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Literature summary for 4.1.1.8 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

Inhibitors Comment Organism Structure
EDTA
-
Oxalobacter formigenes

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activates Oxalobacter formigenes

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Oxalobacter formigenes
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Oxalobacter formigenes

Substrates and Products (Substrate)

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

Subunits

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

pH Optimum

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

Cofactor

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