F
IPR008076

Cyanate hydratase

InterPro entry
Short nameCyanase
Overlapping
homologous
superfamilies
 

Description

Cyanate hydratase or cyanase lyase catalyses the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide, allowing the host organisms to overcome the toxicity of environmental cyanate
[1]
. The enzyme is also known as cyanate lyase and cyanate hydrolase.

The cyanate lyase monomer is composed of two domains: an N-terminal domain that shows structural similarity to the DNA-binding α-helix bundle motif, and a C-terminal domain that has an 'open fold' that shows no structural similarity to other proteins
[1]
.

The enzyme is active as a homodecamer of 17kDa subunits, and displays half-site binding of substrates or substrate analogues. The dimer structure reveals the C-terminal domains to be intertwined; the decamer is formed from a pentamer of these dimers. The active site of the enzyme is located between dimers and comprises residues from four adjacent subunits of the homodecamer.

References

1.Structural properties of cyanase. Denaturation, renaturation, and role of sulfhydryls and oligomeric structure in catalytic activity. Little RM, Anderson PM. J. Biol. Chem. 262, 10120-6, (1987). View articlePMID: 3301828

GO terms

cellular component

  • None

Cross References

Contributing Member Database Entries
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