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Literature summary for 4.1.1.8 extracted from

  • Werther, T.; Zimmer, A.; Wille, G.; Golbik, R.; Weiss, M.S.; Koenig, S.
    New insights into structure-function relationships of oxalyl CoA decarboxylase from Escherichia coli (2010), FEBS J., 277, 2628-2640.
    View publication on PubMed
Search for more literature for 4.1.1.8

Activating Compound

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(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 cells Escherichia coli

Crystallization (Commentary)

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 ADP–bound 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

Inhibitors Comment Organism Structure
acetyl coenzyme A
-
 Escherichia coli
coenzyme A
-
 Escherichia coli

KM Value [mM]

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

Metals/Ions Comment Organism Structure
Mg2+ contains Mg2+ Escherichia coli

Molecular Weight [Da]

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

Organism UniProt Comment Textmining
Escherichia coli P0AFI0
-
-

Purification (Commentary)

Purification (Comment) Organism
streptomycin sulfate precipitation, ammonium sulfate precipitation, Q-Sepharose column chromatography, and Superdex 200 gel filtration Escherichia coli

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
homotetramer 4 * 60581, calculated from amino acid sequence Escherichia coli

Synonyms

Synonyms Comment Organism
ODC
-
 Escherichia coli
oxalyl CoA decarboxylase
-
 Escherichia coli
yfdU
-
 Escherichia coli

Turnover Number [1/s]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5 7
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate dependent on Escherichia coli

Ki Value [mM]

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 [mM/s]

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