Application | Comment | Organism |
---|---|---|
drug development | cyanase is potentially an attractive protein target for the development of acaricides | Tetranychus urticae |
Cloned (Comment) | Organism |
---|---|
gene tetur28g02430, DNA and amino acid sequence determination and analysis, genomic and transcriptomic analysis, phylogenetic analysis, recombinant expression of MBP-tagged or N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3) | Tetranychus urticae |
Crystallization (Comment) | Organism |
---|---|
purified recombinant MBP-tagged enzyme, sitting drop vapor diffusion method, 13 mg/ml protein solution is mixed with crystallization solution, containing 0.1 M Tris, pH 7.5, 15% w/v PEG 6000, in a 1:1 ratio, about 2 months, room temperature, X-ray diffraction structure determination and analysis at 2.8 A resolution, molecular replacement using the crystal structure of Escherichia coli cyanase (PDB ID 2IV1) as the starting model | Tetranychus urticae |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
60000 | - |
recombinant monomeric His-tagged enzyme, gel filtration | Tetranychus urticae |
670000 | - |
recombinant decameric MBP-tagged enzyme, gel filtration | Tetranychus urticae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
cyanate + HCO3- + 2 H+ | Tetranychus urticae | - |
NH3 + 2 CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Tetranychus urticae | T1KZQ3 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration, recombinant MBP-tagged enzyme from Escherichia coli strain BL21(DE3) by affinity chromatography, dialysis in presence of 5 mm maltose, ultrafiltration, and gel filtration | Tetranychus urticae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
cyanate + HCO3- + 2 H+ | - |
Tetranychus urticae | NH3 + 2 CO2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodecamer | 10 * 60000, about, recombinant His-tagged enzyme, SDS-PAGE | Tetranychus urticae |
More | prokaryotic and eukaryotic cyanases all form homodecamers and have conserved active site residues, but display different surface areas between homodimers in the overall decameric structure. Monomer and dimer interfaces analysis, overview | Tetranychus urticae |
Synonyms | Comment | Organism |
---|---|---|
107368746 | - |
Tetranychus urticae |
tetur28g02430 | - |
Tetranychus urticae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Tetranychus urticae |
General Information | Comment | Organism |
---|---|---|
evolution | genomic and transcriptomic analysis, phyloegentic analysis, the cyanase gene originates from a single horizontal gene transfer event, which precedes subsequent speciation, comparison of prokaryotic cyanases to eukaryotic cyanase from Tetranychus urticae, which all form homodecamers and have conserved active site residues, but display different surface areas between homodimers in the overall decameric structure | Tetranychus urticae |
additional information | the enzyme binds specifically to DNA | Tetranychus urticae |
physiological function | cyanase catalyzes the detoxification of cyanate | Tetranychus urticae |