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Literature summary 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

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.1.1.8 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
4.1.1.8 AMP weak activating effect Escherichia coli
4.1.1.8 ATP weak activating effect Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.8 expressed in Escherichia coli BL21 cells Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.8 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

EC Number Inhibitors Comment Organism Structure
4.1.1.8 acetyl coenzyme A
-
 Escherichia coli
4.1.1.8 coenzyme A
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.8 0.0048
-
 oxalyl-CoA at pH 6.5 and 30°C Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.8 Mg2+ contains Mg2+ Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.8 60581
-
 4 * 60581, calculated from amino acid sequence Escherichia coli
4.1.1.8 230000
-
 small-angle X-ray solution scattering Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.8 Escherichia coli P0AFI0
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
4.1.1.8 ODC
-
 Escherichia coli
4.1.1.8 oxalyl CoA decarboxylase
-
 Escherichia coli
4.1.1.8 yfdU
-
 Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.8 60.7
-
 oxalyl-CoA at pH 6.5 and 30°C Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.8 5.5 7
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.8 thiamine diphosphate dependent on Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.1.1.8 0.08
-
 coenzyme A at pH 6.5 and 30°C Escherichia coli

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.1.1.8 12.6
-
 oxalyl-CoA at pH 6.5 and 30°C Escherichia coli