4.1.1.2: oxalate decarboxylase
This is an abbreviated version!
For detailed information about oxalate decarboxylase, go to the full flat file.
Word Map on EC 4.1.1.2
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4.1.1.2
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hyperoxaluria
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velutipes
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oxalate-degrading
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flammulina
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mniii
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mn-dependent
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bicupins
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collybia
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medicine
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agriculture
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paper production
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industry
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biotechnology
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degradation
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synthesis
- 4.1.1.2
- hyperoxaluria
- velutipes
-
oxalate-degrading
-
flammulina
-
mniii
-
mn-dependent
-
bicupins
-
collybia
- medicine
- agriculture
- paper production
- industry
- biotechnology
- degradation
- synthesis
Reaction
Synonyms
AnODC, AtuOXDC, Decarboxylase, oxalate, FvOXDC, More, ODC, ODC B, ODC C, ODC E, ODC F, odc2, oxalate carboxy-lyase, oxalate-decarboxylase, oxazyme, OXD, OXDC, OxDc-CLEC, OxDcase, OxdD, pBy, TOXDC, YoaN, YvrK
ECTree
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General Information
General Information on EC 4.1.1.2 - oxalate decarboxylase
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evolution
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oxalate decarboxylase belongs to the low-pH-inducible cupin superfamily of enzymes
physiological function
additional information
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enzyme expression in Glycine max and Lathyrus sativus improves seed quality and tolerance to the fungal pathogen Sclerotinia sclerotiorum
physiological function
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rats artificially colonized by recombinant Lactobacillus plantarum expressing and secreting heterologous oxalate decarboxylase show reduced urinary oxalate excretion therby preventing renal calcium oxalate stone deposition
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analysis of transport of the product, i.e., CO2, from the reaction center to the surface of the enzyme using atomistic molecular dynamics simulations. Structure-function analysis using protein crystal structure, PDB ID 1L3J, simulations, overview. Domain I is the active site domain, while domain II is nonreceptive to hosting the formate and is incapable of releasing the CO2 molecule
additional information
the conformational properties of an active-site loop segment, defined by residues Ser161-Glu162-Asn163-Ser164, are important for modulating the intrinsic reactivity of Mn(II) in the active site of Bacillus subtilis oxalate decarboxylase. O2 might participate as a reversible electron sink in two putative proton-coupled electron transfer steps and is not merely used to generate a protein-based radical or oxidized metal center. The conserved Arg/Thr hydrogen bond is important for correctly locating the side chain of Glu162, which mediates a proton-coupled electron transfer step prior to decarboxylation in the catalytically competent form of the enzyme
additional information
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the conformational properties of an active-site loop segment, defined by residues Ser161-Glu162-Asn163-Ser164, are important for modulating the intrinsic reactivity of Mn(II) in the active site of Bacillus subtilis oxalate decarboxylase. O2 might participate as a reversible electron sink in two putative proton-coupled electron transfer steps and is not merely used to generate a protein-based radical or oxidized metal center. The conserved Arg/Thr hydrogen bond is important for correctly locating the side chain of Glu162, which mediates a proton-coupled electron transfer step prior to decarboxylation in the catalytically competent form of the enzyme
additional information
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the enzyme is involved in resistance against oxalate- and Nep1-like protein-producing pathogens in plants. Oxalic acid and Nep1-like proteins are recognized as elicitors of programmed cell death in plants, which is crucial for the pathogenic success of necrotrophic plant pathogens and involves reactive oxygen species
additional information
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the conformational properties of an active-site loop segment, defined by residues Ser161-Glu162-Asn163-Ser164, are important for modulating the intrinsic reactivity of Mn(II) in the active site of Bacillus subtilis oxalate decarboxylase. O2 might participate as a reversible electron sink in two putative proton-coupled electron transfer steps and is not merely used to generate a protein-based radical or oxidized metal center. The conserved Arg/Thr hydrogen bond is important for correctly locating the side chain of Glu162, which mediates a proton-coupled electron transfer step prior to decarboxylation in the catalytically competent form of the enzyme
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