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Literature summary extracted from

  • Berthold, C.L.; Toyota, C.G.; Moussatche, P.; Wood, M.D.; Leeper, F.; Richards, N.G.; Lindqvist, Y.
    Crystallographic snapshots of oxalyl-CoA decarboxylase give insights into catalysis by nonoxidative ThDP-dependent decarboxylases (2007), Structure, 15, 853-861.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.8 expressed in Escherichia coli Oxalobacter formigenes

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.8 cocrystallization of wild-type OXC with 1 mM CoA, with a precipitating solution containing 0.5 M CaCl2, 0.1 M BisTris propane (2-[bis(2-hydroxyethyl)amino]-2-(hydroxymethyl) propane-1,3-diol), pH 6.5, and 26% polyethylene glycol 550 monomethyl ether Oxalobacter formigenes

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.8 E121A 0.1% activity compared to the wild type enzyme Oxalobacter formigenes
4.1.1.8 E121Q 3.8% activity compared to the wild type enzyme Oxalobacter formigenes
4.1.1.8 E56A no activity, mutant elutes with a retention time corresponding to that of a dimer Oxalobacter formigenes
4.1.1.8 additional information deletion mutant DELTA553-565 shows almost no activity Oxalobacter formigenes
4.1.1.8 R555A 96% activity compared to the wild type enzyme Oxalobacter formigenes
4.1.1.8 S553A 15% activity compared to the wild type enzyme Oxalobacter formigenes
4.1.1.8 Y120A 0.3% activity compared to the wild type enzyme Oxalobacter formigenes
4.1.1.8 Y120F 8.2% activity compared to the wild type enzyme Oxalobacter formigenes
4.1.1.8 Y483A 1.6% activity compared to the wild type enzyme Oxalobacter formigenes
4.1.1.8 Y483F 1.9% activity compared to the wild type enzyme Oxalobacter formigenes

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.8 3-deazathiamine diphosphate efficient inhibitor Oxalobacter formigenes

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.8 0.018
-
 oxalyl-CoA mutant enzyme E121Q, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl Oxalobacter formigenes
4.1.1.8 0.021
-
 oxalyl-CoA mutant enzyme S553A, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl Oxalobacter formigenes
4.1.1.8 0.0235
-
 oxalyl-CoA wild type enzyme Oxalobacter formigenes
4.1.1.8 0.024
-
 oxalyl-CoA mutant enzyme Y483A, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl Oxalobacter formigenes
4.1.1.8 0.04
-
 oxalyl-CoA mutant enzyme Y483F, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl Oxalobacter formigenes
4.1.1.8 0.041
-
 oxalyl-CoA mutant enzyme E121A, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl Oxalobacter formigenes
4.1.1.8 0.043
-
 oxalyl-CoA mutant enzyme Y120F, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl Oxalobacter formigenes
4.1.1.8 0.06
-
 oxalyl-CoA mutant enzyme Y120A, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl Oxalobacter formigenes
4.1.1.8 0.066
-
 oxalyl-CoA mutant enzyme R555A, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl Oxalobacter formigenes

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.8 Oxalobacter formigenes P40149
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.8 Blue-sepharose column chromatography Oxalobacter formigenes

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
4.1.1.8 tetramer x-ray crystallography Oxalobacter formigenes

Synonyms

EC Number Synonyms Comment Organism
4.1.1.8 Oxalyl coenzyme A decarboxylase
-
 Oxalobacter formigenes
4.1.1.8 OXC
-
 Oxalobacter formigenes

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.8 0.1
-
 oxalyl-CoA mutant enzyme E121A, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl Oxalobacter formigenes
4.1.1.8 0.26
-
 oxalyl-CoA mutant enzyme Y120A, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl Oxalobacter formigenes
4.1.1.8 1.4
-
 oxalyl-CoA mutant enzyme Y483A, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl Oxalobacter formigenes
4.1.1.8 1.7
-
 oxalyl-CoA mutant enzyme Y483F, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl Oxalobacter formigenes
4.1.1.8 3.3
-
 oxalyl-CoA mutant enzyme E121Q, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl Oxalobacter formigenes
4.1.1.8 7.2
-
 oxalyl-CoA mutant enzyme Y120F, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl Oxalobacter formigenes
4.1.1.8 13
-
 oxalyl-CoA mutant enzyme S553A, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl Oxalobacter formigenes
4.1.1.8 85
-
 oxalyl-CoA mutant enzyme R555A, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl Oxalobacter formigenes
4.1.1.8 88
-
 oxalyl-CoA wild type enzyme, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl Oxalobacter formigenes

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.8 thiamine diphosphate required Oxalobacter formigenes