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Literature summary for 4.1.1.8 extracted from

  • Berthold, C.L.; Moussatche, P.; Richards, N.G.; Lindqvist, Y.
    Structural basis for activation of the thiamin diphosphate-dependent enzyme oxalyl-CoA decarboxylase by adenosine diphosphate (2005), J. Biol. Chem., 280, 41645-41654.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
ADP stimulates Oxalobacter formigenes

Crystallization (Commentary)

Crystallization (Comment) Organism
recombinant, hanging-drop vapour-diffusion method Oxalobacter formigenes

Inhibitors

Inhibitors Comment Organism Structure
CoA mixed inhibitor with respect to oxalyl-CoA Oxalobacter formigenes

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.023
-
oxalyl-CoA pH 6.7, 30°C Oxalobacter formigenes

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
243000
-
gel filtration Oxalobacter formigenes

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Oxalyl-CoA Oxalobacter formigenes essential step in ATP generation Formyl-CoA + CO2
-
?

Organism

Organism UniProt Comment Textmining
Oxalobacter formigenes
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant Oxalobacter formigenes

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Oxalyl-CoA
-
Oxalobacter formigenes Formyl-CoA + CO2
-
?
Oxalyl-CoA essential step in ATP generation Oxalobacter formigenes Formyl-CoA + CO2
-
?

Subunits

Subunits Comment Organism
tetramer
-
Oxalobacter formigenes

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
88
-
oxalyl-CoA pH 6.7, 30°C Oxalobacter formigenes

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.4
-
CoA pH 6.7, 30°C Oxalobacter formigenes