Molecular characterization and <i>in silico</i> analysis of oxalate decarboxylase of <i>Pseudomonas</i> sp. OXDC12

Gupta, Sushmita; Kanwar, Shamsher S.

doi:10.1080/07391102.2021.2024882

Cited by 4 publications

(2 citation statements)

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“…11 Oxalate decarboxylase activity has also been reported in bacteria Bacillus subtilis and Pseudomonas sp., and in guinea pig liver. 12,13 Gene mining based on the NCBI protein database also found some oxalate decarboxylase genes in archaea, but their biochemical properties have never been studied.…”

Section: Introductionmentioning

confidence: 99%

“…Since the first discovery of oxalate decarboxylase in the mycelia of the white rot fungi Coriolus hirsutus ( Trametes hirsuta ) and Collyvia veltipes ( Flammulina velutipes ), − the enzyme has been identified in many species of filamentous fungi such as Aspergillus niger , Myrothecium verrucaria , Trametes ochracea , and Agaricus bisporus . Oxalate decarboxylase activity has also been reported in bacteria Bacillus subtilis and Pseudomonas sp., and in guinea pig liver. , Gene mining based on the NCBI protein database also found some oxalate decarboxylase genes in archaea, but their biochemical properties have never been studied.…”

Section: Introductionmentioning

confidence: 99%

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Recent Advances of Oxalate Decarboxylase: Biochemical Characteristics, Catalysis Mechanisms, and Gene Expression and Regulation

Zan,

Yan,

Chen

et al. 2024

J. Agric. Food Chem.

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Oxalate decarboxylase (OXDC) is a typical Mn 2+ /Mn 3+ dependent metal enzyme and splits oxalate to formate and CO 2 without any organic cofactors. Fungi and bacteria are the main organisms expressing the OXDC gene, but with a significantly different mechanism of gene expression and regulation. Many articles reported its potential applications in the clinical treatment of hyperoxaluria, low-oxalate food processing, degradation of oxalate salt deposits, oxalate acid diagnostics, biocontrol, biodemulsifier, and electrochemical oxidation. However, some questions still remain to be clarified about the role of substrate binding and/or protein environment in modulating the redox properties of enzyme-bound Mn(II)/Mn(III), the nature of dioxygen involved in the catalytic mechanism, and how OXDC acquires Mn(II) /Mn(III). This review mainly summarizes its biochemical and structure characteristics, gene expression and regulation, and catalysis mechanism. We also deep-mined oxalate decarboxylase gene data from National Center for Biotechnology Information to give some insights to explore new OXDC with diverse biochemical properties.

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Section: Introductionmentioning

confidence: 99%