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Literature summary extracted from

  • Schlachter, C.R.; Klapper, V.; Wybouw, N.; Radford, T.; Van Leeuwen, T.; Grbic, M.; Chruszcz, M.
    Structural characterization of a eukaryotic cyanase from Tetranychus urticae (2017), J. Agric. Food Chem., 65, 5453-5462 .
    View publication on PubMed

Application

EC Number Application Comment Organism
4.2.1.104 drug development cyanase is potentially an attractive protein target for the development of acaricides Tetranychus urticae

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.104 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 (Commentary)

EC Number Crystallization (Comment) Organism
4.2.1.104 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.1.104 60000
-
 recombinant monomeric His-tagged enzyme, gel filtration Tetranychus urticae
4.2.1.104 670000
-
 recombinant decameric MBP-tagged enzyme, gel filtration Tetranychus urticae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.104 cyanate + HCO3- + 2 H+ Tetranychus urticae
-
 NH3 + 2 CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.104 Tetranychus urticae T1KZQ3
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.104 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 and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.104 cyanate + HCO3- + 2 H+
-
 Tetranychus urticae NH3 + 2 CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.104 homodecamer 10 * 60000, about, recombinant His-tagged enzyme, SDS-PAGE Tetranychus urticae
4.2.1.104 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

EC Number Synonyms Comment Organism
4.2.1.104 107368746
-
 Tetranychus urticae
4.2.1.104 tetur28g02430
-
 Tetranychus urticae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.104 7.5
-
 assay at Tetranychus urticae

General Information

EC Number General Information Comment Organism
4.2.1.104 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
4.2.1.104 additional information the enzyme binds specifically to DNA Tetranychus urticae
4.2.1.104 physiological function cyanase catalyzes the detoxification of cyanate Tetranychus urticae