ArticleBiochemistry2010
Biochemical and structural characterization of a ureidoglycine aminotransferase in the Klebsiella pneumoniae uric acid catabolic pathway.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- A high throughput assay for phosphoribosylformylglycinamidine synthase.SLAS discovery : advancing life sciences R & D · 2025Article
- The multi-drug efflux system AcrABZ-TolC is essential for infection ofJournal of virology · 2021Article
- Alternative conformation induced by substrate binding for Arabidopsis thalianaN6-methyl-AMP deaminase.Nucleic acids research · 2019Article
- Biochemical and structural characterization of Klebsiella pneumoniae oxamate amidohydrolase in the uric acid degradation pathway.Acta crystallographica. Section D, Structural biology · 2016Article
- Identifying reaction modules in metabolic pathways: bioinformatic deduction and experimental validation of a new putative route in purine catabolism.BMC systems biology · 2013Article
- The purinosome, a multi-protein complex involved in the de novo biosynthesis of purines in humans.Chemical communications (Cambridge, England) · 2013Article
- Structural and kinetic insights into the mechanism of 5-hydroxyisourate hydrolase from Klebsiella pneumoniae.Acta crystallographica. Section D, Biological crystallography · 2011Article
- An aminotransferase branch point connects purine catabolism to amino acid recycling.Nature chemical biology · 2010Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Many plants, fungi, and bacteria catabolize allantoin as a mechanism for nitrogen assimilation. Recent reports have shown that in plants and some bacteria the product of hydrolysis of allantoin by allantoinase is the unstable intermediate ureidoglycine. While this molecule can spontaneously decay, genetic analysis of some bacterial genomes indicates that an aminotransferase may be present in the pathway. Here we present evidence that Klebsiella pneumoniae HpxJ is an aminotransferase that preferentially converts ureidoglycine and an alpha-keto acid into oxalurate and the corresponding amino acid. We determined the crystal structure of HpxJ, allowing us to present an explanation for substrate specificity.
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