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

BRENDA support

Literature summary extracted from

  • Baetz, A.L.; Allison, M.J.
    Purification and characterization of oxalyl-coenzyme A decarboxylase from Oxalobacter formigenes (1989), J. Bacteriol., 171, 2605-2608.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.8 EDTA
-
 Oxalobacter formigenes

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.8 0.24
-
 oxalyl-CoA
-
 Oxalobacter formigenes

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.8 Mg2+ activates Oxalobacter formigenes

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.8 65000
-
 4 * 65000, SDS-PAGE Oxalobacter formigenes
4.1.1.8 260000
-
 PAGE Oxalobacter formigenes

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.8 Oxalobacter formigenes
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.8
-
 Oxalobacter formigenes

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.8 Oxalyl-CoA
-
 Oxalobacter formigenes Formyl-CoA + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.8 tetramer 4 * 65000, SDS-PAGE Oxalobacter formigenes

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.8 6.7
-
 oxalyl-CoA Oxalobacter formigenes

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.8 thiamine diphosphate Km: 1.1 picomol Oxalobacter formigenes