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Literature summary for 4.1.1.2 extracted from

  • Karmakar, T.; Periyasamy, G.; Balasubramanian, S.
    CO2 migration pathways in oxalate decarboxylase and clues about its active site (2013), J. Phys. Chem. B, 117, 12451-12460.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
additional information mutation of Glu 333 present in domain II leads to a reduction in the activity of the enzyme Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ the enzyme has two domains, each containing a Mn(II) ion coordinated with three histidine residues, binding structure in domain I, overview Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
oxalate + H+ Bacillus subtilis
-
 formate + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oxalate + H+
-
 Bacillus subtilis formate + CO2
-
 ?

Synonyms

Synonyms Comment Organism
OXDC
-
 Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
O2 required Bacillus subtilis

General Information

General Information Comment Organism
additional information 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 Bacillus subtilis