| EC |
3.5.3.9 |
| Accepted name: |
allantoate deiminase |
| Reaction: |
allantoate + H2O = (S)-ureidoglycine + NH3 + CO2 |
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For diagram of AMP catabolism, click here |
| Other name(s): |
allantoate amidohydrolase |
| Systematic name: |
allantoate amidinohydrolase (decarboxylating) |
| Comments: |
This enzyme is part of the ureide pathway, which permits certain organisms to recycle the nitrogen in purine compounds. This enzyme, which liberates ammonia from allantoate, is present in plants and bacteria. In plants it is localized in the endoplasmic reticulum. Requires manganese. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37289-13-7 |
| References: |
| 1. |
Vogels, G.D. Reversible activation of allantoate amidohydrolase by acid-pretreatment and other properties of the enzyme. Biochim. Biophys. Acta 113 (1966) 277–291. [PMID: 5328936] |
| 2. |
Serventi, F., Ramazzina, I., Lamberto, I., Puggioni, V., Gatti, R. and Percudani, R. Chemical basis of nitrogen recovery through the ureide pathway: formation and hydrolysis of S-ureidoglycine in plants and bacteria. ACS Chem. Biol. 5 (2010) 203–214. [DOI] [PMID: 20038185] |
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| [EC 3.5.3.9 created 1972, modified 2010] |
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