| Type: | Family | Name: | Cyanate hydratase |
| Description: | Cyanate hydratase or cyanase catalyses the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide, allowing the host organisms to overcome the toxicity of environmental cyanate []. 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 alpha-helix bundlemotif, and a C-terminal domain that has an 'open fold' that shows no structural similarity to other proteins [].The enzyme is active as a homodecamer of 17kDa subunits, and displays half-site binding of substrates or substrate analogues. The dimer structurereveals the C-terminal domains to be intertwined; the decamer is formed from a pentamer of these dimers. The active site of the enzyme is locatedbetween dimers and comprises residues from four adjacent subunits of the homodecamer. | Short Name: | Cyanase |
