EC 4.2.1.104 - Cyanase

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IntEnz Enzyme Nomenclature
EC 4.2.1.104

Names

Accepted name:
cyanase
Other names:
cyanate hydratase
cyanate aminohydrolase
cyanate hydrolase
cyanate lyase
cyanate C-N-lyase
Systematic name:
carbamate hydro-lyase

Reactions

Comments:

This enzyme, which is found in bacteria and plants, is used to decompose cyanate, which can be used as the sole source of nitrogen [6,7]. Reaction (1) can be considered as the reverse of 'carbamate = cyanate + H2O', where this is assisted by reaction with bicarbonate and carbon dioxide (see mechanism above) [2], and hence is classified in sub-subclass 4.2.1. Bicarbonate functions as a recycling substrate [2].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008824
CAS Registry Number: 37289-24-0
UniProtKB/Swiss-Prot: (124) [show] [UniProt]

References

  1. Anderson, P.M.
    Purification and properties of the inducible enzyme cyanase.
    Biochemistry 19: 2882-2888 (1980). [PMID: 6994799]
  2. Johnson, W.V. and Anderson, P.M.
    Bicarbonate is a recycling substrate for cyanase.
    J. Biol. Chem. 262: 9021-9025 (1987). [PMID: 3110153]
  3. Taussig, A.
    The synthesis of the induced enzyme, "cyanase", in E. coli.
    Biochim. Biophys. Acta 44: 510-519 (1960). [PMID: 13775509]
  4. Taussig, A.
    Some properties of the induced enzyme cyanase.
    Can. J. Biochem. 43: 1063-1069 (1965). [PMID: 5322950]
  5. Anderson, P.M., Korte, J.J. and Holcomb, T.A.
    Reaction of the N-terminal methionine residues in cyanase with diethylpyrocarbonate.
    Biochemistry 33: 14121-14125 (1994). [PMID: 7947823]
  6. Kozliak, E.I., Fuchs, J.A., Guilloton, M.B. and Anderson, P.M.
    Role of bicarbonate/CO2 in the inhibition of Escherichia coli growth by cyanate.
    J. Bacteriol. 177: 3213-3219 (1995). [PMID: 7768821]
  7. Walsh, M.A., Otwinowski, Z., Perrakis, A., Anderson, P.M. and Joachimiak, A.
    Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site.
    Structure 8: 505-514 (2000). [PMID: 10801492]

[EC 4.2.1.104 created 1972 as EC 3.5.5.3, transferred 1990 to EC 4.3.99.1, transferred 2001 to EC 4.2.1.104, modified 2007]