EC |
2.6.1.112 |
Accepted name: |
(S)-ureidoglycine—glyoxylate transaminase |
Reaction: |
(S)-ureidoglycine + glyoxylate = N-carbamoyl-2-oxoglycine + glycine |
Glossary: |
(S)-ureidoglycine = (2S)-(carbamoylamino)glycine |
Other name(s): |
(S)-ureidoglycine—glyoxylate aminotransferase; UGXT; PucG |
Systematic name: |
(S)-ureidoglycine:glyoxylate aminotransferase |
Comments: |
A pyridoxal 5′-phosphate protein. The protein, found in bacteria, can use other amino-group acceptors, but is specific for (S)-ureidoglycine. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Ramazzina, I., Costa, R., Cendron, L., Berni, R., Peracchi, A., Zanotti, G. and Percudani, R. An aminotransferase branch point connects purine catabolism to amino acid recycling. Nat. Chem. Biol. 6 (2010) 801–806. [DOI] [PMID: 20852637] |
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[EC 2.6.1.112 created 2017] |
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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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EC |
3.5.3.26 |
Accepted name: |
(S)-ureidoglycine aminohydrolase |
Reaction: |
(S)-2-ureidoglycine + H2O = (S)-ureidoglycolate + NH3 |
Other name(s): |
UGlyAH; UGHY; ylbA (gene name) |
Systematic name: |
(S)-ureidoglycine aminohydrolase |
Comments: |
Binds Mn2+. This enzyme, found in plants and bacteria, is part of the ureide pathway, which enables the recycling of the nitrogen in purine compounds. In plants it is localized in the endoplasmic reticulum. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
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] |
2. |
Werner, A.K., Romeis, T. and Witte, C.P. Ureide catabolism in Arabidopsis thaliana and Escherichia coli. Nat. Chem. Biol. 6 (2010) 19–21. [DOI] [PMID: 19935661] |
3. |
Shin, I., Percudani, R. and Rhee, S. Structural and functional insights into (S)-ureidoglycine aminohydrolase, key enzyme of purine catabolism in Arabidopsis thaliana. J. Biol. Chem. 287 (2012) 18796–18805. [DOI] [PMID: 22493446] |
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[EC 3.5.3.26 created 2013] |
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