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Recent Advances of Oxalate Decarboxylase: Biochemical Characteristics, Catalysis Mechanisms, and Gene Expression and Regulation.
- Source :
-
Journal of agricultural and food chemistry [J Agric Food Chem] 2024 May 08; Vol. 72 (18), pp. 10163-10178. Date of Electronic Publication: 2024 Apr 23. - Publication Year :
- 2024
-
Abstract
- Oxalate decarboxylase (OXDC) is a typical Mn <superscript>2+</superscript> /Mn <superscript>3+</superscript> dependent metal enzyme and splits oxalate to formate and CO <subscript>2</subscript> 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.
- Subjects :
- Fungi genetics
Fungi enzymology
Fungal Proteins genetics
Fungal Proteins metabolism
Fungal Proteins chemistry
Biocatalysis
Oxalates metabolism
Oxalates chemistry
Bacterial Proteins genetics
Bacterial Proteins metabolism
Bacterial Proteins chemistry
Gene Expression Regulation, Enzymologic
Humans
Catalysis
Animals
Carboxy-Lyases genetics
Carboxy-Lyases metabolism
Carboxy-Lyases chemistry
Bacteria genetics
Bacteria enzymology
Bacteria metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1520-5118
- Volume :
- 72
- Issue :
- 18
- Database :
- MEDLINE
- Journal :
- Journal of agricultural and food chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 38653191
- Full Text :
- https://doi.org/10.1021/acs.jafc.4c00172