ArticleJournal of bacteriology2000
Functional expression and characterization of the two cyclic amidohydrolase enzymes, allantoinase and a novel phenylhydantoinase, from Escherichia coli.
Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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23 citing papers in PubMed, 52 citations in OpenAlex.
- Secretory Expression ofJournal of microbiology and biotechnology · 2025Article
- Dual Regulation of theJournal of microbiology and biotechnology · 2025Article
- Gut bacteria degrade purines via the 2,8-dioxopurine pathway.Nature microbiology · 2025Article
- Oxamic transcarbamylase ofApplied and environmental microbiology · 2024Article
- Anti-Biofilm Activity of Chlorogenic Acid againstFoods (Basel, Switzerland) · 2023Article
- Crystal Structure of Allantoinase from Escherichia coli BL21: A Molecular Insight into a Role of the Active Site Loops in CatalysisMolecules (Basel, Switzerland) · 2023Article
- Expression and Characterization of Monomeric Recombinant Isocitrate Dehydrogenases fromInternational journal of molecular sciences · 2022Article
- Article
- Rational Engineering of the Substrate Specificity of a Thermostable D-Hydantoinase (Dihydropyrimidinase).High-throughput · 2020Article
- Metagenomic binning of a marine sponge microbiome reveals unity in defense but metabolic specialization.The ISME journal · 2017Article
- Functional Characterization of a Novel Member of the Amidohydrolase 2 Protein Family, 2-Hydroxy-1-Naphthoic Acid Nonoxidative Decarboxylase from Burkholderia sp. Strain BC1.Journal of bacteriology · 2016Article
- Cloning, expression, purification, crystallization and preliminary X-ray characterization of allantoinase from Bacillus licheniformis ATCC 14580.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Identifying reaction modules in metabolic pathways: bioinformatic deduction and experimental validation of a new putative route in purine catabolism.BMC systems biology · 2013Article
- Evolution of cyclic amidohydrolases: a highly diversified superfamily.Journal of molecular evolution · 2013Article
- Novel amidases of two Aminobacter sp. strains: Biotransformation experiments and elucidation of gene sequences.AMB Express · 2012Article
- Biochemical characterization of allantoinase from Escherichia coli BL21.The protein journal · 2011Article
- Escherichia coli dihydropyrimidine dehydrogenase is a novel NAD-dependent heterotetramer essential for the production of 5,6-dihydrouracil.Journal of bacteriology · 2011Article
- Crystallization and preliminary crystallographic studies of the recombinant dihydropyrimidinase from Sinorhizobium meliloti CECT4114.Acta crystallographica. Section F, Structural biology and crystallization communications · 2006Article
- A novel data mining method to identify assay-specific signatures in functional genomic studies.BMC bioinformatics · 2006Article
- Functional characterization of allantoinase genes from Arabidopsis and a nonureide-type legume black locust.Plant physiology · 2004Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A superfamily of cyclic amidohydrolases, including dihydropyrimidinase, allantoinase, hydantoinase, and dihydroorotase, all of which are involved in the metabolism of purine and pyrimidine rings, was recently proposed based on the rigidly conserved structural domains in identical positions of the related enzymes. With these conserved domains, two putative cyclic amidohydrolase genes from Escherichia coli, flanked by related genes, were identified and characterized. From the genome sequence of E. coli, the allB gene and a putative open reading frame, tentatively designated as a hyuA (for hydantoin-utilizing enzyme) gene, were predicted to express hydrolases. In contrast to allB, high-level expression of hyuA in E. coli of a single protein was unsuccessful even under various induction conditions. We expressed HyuA as a maltose binding protein fusion protein and AllB in its native form and then purified each of them by conventional procedures. allB was found to encode a tetrameric allantoinase (453 amino acids) which specifically hydrolyzes the purine metabolite allantoin to allantoic acid. Another open reading frame, hyuA, located near 64.4 min on the physical map and known as a UUG start, coded for D-stereospecific phenylhydantoinase (465 amino acids) which is a homotetramer. As a novel enzyme belonging to a cyclic amidohydrolase superfamily, E. coli phenylhydantoinase exhibited a distinct activity toward the hydantoin derivative with an aromatic side chain at the 5' position but did not readily hydrolyze the simple cyclic ureides. The deduced amino acid sequence of the novel phenylhydantoinase shared a significant homology (>45%) with those of allantoinase and dihydropyrimidinase, but its functional role still remains to be elucidated. Despite the unclear physiological function of HyuA, its presence, along with the allantoin-utilizing AllB, strongly suggested that the cyclic ureides might be utilized as nutrient sources in E. coli.
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