Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Angerhofer, A.; Moomaw, E.W.; Garcia-Rubio, I.; Ozarowski, A.; Krzystek, J.; Weber, R.T.; Richards, N.G.
    Multifrequency EPR studies on the Mn(II) centers of oxalate decarboxylase (2007), J. Phys. Chem. B, 111, 5043-5046.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.2 Mn2+ the enzyme is composed of two cupin domains, each of which contains a Mn2+ ion coordinated by four identical conserved residues, multifrequency EPR studies on the Mn2+ centers of oxalate decarboxylase, 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 Bacillus subtilis
-
 Formate + CO2
-
 ?

Organism

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

Reaction

EC Number Reaction Comment Organism Reaction ID
4.1.1.2 oxalate = formate + CO2 catalytic mechanism Bacillus subtilis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.2 Oxalate
-
 Bacillus subtilis Formate + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.2 More the enzyme is composed of two cupin domains, each of which contains a Mn2+ ion coordinated by four identical conserved residues Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
4.1.1.2 OXDC
-
 Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.2 4
-
-
 Bacillus subtilis