Activating Compound | Comment | Organism | Structure |
---|---|---|---|
ADP | the presence of 0.3 mM ADP results in a marginal increase in kcat and a small decrease in Km, leading to a 1.7fold higher catalytic efficiency. One molecule of ADP is bound per monomer distant from the CoA binding site | Escherichia coli | |
AMP | weak activating effect | Escherichia coli | |
ATP | weak activating effect | Escherichia coli |
Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli BL21 cells | Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
ODC alone or in complex with either ADP or acetyl CoA, hanging drop vapor diffusion method, using 100 mM MES/NaOH, pH 6.5 and 1.5 M ammonium sulfate for ODC alone, or 100 mM MES/NaOH, pH 6.25 and 1.75 M ammonium sulfate for ADPbound ODC, or 100 mM MES/NaOH, pH 6.0, 0.2 M sodium acetate and 5% (w/v) poly(ethylene glycol) 4000 for acetyl CoA-bound ODC | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
acetyl coenzyme A | - |
Escherichia coli | |
coenzyme A | - |
Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0048 | - |
oxalyl-CoA | at pH 6.5 and 30°C | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | contains Mg2+ | Escherichia coli |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
60581 | - |
4 * 60581, calculated from amino acid sequence | Escherichia coli |
230000 | - |
small-angle X-ray solution scattering | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0AFI0 | - |
- |
Purification (Comment) | Organism |
---|---|
streptomycin sulfate precipitation, ammonium sulfate precipitation, Q-Sepharose column chromatography, and Superdex 200 gel filtration | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Oxalyl-CoA | - |
Escherichia coli | Formyl-CoA + CO2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
homotetramer | 4 * 60581, calculated from amino acid sequence | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
ODC | - |
Escherichia coli |
oxalyl CoA decarboxylase | - |
Escherichia coli |
yfdU | - |
Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
60.7 | - |
oxalyl-CoA | at pH 6.5 and 30°C | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.5 | 7 | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
thiamine diphosphate | dependent on | Escherichia coli |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.08 | - |
coenzyme A | at pH 6.5 and 30°C | Escherichia coli |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
12.6 | - |
oxalyl-CoA | at pH 6.5 and 30°C | Escherichia coli |