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Literature summary for 4.2.1.104 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

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Inhibitors Comment Organism Structure
chloride
-
Escherichia coli
oxalate
-
Escherichia coli

Molecular Weight [Da]

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

Organism

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

Reaction

Reaction Comment Organism Reaction ID
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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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