IPR008076
Cyanate hydratase
InterPro entry
Short name | Cyanase |
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
biological process
molecular function
cellular component
- None
Cross References
ENZYME
Genome Properties
Contributing Member Database Entries
- PANTHER:PTHR34186
- PRINTS:PR01693
- HAMAP:MF_00535
- NCBIfam:TIGR00673
- PIRSF:PIRSF001263
Representative structure
8k6h: Crystal structure of e.coli cyanase complex with cyanate