffusion method, over 4.0 M NaH2PO4/K2HPO4 pH 7.0 | Helicobacter pylori |
3.2.2.30 | hanging drop vapor diffusion method, mutants E14Q (0.1 M HEPES pH 7.5, 25% (w/v) PEG 3350, 0.2 M NaCl), D199N (0.1 M bis-Tris pH 5.5, 25% (w/v) PEG 3350, 0.2 M MgCl2-6H2O) and D199A (0.1 M bis-tris pH 6.5, 25% (w/v) PEG 3350, 0.2 M Li2SO4-H2O) | Helicobacter pylori |
3.2.2.30 | wild type and mutant enzymes E14Q, D199N, and D199A, sitting drop vapor diffusion method, using 4.0 M NaH2PO4/K2HPO4 pH 7.0 (wild type), 0.1 M HEPES pH 7.5, 25% PEG 3350, 0.2 M NaCl (E14Q), 0.1 M bis-Tris pH 5.5, 25% (w/v) PEG 3350, 0.2 M MgCl2-6H2O (D199N), and 0.1 M bis-Tris pH 6.5, 25% (w/v) PEG 3350, 0.2 M Li2SO4-H2O (D199A) | Helicobacter pylori |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.2.2.16 | D199A | site-directed mutagenesis, structure determination and comparison to the wild-type enzyme | Helicobacter pylori |
3.2.2.16 | D199A | the enzyme shows minor activity towards 6-amino-6-deoxyfutalosine | Helicobacter pylori |
3.2.2.16 | D199N | inactive | Helicobacter pylori |
3.2.2.16 | D199N | site-directed mutagenesis, structure determination and comparison to the wild-type enzyme | Helicobacter pylori |
3.2.2.16 | E14A | inactive | Helicobacter pylori |
3.2.2.16 | E14Q | site-directed mutagenesis, structure determination and comparison to the wild-type enzyme | Helicobacter pylori |
3.2.2.16 | E14Q | the enzyme shows minor activity towards 6-amino-6-deoxyfutalosine | Helicobacter pylori |
3.2.2.30 | D199A | inactive | Helicobacter pylori |
3.2.2.30 | D199A | active-site mutant | Helicobacter pylori |
3.2.2.30 | D199N | active-site mutant | Helicobacter pylori |
3.2.2.30 | D199N | the mutant shows residual activity | Helicobacter pylori |
3.2.2.30 | E14Q | active-site mutant | Helicobacter pylori |
3.2.2.30 | E14Q | the mutant shows residual activity | Helicobacter pylori |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.2.16 | 5'-methylthioadenosine + H2O | Helicobacter pylori | - |
adenine + S-methyl-5-thio-D-ribose | - |
? | |
3.2.2.16 | 6-amino-6-deoxyfutalosine + H2O | Helicobacter pylori | - |
3-{3-[(2R,3S,4R,5R)-3,4,5-trihydroxytetrahydrofuran-2-yl]propanoyl}benzoic acid + 9H-purine-6-amine | - |
? | |
3.2.2.16 | S-methyl-5'-thioadenosine + H2O | Helicobacter pylori | - |
S-methyl-5-thio-D-ribose + adenine | - |
? | |
3.2.2.30 | 6-amino-6-deoxyfutalosine + H2O | Helicobacter pylori | - |
dehypoxanthine futalosine + adenine | - |
? | |
3.2.2.30 | 6-amino-6-deoxyfutalosine + H2O | Helicobacter pylori | - |
adenine + dehypoxanthinyl futalosine | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.2.16 | Helicobacter pylori | O24915 | - |
- |
3.2.2.16 | Helicobacter pylori | O24915 | gene mnqB | - |
3.2.2.26 | no activity in Helicobacter pylori strain 26695 | - |
- |
- |
3.2.2.30 | Helicobacter pylori | O24915 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.2.2.16 | HisTrap column chromatography and Superdex 75 gel filtration | Helicobacter pylori |
3.2.2.16 | recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and gel filtration | Helicobacter pylori |
3.2.2.30 | HisTrap column chromatography | Helicobacter pylori |
3.2.2.30 | HisTrap column chromatography and Superdex 75 gel filtration | Helicobacter pylori |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.2.2.16 | S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine | structure-function analysis and reaction mechanism, overview. The proposed mechanism of action for the hydrolysis of methylthioadenosine by the enzyme involves the essential acidic residue in the lid of the active site and a water molecule that acts as a nucleophile which is activated by an arginine and a glutamic acid residue | Helicobacter pylori |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.2.16 | 5'-methylthioadenosine + H2O | - |
Helicobacter pylori | adenine + S-methyl-5-thio-D-ribose | - |
? | |
3.2.2.16 | 6-amino-6-deoxyfutalosine + H2O | - |
Helicobacter pylori | 3-{3-[(2R,3S,4R,5R)-3,4,5-trihydroxytetrahydrofuran-2-yl]propanoyl}benzoic acid + 9H-purine-6-amine | - |
? | |
3.2.2.16 | 6-amino-6-deoxyfutalosine + H2O | - |
Helicobacter pylori | adenine + dehypoxanthinyl futalosine | - |
? | |
3.2.2.16 | additional information | broad substrate specificity | Helicobacter pylori | ? | - |
? | |
3.2.2.16 | S-methyl-5'-thioadenosine + H2O | - |
Helicobacter pylori | S-methyl-5-thio-D-ribose + adenine | - |
? | |
3.2.2.30 | 6-amino-6-deoxyfutalosine + H2O | - |
Helicobacter pylori | dehypoxanthine futalosine + adenine | - |
? | |
3.2.2.30 | 6-amino-6-deoxyfutalosine + H2O | - |
Helicobacter pylori | adenine + dehypoxanthinyl futalosine | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.2.2.16 | homodimer | x-ray crystallography | Helicobacter pylori |
3.2.2.30 | homodimer | x-ray crystallography | Helicobacter pylori |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.2.16 | 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase | - |
Helicobacter pylori |
3.2.2.16 | 50-methylthioadenosine/S-adenosylhomocysteine nucleosidase | - |
Helicobacter pylori |
3.2.2.16 | HpyMqnB | - |
Helicobacter pylori |
3.2.2.16 | methylthioadenosine nucleosidase | - |
Helicobacter pylori |
3.2.2.16 | MqnB | - |
Helicobacter pylori |
3.2.2.16 | MTAN | - |
Helicobacter pylori |
3.2.2.30 | methylthioadenosine nucleosidase | - |
Helicobacter pylori |
3.2.2.30 | MqnB | - |
Helicobacter pylori |
3.2.2.30 | MTAN | - |
Helicobacter pylori |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.2.2.16 | metabolism | the enzyme is involved in the second step of the futalosine pathway, which is crucial for the biosynthesis of the essential prokaryotic respiratory compound menaquinone, which is a key molecule in the bacterial respiratory pathway and a lipid-soluble electron carrier known in eukaryotes as vitamin K2, overview | Helicobacter pylori |
3.2.2.16 | additional information | active site structure involving E14 and D199, overview | Helicobacter pylori |