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Lan-Xin Tang1,2,3, Zheng-Feng Yang1,2,3, Yun-Shu Yang1,2,4

  • 1College of Agriculture and Biological Science, Dali University, Dali, 671003, People's Republic of China.

AMB Express
|January 4, 2026
PubMed

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Summary
This summary is machine-generated.

A novel uricase (tc1-uox2) from hot springs shows high activity and thermal stability, effectively lowering uric acid in hyperuricemia patients. This enzyme offers a promising biotherapeutic target for metabolic diseases.

Area of Science:

  • Biochemistry
  • Enzymology
  • Metabolic Engineering

Background:

  • Uricase is crucial for purine metabolism and used in treating hyperuricemia.
  • Existing uricases often lack sufficient thermal stability for therapeutic applications.

Purpose of the Study:

  • To discover and characterize a novel uricase with enhanced activity and thermal stability.
  • To investigate the structural basis for the enzyme's stability.

Main Methods:

  • Cloning and heterologous expression of the tc1-uox2 gene.
  • Enzymatic characterization (activity, pH, temperature stability).
  • In vitro uric acid-lowering assays and comparative molecular dynamics simulations.

Main Results:

Keywords:
MetagenomicsMolecular dynamics simulationTengchong hot springsUrate-lowering therapyUricase

Related Experiment Videos

  • TC1-Uox2 demonstrated optimal activity at 35°C and pH 8.0.
  • Exceptional thermal stability: >40% activity after 16h at 40°C, >80% at 37°C for 14h.
  • Effective in vitro reduction of serum uric acid in hyperuricemic patient samples.
  • Molecular dynamics simulations revealed TC1-Uox2's compact structure and enhanced thermodynamic stability.

    • Conclusions:

    • TC1-Uox2 is a highly active and thermostable uricase.
    • Its structural properties underpin its enhanced stability.
    • Represents a promising candidate for hyperuricemia biotherapeutics and highlights metagenomics potential.