Reaction: urea-1-carboxylate + H2O = 2 CO2 + 2 NH3
Glossary: allophanate = urea-1-carboxylate
Other name(s): allophanate lyase; AtzF; TrzF
Systematic name: urea-1-carboxylate amidohydrolase
Comments: Along with EC 126.96.36.199 (cyanuric acid amidohydrolase) and EC 188.8.131.52 (biuret amidohydrolase), this enzyme forms part of the cyanuric-acid metabolism pathway, which degrades s-triazide herbicides, such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine], in bacteria. The yeast enzyme (but not that from green algae) also catalyses the reaction of EC 184.108.40.206, urea carboxylase, thus bringing about the hydrolysis of urea to CO2 and NH3 in the presence of ATP and bicarbonate. The enzyme from Pseudomonas sp. strain ADP has a narrow substrate specificity, being unable to use the structurally analogous compounds urea, hydroxyurea or methylcarbamate as substrate .
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 79121-96-3
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2. Roon, R.J. and Levenberg, B. Urea amidolyase. I. Properties of the enzyme from Candida utilis. J. Biol. Chem. 247 (1972) 4107-4113. [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 (1982) 9119-9127. [PMID: 6124544]
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6. Shapir, N., Sadowsky, M.J. and Wackett, L.P. Purification and characterization of allophanate hydrolase (AtzF) from Pseudomonas sp. strain ADP. J. Bacteriol. 187 (2005) 3731-3738. [PMID: 15901697]
7. Shapir, N., Cheng, G., Sadowsky, M.J. and Wackett, L.P. Purification and characterization of TrzF: biuret hydrolysis by allophanate hydrolase supports growth. Appl. Environ. Microbiol. 72 (2006) 2491-2495. [PMID: 16597948]