EC Number | Cloned (Comment) | Organism |
---|---|---|
3.5.4.23 | bsd overexpressed in Escherichia coli BL 21 | Aspergillus terreus |
3.5.4.23 | overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli BL21(DE3), Cys91 mutants are expressed in inclusion bodies | Aspergillus terreus |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.5.4.23 | - |
Aspergillus terreus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.5.4.23 | C91A | site-directed mutagenesis, inactive mutant, gross perturbation of the enzyme structure | Aspergillus terreus |
3.5.4.23 | C91H | site-directed mutagenesis, inactive mutant, gross perturbation of the enzyme structure | Aspergillus terreus |
3.5.4.23 | C91S | site-directed mutagenesis, inactive mutant, gross perturbation of the enzyme structure | Aspergillus terreus |
3.5.4.23 | E56D | site-directed mutagenesis, inactive mutant | Aspergillus terreus |
3.5.4.23 | E56Q | site-directed mutagenesis, inactive mutant | Aspergillus terreus |
EC Number | General Stability | Organism |
---|---|---|
3.5.4.23 | the tetrameric enzyme form is very resistant against denaturation by SDS, 90% remaining activity at 2% SDS, diluted 10fold and incubated 2 h at room temperature | Aspergillus terreus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.5.4.23 | additional information | no inhibition by EDTA and o-phenanthroline | Aspergillus terreus | |
3.5.4.23 | p-Hydroxymercuriphenylsulfonic acid | leads to destabilization of the enzyme structure due to removal of required zinc | Aspergillus terreus |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.5.4.23 | Zn2+ | tightly bound catalytic zinc, 1 zinc ion per subunit, enzyme contains the catalytic zinc-coordinating sequence motif, role in enzyme tetrameric structure stabilization and protein folding, overview | Aspergillus terreus |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.5.4.23 | 13000 | - |
SDS-PAGE, heat treatment | Aspergillus terreus |
3.5.4.23 | 13340 | - |
recombinant enzyme, calculated by amino acid residues per subunit | Aspergillus terreus |
3.5.4.23 | 36000 | - |
SDS-PAGE without heat treatment | Aspergillus terreus |
3.5.4.23 | 49000 | - |
native PAGE | Aspergillus terreus |
3.5.4.23 | 49000 | - |
recombinant wild-type enzyme, native PAGE | Aspergillus terreus |
3.5.4.23 | 52000 | - |
ultracentrifugal sedimentation analysis | Aspergillus terreus |
3.5.4.23 | 54000 | - |
gel filtration | Aspergillus terreus |
3.5.4.23 | 54000 | - |
recombinant and native wild-type enzyme, gel filtration | Aspergillus terreus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.4.23 | blasticidin S + H2O | Bacillus cereus | - |
deaminohydroxyblasticidin S + NH3 | - |
? | |
3.5.4.23 | blasticidin S + H2O | Aspergillus terreus | - |
deaminohydroxyblasticidin S + NH3 | - |
? |
EC Number | Organic Solvent | Comment | Organism |
---|---|---|---|
3.5.4.23 | SDS | quite resistant to denaturation | Aspergillus terreus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.4.23 | Aspergillus terreus | - |
- |
- |
3.5.4.23 | Bacillus cereus | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.5.4.23 | - |
Aspergillus terreus |
3.5.4.23 | native enzyme from Aspergiluus terreus, recombinant His-tagged enzyme from Escherichia coli by nickel chelate affinity chromatography | Aspergillus terreus |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.5.4.23 | blasticidin S + H2O = deaminohydroxyblasticidin S + NH3 | catalyses the deamination of the cytosine moiety of the antibiotics blasticidin S, cytomycin and acetylblasticidin S, Glu56 is required for catalysis, and Cys91 is required for structural maintenance | Aspergillus terreus |
EC Number | Renatured (Comment) | Organism |
---|---|---|
3.5.4.23 | reconstitution of the enzyme after denaturation with guanidine-HCl, acid, or p-hydroxymercuriphenylsulfonic acid, using different divalent metal ions, renaturation of the enzyme is completely blocked in presence of 1 mM EDTA, refolding of recombinant Cys91 mutant enzymes from inclusion bodies | Aspergillus terreus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.4.23 | blasticidin S + H2O | - |
Bacillus cereus | deaminohydroxyblasticidin S + NH3 | - |
? | |
3.5.4.23 | blasticidin S + H2O | - |
Aspergillus terreus | deaminohydroxyblasticidin S + NH3 | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.5.4.23 | More | zinc has a role in enzyme tetrameric structure stabilization and protein folding | Aspergillus terreus |
3.5.4.23 | tetramer | 4 * 13000, SDS-PAGE | Aspergillus terreus |
3.5.4.23 | tetramer | 4 * 13000, SDS-PAGE containing 15% SDS | Aspergillus terreus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.5.4.23 | blasticidin S deaminase | - |
Aspergillus terreus |
3.5.4.23 | BSD | - |
Aspergillus terreus |