ArticleActa crystallographica. Section D, Biological crystallography2011
Structural and kinetic insights into the mechanism of 5-hydroxyisourate hydrolase from Klebsiella pneumoniae.
Article in Acta crystallographica. Section D, Biological crystallography, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 14 citations in OpenAlex.
- Sacha Inchi Oil Press-Cake Protein Hydrolysates Exhibit Anti-Hyperuricemic Activity via Attenuating Renal Damage and Regulating Gut Microbiota.Foods (Basel, Switzerland) · 2022Article
- Theoretical Studies on the Binding Mode and Reaction Mechanism of TLP HydrolaseMolecules (Basel, Switzerland) · 2021Article
- Ethanol Adaptation Strategies in Salmonella enterica Serovar Enteritidis Revealed by Global Proteomic and Mutagenic Analyses.Applied and environmental microbiology · 2019Article
- Genetic characterization of caffeine degradation by bacteria and its potential applications.Microbial biotechnology · 2015Review
- Tweaking the structure to radically change the function: the evolution of transthyretin from 5-hydroxyisourate hydrolase to triiodothyronine distributor to thyroxine distributor.Frontiers in endocrinology · 2014Review
- Delineation of the caffeine C-8 oxidation pathway in Pseudomonas sp. strain CBB1 via characterization of a new trimethyluric acid monooxygenase and genes involved in trimethyluric acid metabolism.Journal of bacteriology · 2012Article
- The structure of Serratia marcescens Lip, a membrane-bound component of the type VI secretion system.Acta crystallographica. Section D, Biological crystallography · 2011Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
The stereospecific oxidative degradation of uric acid to (S)-allantoin has recently been demonstrated to proceed via two unstable intermediates and requires three separate enzymatic reactions. The second step of this reaction, the conversion of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline, is catalyzed by HIU hydrolase (HIUH). The high-resolution crystal structure of HIUH from the opportunistic pathogen Klebsiella pneumoniae (KpHIUH) has been determined. KpHIUH is a homotetrameric protein that, based on sequence and structural similarity, belongs to the transthyretin-related protein family. In addition, the steady-state kinetic parameters for this enzyme and four active-site mutants have been measured. These data provide valuable insight into the functional roles of the active-site residues. Based upon the structural and kinetic data, a mechanism is proposed for the KpHIUH-catalyzed reaction.
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