| Entry |
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| Name |
urea carboxylase;
urease (ATP-hydrolysing);
urea carboxylase (hydrolysing);
ATP---urea amidolyase;
urea amidolyase;
UALase;
UCA
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| Class |
Ligases;
Forming carbon-nitrogen bonds;
Other carbon-nitrogen ligases
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| Sysname |
urea:carbon-dioxide ligase (ADP-forming)
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| Reaction(IUBMB) |
ATP + urea + HCO3- = ADP + phosphate + urea-1-carboxylate [RN: R00774]
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| Reaction(KEGG) |
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| Substrate |
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| Product |
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| Comment |
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].
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| History |
EC 6.3.4.6 created 1972, modified 1986 (EC 3.5.1.45 created 1978, incorporated 1986)
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| Pathway |
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| Orthology |
| K14541 | urea carboxylase / allophanate hydrolase |
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| Genes |
» show all
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| Reference |
1 |
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| Authors |
Roon, R.J. and Levenberg, B. |
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| Title |
ATP-Urea amidolyase (ADP) (Candida utilis). |
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| Journal |
Methods Enzymol 17A:317-324 (1970) |
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| Reference |
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| Authors |
Roon RJ, Levenberg B. |
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| Title |
Urea amidolyase. I. Properties of the enzyme from Candida utilis. |
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| Journal |
J Biol Chem 247:4107-13 (1972) |
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| Reference |
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| Authors |
Sumrada RA, Cooper TG. |
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| Title |
Urea carboxylase and allophanate hydrolase are components of a multifunctional protein in yeast. |
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| Journal |
J Biol Chem 257:9119-27 (1982) |
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| Reference |
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| Authors |
Kanamori T, Kanou N, Atomi H, Imanaka T. |
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| Title |
Enzymatic characterization of a prokaryotic urea carboxylase. |
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| Journal |
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| Sequence |
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| Other DBs |
| ExplorEnz - The Enzyme Database: | 6.3.4.6 |
| ExPASy - ENZYME nomenclature database: | 6.3.4.6 |
| BRENDA, the Enzyme Database: | 6.3.4.6 |
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