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Literature summary 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

Protein Variants

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.2 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)

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

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.2 Bacillus subtilis
-
-
-

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
4.1.1.2 OXDC
-
Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.2 O2 required Bacillus subtilis

General Information

EC Number General Information Comment Organism
4.1.1.2 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