ArticleIranian journal of biotechnology2020
Enhancement of Pharmaceutical Urate Oxidase Thermostability by Rational Design of
Article in Iranian journal of biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 6 citations in OpenAlex.
- Article
- Stability and functional consequences of disulfide bond engineering in Aspergillus flavus uricase.Scientific reports · 2025Article
- The role of Gln269Leu mutation on the thermostability and structure of uricase from Aspergillus flavus.Scientific reports · 2025Article
- High yield expression and purification of3 Biotech · 2023Article
- The effects of free Cys residues on the structure, activity, and tetrameric stability of mammalian uricase.Applied microbiology and biotechnology · 2023Article
- Rasburicase-Induced Falsely Low Measurement of Uric Acid in Tumor Lysis Syndrome: A Report of Two Cases.Cureus · 2023Article
Corrections and comments
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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
background and purposeAs a therapeutic enzyme, urate oxidase is utilized in the reduction of uric acid in various conditions such as gout or tumor syndrome lysis. However, even bearing kinetical advantage over other counterparts, it suffers from structural instability most likely due to its subcellular and fungal origin.
objectivesIn this research, by using rational design and introduction of MATERIALS AND
methodsUtilizing site-directed mutagenesis and only with one point mutation we constructed two separate mutants: Ala6Cys and Ser282Cys which covalently linked subunits of enzyme each other. Single mutation to cysteine created three inter-chain disulfide bridges and one hydrogen bond in Ala6Cys and two disulfide bridges in Ser282Cys.
resultsBoth mutants showed 10 °C increase in optimum activity compared to wild-type enzyme while the
conclusionIt seemed that introducing disulfide bridges resulted in local and overall rigidity by bringing two adjacent sites of enzyme together and decreasing the conformational entropy of unfolding state is responsible for the enhancement of thermostability.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.