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4.1.1.9: malonyl-CoA decarboxylase

This is an abbreviated version!
For detailed information about malonyl-CoA decarboxylase, go to the full flat file.

Word Map on EC 4.1.1.9

Reaction

malonyl-CoA
=
acetyl-CoA
 +
CO2

Synonyms

Acyl-CoA: malonate CoA transferase/malonyl-CoA decarboxylase, Decarboxylase, malonyl coenzyme A, hMCD, malonyl CoA decarboxylase, Malonyl coenzyme A decarboxylase, Malonyl-CoA decarboxylase, malonyl-CoA decarboxylase/acetyltransferase, malonyl-coenzyme A decarboxylase, MCD, MLYCD

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.9 malonyl-CoA decarboxylase

Crystallization

Crystallization on EC 4.1.1.9 - malonyl-CoA decarboxylase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, microbatch method, 0.002 ml of the protein solution containing 10 mM Tris, pH 7.5, 100 mM NaCl, 5 mM DTT, and 0.02% NaN3 are mixed with 0.002 ml of the precipitant solution consisting of 200 mM ammonium sulfate, and 20% w/v PEG3350, 18°C, X-ray diffraction structure determination and analysis at 2.3-3.1 A, selenomethionyl single-wavelength anomalous diffraction method, molecular replacement
purified recombinant enzyme, microbatch method, mixingof 0.002 ml of protein in 20 mM Tris, pH 7.0, 250 mM NaCl, 5% v/v glycerol, and 3 mM malonyl-CoA with crystallization solution containing 160 mM magnesium chloride, 80 mM Tris, pH 8.5, 24% w/v PEG 4000, 20% v/v glycerol, and 3% v/v ethanol, 18°C, X-ray diffraction structure determination and analysis at 2.3-3.1 A, selenomethionyl single-wavelength anomalous diffraction method, molecular replacement
purified recombinant detagged enzyme, from 15% PEG 2000 monomethyl ether and 0.1 M sodium acetate, pH 4.5, and 10 mM sodium citrate, sitting drop vapor diffusion method, X-ray diffraction structure determination and analysis at 3.3-4.3 A resolution, molecular replacement
recombinant mutant E58A/K59A/E278A/E279A/K280A, sitting-drop vapor diffusion method, mixing of 10 mg/ml protein in HEPES, pH 7.5, 100 mM NaCl, 1% v/v glycerol, and 5 mM decanoyl-CoA. in a 2:1 ratio with a precipitant solution containing 10% w/v PEG 20000 and 0.1 M 2-(N-morpholino)ethanesulfonic acid, pH 6.0, at room temperature, X-ray diffraction structure determination and analysis at 2.8 A, by single isomorphous replacement with anomalous scattering
hanging drop vapour-diffusion method, X-ray analysis
purified recombinant enzyme, microbatch method, 0.002 ml of the protein solution containing 10 mM Tris, pH 7.5, 100 mM NaCl, 5 mM DTT, and 0.02% NaN3 are mixed with 0.002 ml of the precipitant solution consisting of 0.1 M magnesium nitrate, 100 mM Tris, pH 8.5, and 33% v/v PEG 400, 18°C, X-ray diffraction structure determination and analysis at 2.3-3.1 A, selenomethionyl single-wavelength anomalous diffraction method, molecular replacement
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