If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Locations of Mapped Genes:
|Superclasses:||Degradation/Utilization/Assimilation → Amines and Polyamines Degradation → Allantoin Degradation|
(S)-(+)-allantoin is a common product of purine degradation. Escherichia coli K-12 substr. MG1655 is able to utilize (S)-(+)-allantoin as a sole source of nitrogen under anaerobic conditions, but can not utilize it as a sole source of carbon [Cusa99].
The first step in allantoin degradation is the opening of the aromatic ring, yielding allantoate, performed by allantoinase. In the next step allantoate is hydrolyzed to S-ureidoglycine by allantoate amidohydrolase. While the second hydrolysis step (from S-ureidoglycine to S-ureidoglycolate) can happen spontaneously in a non-stereospecific manner, it is stereospecifically catalyzed by S-ureidoglycine aminohydrolase.
ureidoglycolate dehydrogenase then oxidizes ureidoglycolate to oxalurate. While not proven unequivocally in E. coli, it is believed oxalurate is converted into oxamate and carbamoyl-phosphate, which can be further metabolized to CO2, ammonia and ATP [Cusa99].
The variant pathway allantoin degradation to glyoxylate III shows a possible alternative route of allantoin degradation, where the ureidoglycolate intermediate is processed differently. The enzyme ureidoglycolate lyase can convert ureidoglycolate to glyoxylate and urea; glyoxylate could then enter general metabolism, where it would be converted by the successive action of three enzymes to 3-phosphoglycerate, feeding into glycolysis I (from glucose-6P) (see glycolate and glyoxylate degradation I). However, this route would imply that allantoin can serve as a sole source of carbon in E. coli, which it can not. Additionally, ureidoglycolate lyase is poorly characterized.
Variants: allantoin degradation to glyoxylate III
Created 28-Feb-2000 by Pellegrini-Toole A , Marine Biological Laboratory
Revised 22-Aug-2007 by Keseler I , SRI International
Revised 06-Nov-2007 by Caspi R , SRI International
Revised 21-Mar-2008 by Keseler I , SRI International
Revised 04-Jan-2010 by Keseler I , SRI International
Last-Curated 21-Mar-2008 by Keseler I , SRI International
Cusa99: Cusa E, Obradors N, Baldoma L, Badia J, Aguilar J (1999). "Genetic analysis of a chromosomal region containing genes required for assimilation of allantoin nitrogen and linked glyoxylate metabolism in Escherichia coli." J Bacteriol 1999;181(24);7479-84. PMID: 10601204
Agarwal07: Agarwal R, Burley SK, Swaminathan S (2007). "Structural analysis of a ternary complex of allantoate amidohydrolase from Escherichia coli reveals its mechanics." J Mol Biol 368(2);450-63. PMID: 17362992
DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114
Kim00c: Kim GJ, Lee DE, Kim HS (2000). "Functional expression and characterization of the two cyclic amidohydrolase enzymes, allantoinase and a novel phenylhydantoinase, from Escherichia coli." J Bacteriol 2000;182(24);7021-8. PMID: 11092864
Kim12a: Kim MI, Shin I, Cho S, Lee J, Rhee S (2012). "Structural and functional insights into (s)-ureidoglycolate dehydrogenase, a metabolic branch point enzyme in nitrogen utilization." PLoS One 7(12);e52066. PMID: 23284870
ParadisBleau14: Paradis-Bleau C, Kritikos G, Orlova K, Typas A, Bernhardt TG (2014). "A genome-wide screen for bacterial envelope biogenesis mutants identifies a novel factor involved in cell wall precursor metabolism." PLoS Genet 10(1);e1004056. PMID: 24391520
Puggioni14: Puggioni V, Dondi A, Folli C, Shin I, Rhee S, Percudani R (2014). "Gene context analysis reveals functional divergence between hypothetically equivalent enzymes of the purine-ureide pathway." Biochemistry 53(4);735-45. PMID: 24417435
Serventi10: Serventi F, Ramazzina I, Lamberto I, Puggioni V, Gatti R, Percudani R (2010). "Chemical basis of nitrogen recovery through the ureide pathway: formation and hydrolysis of S-ureidoglycine in plants and bacteria." ACS Chem Biol 5(2);203-14. PMID: 20038185
Shin14: Shin I, Han K, Rhee S (2014). "Structural Insights into the Substrate Specificity of (S)-Ureidoglycolate Amidohydrolase and Its Comparison with Allantoate Amidohydrolase." J Mol Biol. PMID: 25020232
Smith12: Smith AA, Belda E, Viari A, Medigue C, Vallenet D (2012). "The CanOE Strategy: Integrating Genomic and Metabolic Contexts across Multiple Prokaryote Genomes to Find Candidate Genes for Orphan Enzymes." PLoS Comput Biol 8(5);e1002540. PMID: 22693442
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