EC 6.3.4.6 - Urea carboxylase

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IntEnz Enzyme Nomenclature
EC 6.3.4.6

Names

Accepted name:
urea carboxylase
Other names:
ATP—urea amidolyase
UALase
urea amidolyase
urea carboxylase (hydrolysing)
urease (ATP-hydrolysing)
UCA
Systematic name:
urea:carbon-dioxide ligase (ADP-forming)

Reaction

Cofactor

Comments:

A biotinyl-protein. The yeast enzyme (but not that from green algae) also catalyses the reaction of EC 3.5.1.54 allophanate hydrolase, thus bringing about the hydrolysis of urea to CO2 and NH3. Previously also listed as EC 3.5.1.45. The enzyme from the prokaryotic bacterium Oleomonas sagaranensis can also use acetamide and formamide as substrates [4].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00167 , PROSITE:PDOC00676 , PROSITE:PDOC50975 , PROSITE:PDOC50979
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004847
CAS Registry Number: 9058-98-4
UniProtKB/Swiss-Prot:

References

  1. Roon, R.J. and Levenberg, B.
    ATP-Urea amidolyase (ADP) (Candida utilis)
    Methods Enzymol. 17A: 317-324 (1970).
  2. Roon, R.J. and Levenberg, B.
    Urea amidolyase. I. Properties of the enzyme from Candida utilis.
    J. Biol. Chem. 247: 4107-4113 (1972). [PMID: 4556303]
  3. Sumrada, R.A. and Cooper, T.G.
    Urea carboxylase and allophanate hydrolase are components of a multifunctional protein in yeast.
    J. Biol. Chem. 257: 9119-9127 (1982). [PMID: 6124544]
  4. Kanamori, T., Kanou, N., Atomi, H. and Imanaka, T.
    Enzymatic characterization of a prokaryotic urea carboxylase.
    J. Bacteriol. 186: 2532-2539 (2004). [PMID: 15090492]

[EC 6.3.4.6 created 1972, modified 1986 (EC 3.5.1.45 created 1978, incorporated 1986)]