IPR003712
Cyanate lyase, C-terminal
InterPro entry
Short name | Cyanate_lyase_C |
Overlapping homologous superfamilies |
Description
Some bacteria can overcome the toxicity of environmental cyanate by hydrolysis of cyanate. This reaction is catalyzed by cyanate lyase (also known as cyanase)
[1]. Cyanate lyase is found in bacteria and plants and catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
The cyanate lyase monomer is composed of two domains. The N-terminal domain shows structural similarity to the DNA-binding α-helix bundle motif. The C-terminal domain has an 'open fold' with no structural homology to other proteins. The dimer structure reveals the C-terminal domains to be intertwined, and the decamer is formed by a pentamer of these dimers. The active site of the enzyme is located between dimers and is comprised of residues from four adjacent subunits of the homodecamer
[2].
References
1.Characterization of the cyn operon in Escherichia coli K12. Sung YC, Fuchs JA. J. Biol. Chem. 263, 14769-75, (1988). View articlePMID: 3049588
2.Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site. Walsh MA, Otwinowski Z, Perrakis A, Anderson PM, Joachimiak A. Structure 8, 505-14, (2000). View articlePMID: 10801492
GO terms
biological process
molecular function
- None
cellular component
- None
Cross References
ENZYME