allophanate hydrolase

Identifiers
EC no.| 3.5.1.54
CAS no.| 79121-96-3
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KEGG| KEGG entry
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PDB structures| RCSB PDB PDBe PDBsum
Gene Ontology| AmiGO  / QuickGO
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In enzymology, an allophanate hydrolase (EC 3.5.1.54) is an enzyme that catalyzes the chemical reaction

allophanate + 3 H2O + H+ ⇌ {\displaystyle \rightleftharpoons } 2 HCO3− \+ 2 NH4+

Thus, the two substrates of this enzyme are allophanate (urea-1-carboxylate or N-carbamoylcarbamate) and H2O, whereas its two products are HCO3− and NH4+.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is urea-1-carboxylate amidohydrolase. This enzyme is also called allophanate lyase. This enzyme participates in urea cycle and metabolism of amino groups and atrazine degradation.

## See also

[edit]

* Urea carboxylase

## References

[edit]

* Maitz GS, Haas EM, Castric PA (1982). "Purification and properties of the allophanate hydrolase from Chlamydomonas reinhardii". Biochim. Biophys. Acta. 714 (3): 486–491\. doi:10.1016/0304-4165(82)90158-1.
* Roon RJ, Levenberg B (1972). "Urea amidolyase. I. Properties of the enzyme from Candida utilis". J. Biol. Chem. 247 (13): 4107–13\. doi:10.1016/S0021-9258(19)45046-1. PMID 4556303.
* Sumrada RA, Cooper TG (1982). "Urea carboxylase and allophanate hydrolase are components of a multifunctional protein in yeast". J. Biol. Chem. 257 (15): 9119–27\. doi:10.1016/S0021-9258(18)34251-0. PMID 6124544.
* Kanamori T, Kanou N, Kusakabe S, Atomi H, Imanaka T (2005). "Allophanate hydrolase of Oleomonas sagaranensis involved in an ATP-dependent degradation pathway specific to urea". FEMS Microbiol. Lett. 245 (1): 61–5\. doi:10.1016/j.femsle.2005.02.023. PMID 15796980.

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Hydrolases: carbon-nitrogen non-peptide (EC 3.5)

3.5.1: Linear amides /
Amidohydrolases|

* Asparaginase
* Glutaminase
* Urease
* Biotinidase
* Aminoacylase
* ACY1
* Aspartoacylase(ACY2)
* ACY3
* Ceramidase
* Aspartylglucosaminidase
* Fatty acid amide hydrolase
* Histone deacetylase
* Sirtuin

3.5.2: Cyclic amides/
Amidohydrolases|

* Barbiturase
* Beta-lactamase
* Dihydroorotase

3.5.3: Linear amidines/
Ureohydrolases|

* Arginase
* Agmatinase
* Protein-arginine deiminase

3.5.4: Cyclic amidines/
Aminohydrolases|

* Guanine deaminase
* Adenosine deaminase
* AMP deaminase
* Inosine monophosphate synthase
* DCMP deaminase
* GTP cyclohydrolase I
* Cytidine deaminase
* AICDA
* Activation-induced cytidine deaminase

3.5.5: Nitriles/
Aminohydrolases|

* Nitrilase

3.5.99: Other|

* Riboflavinase
* Thiaminase II

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Enzymes

Activity|

* Active site
* Binding site
* Catalytic triad
* Oxyanion hole
* Enzyme promiscuity
* Diffusion-limited enzyme
* Cofactor
* Enzyme catalysis

Regulation|

* Allosteric regulation
* Cooperativity
* Enzyme inhibitor
* Enzyme activator

Classification|

* EC number
* Enzyme superfamily
* Enzyme family
* List of enzymes

Kinetics|

* Enzyme kinetics
* Eadie–Hofstee diagram
* Hanes–Woolf plot
* Lineweaver–Burk plot
* Michaelis–Menten kinetics

Types|

* EC1 Oxidoreductases (list)
* EC2 Transferases (list)
* EC3 Hydrolases (list)
* EC4 Lyases (list)
* EC5 Isomerases (list)
* EC6 Ligases (list)
* EC7 Translocases (list)

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