Structural landscape of bacterial urease: implications for catalyst and adaptation.

Λεπτομέρειες βιβλιογραφικής εγγραφής
Τίτλος: Structural landscape of bacterial urease: implications for catalyst and adaptation.
Συγγραφείς: Putri ANH; Research Center for Genetic Engineering, National Research and Innovation Agency (BRIN), Bogor, Indonesia.; Department of Biochemistry, Faculty of Mathematics and Natural Science, IPB University, Bogor, Indonesia., Islami RH; Research Center for Genetic Engineering, National Research and Innovation Agency (BRIN), Bogor, Indonesia.; School of Life Sciences and Technology, Bandung Institute of Technology, Bandung, Indonesia., Andrianto D; Department of Biochemistry, Faculty of Mathematics and Natural Science, IPB University, Bogor, Indonesia. dimasandrianto@apps.ipb.ac.id., Pratama R; Department of Biochemistry, Faculty of Mathematics and Natural Science, IPB University, Bogor, Indonesia., Pangestu R; Research Center for Genetic Engineering, National Research and Innovation Agency (BRIN), Bogor, Indonesia. radityo.pangestu@brin.go.id.
Πηγή: Archives of microbiology [Arch Microbiol] 2026 Feb 23; Vol. 208 (5). Date of Electronic Publication: 2026 Feb 23.
Τύπος έκδοσης: Journal Article; Review
Γλώσσα: English
Στοιχεία περιοδικού: Publisher: Springer-Verlag Country of Publication: Germany NLM ID: 0410427 Publication Model: Electronic Cited Medium: Internet ISSN: 1432-072X (Electronic) Linking ISSN: 03028933 NLM ISO Abbreviation: Arch Microbiol Subsets: MEDLINE
Imprint Name(s): Original Publication: Berlin, New York, Springer-Verlag.
Ιατρικοί όροι (MeSH): Urease*/chemistry , Urease*/metabolism , Urease*/genetics , Bacteria*/enzymology , Bacteria*/genetics , Bacteria*/chemistry , Bacterial Proteins*/chemistry , Bacterial Proteins*/metabolism , Bacterial Proteins*/genetics, Nickel/metabolism ; Catalytic Domain ; Protein Conformation ; Catalysis ; Models, Molecular ; Adaptation, Physiological ; Hydrogen-Ion Concentration
Περίληψη: Bacterial ureases are unique enzymes full of paradoxes. They catalyze a simple hydrolysis reaction yet embody an architectural marvel of quaternary organization, comprising multiple subunits and requiring complex accessory systems for maturation. This review scrutinizes ureases from a structural perspective, exploring the diversity of their oligomeric assemblies in pathogenic and soil bacteria, the detailed coordination chemistry of the nickel-containing active site, and the conformational dynamics of other catalytic elements. Furthermore, it explains the structural changes that occur in response to environmental factors, including pH, temperature, and inhibitors. The analysis also encompasses genetic regulation and the design of expression systems for biotechnological applications. Knowledge of urease structural biology will guide future efforts to redesign this enzyme for specific purposes across diverse scientific contexts.
Competing Interests: Declarations. Competing interests: The authors declare no competing interests.
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Contributed Indexing: Keywords: Bacterial enzyme; Environmental adaptation; Structural biology; Urease
Substance Nomenclature: EC 3.5.1.5 (Urease)
0 (Bacterial Proteins)
7OV03QG267 (Nickel)
Entry Date(s): Date Created: 20260222 Date Completed: 20260627 Latest Revision: 20260627
Update Code: 20260627
DOI: 10.1007/s00203-026-04767-z
PMID: 41724831
Βάση Δεδομένων: MEDLINE