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Literature summary extracted from

  • Walsh, M.A.; Otwinowski, Z.; Perrakis, A.; Anderson, P.M.; Joachimiak, A.
    Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site (2000), Structure, 8, 505-514.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.2.1.104 bicarbonate
-
 Escherichia coli
4.2.1.104 Cyanate extracellular, enzyme induction Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.1.104 selenomethionine-labeled purified recombinant enzyme, also crystals of enzyme with complexed inhibitors oxalate and chloride, 2 mM dithiothreitol, sitting drop vapour diffusion method, from 2.1 M ammonium sulfate, 50 mM Na2KPO4, pH 7.3, microseeding with large sitting drops at 18°C with wild-type crystals, 5-7 days, X-ray diffraction structure determinzation and analysis at 1.65 A resolution by multiwavelength anomalous diffraction MAD method Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.104 chloride
-
 Escherichia coli
4.2.1.104 oxalate
-
 Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.1.104 17000
-
 10 * 17000, SDS-PAGE Escherichia coli
4.2.1.104 170000
-
 crystal structure Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.104 Escherichia coli
-
 gene of cyn operon, inducible enzyme
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.1.104 cyanate + HCO3- + 2 H+ = NH3 + 2 CO2 the enzyme requires bicarbonate as a cofactor. Its mechanism is to catalyse the attack of bicarbonate on cyanate, with elimination of carbon dioxide, thus catalysing hydration of the cyanate to carbamae. The carbamate spontaneously hydrolyses to ammonia and carbon dioxide, the decamer shows half-side binding of substrates and substrate analogues, catalytic mechanism, catalytic site involves Arg96, Glu99, and Ser122 Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.104 NCO- + HCO3-
-
 Escherichia coli NH4+ + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.104 decamer 10 * 17000, SDS-PAGE Escherichia coli
4.2.1.104 More the monomers are composed of 2 domains, subunit arrangement, decamer is formed by 5 dimers assembled into a pentamer, model Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
4.2.1.104 cyanase
-
 Escherichia coli
4.2.1.104 EC 4.3.99.1 formerly Escherichia coli