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Literature summary for 3.5.4.23 extracted from
- Expression, purification, and characterization of blasticidin S deaminase (BSD) from Aspergillus terreus: The role of catalytic zinc in enzyme structure (2000), J. Biochem., 127, 955-963.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| bsd overexpressed in Escherichia coli BL 21 | Aspergillus terreus |
| overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli BL21(DE3), Cys91 mutants are expressed in inclusion bodies | Aspergillus terreus |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
- |
Aspergillus terreus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C91A | site-directed mutagenesis, inactive mutant, gross perturbation of the enzyme structure | Aspergillus terreus |
| C91H | site-directed mutagenesis, inactive mutant, gross perturbation of the enzyme structure | Aspergillus terreus |
| C91S | site-directed mutagenesis, inactive mutant, gross perturbation of the enzyme structure | Aspergillus terreus |
| E56D | site-directed mutagenesis, inactive mutant | Aspergillus terreus |
| E56Q | site-directed mutagenesis, inactive mutant | Aspergillus terreus |
General Stability
| General Stability | Organism |
|---|---|
| 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 |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | no inhibition by EDTA and o-phenanthroline | Aspergillus terreus | |
| p-Hydroxymercuriphenylsulfonic acid | leads to destabilization of the enzyme structure due to removal of required zinc | Aspergillus terreus |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| 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 | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 13000 | - |
SDS-PAGE, heat treatment | Aspergillus terreus |
| 13340 | - |
recombinant enzyme, calculated by amino acid residues per subunit | Aspergillus terreus |
| 36000 | - |
SDS-PAGE without heat treatment | Aspergillus terreus |
| 49000 | - |
native PAGE | Aspergillus terreus |
| 49000 | - |
recombinant wild-type enzyme, native PAGE | Aspergillus terreus |
| 52000 | - |
ultracentrifugal sedimentation analysis | Aspergillus terreus |
| 54000 | - |
gel filtration | Aspergillus terreus |
| 54000 | - |
recombinant and native wild-type enzyme, gel filtration | Aspergillus terreus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| blasticidin S + H2O | Bacillus cereus | - |
deaminohydroxyblasticidin S + NH3 | - |
? | |
| blasticidin S + H2O | Aspergillus terreus | - |
deaminohydroxyblasticidin S + NH3 | - |
? | |
Organic Solvent Stability
| Organic Solvent | Comment | Organism |
|---|---|---|
| SDS | quite resistant to denaturation | Aspergillus terreus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus terreus | - |
- |
- |
| Bacillus cereus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Aspergillus terreus |
| native enzyme from Aspergiluus terreus, recombinant His-tagged enzyme from Escherichia coli by nickel chelate affinity chromatography | Aspergillus terreus |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 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 |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| 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 |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| blasticidin S + H2O | - |
Bacillus cereus | deaminohydroxyblasticidin S + NH3 | - |
? | |
| blasticidin S + H2O | - |
Aspergillus terreus | deaminohydroxyblasticidin S + NH3 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | zinc has a role in enzyme tetrameric structure stabilization and protein folding | Aspergillus terreus |
| tetramer | 4 * 13000, SDS-PAGE | Aspergillus terreus |
| tetramer | 4 * 13000, SDS-PAGE containing 15% SDS | Aspergillus terreus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| blasticidin S deaminase | - |
Aspergillus terreus |
| BSD | - |
Aspergillus terreus |
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