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2.3.1.39: [acyl-carrier-protein] S-malonyltransferase

This is an abbreviated version!
For detailed information about [acyl-carrier-protein] S-malonyltransferase, go to the full flat file.

Word Map on EC 2.3.1.39

Reaction

malonyl-CoA
+
an [acyl-carrier protein]
=
CoA
 +
a malonyl-[acyl-carrier protein]

Synonyms

EtMCAT, FabD, FabD2, FAS, fatty acid synthase, HpMCAT, malonyl CoA-ACP malonyltransferase, malonyl CoA-ACP transacylase, malonyl CoA-acyl carrier protein transacylase, malonyl coenzyme A-acyl carrier protein transacylase, malonyl coenzyme A:acyl carrier protein transacylase, malonyl transacylase, malonyl transferase, malonyl-CoA acyl carrier protein transacylase, malonyl-CoA-acyl carrier protein transacylase, malonyl-CoA/ACP transacylase, malonyl-CoA/holo-ACP transacylase, malonyl-CoA: ACP transacylase, malonyl-CoA:ACP transacylase, malonyl-CoA:AcpM transacylase, malonyl-CoA:acyl carrier protein transacylase, malonyl-CoA:acyl-carrier protein transacylase, malonyl-CoA–acyl carrier protein transacylase, malonyl-coenzyme A (CoA)/holo-ACP transacylase, malonyl-coenzyme A-holo-acyl-carrier protein transacylase, malonyl-coenzyme A: acyl-carrier protein transacylase, malonyl-coenzyme A:ACP transacylase, malonyl-coenzymeA:acyl-carrier protein transacylase, malonyltransferase, [acyl-carrier-protein], MAT, MCAMT, MCAT, MCT, MdcH, More, mtFabD, SaMCAT, SpnMCAT, XoMCAT, [acyl carrier protein]malonyltransferase

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.39 [acyl-carrier-protein] S-malonyltransferase

Crystallization

Crystallization on EC 2.3.1.39 - [acyl-carrier-protein] S-malonyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method
sitting drop vapor diffusion method, using 1.4 M ammonium tartrate dibasic and 0.1 M Tris (pH 8.5)
mapping the active site of Escherichia coli malonyl-CoA-acyl carrier protein transacylase by protein crystallography
-
crystal structure of HpMCAT at 2.5 A resolution is shown. HpMCAT has a compact folding composed of a large subdomain with a similar core as in alpha/beta hydrolases, and a similar ferredoxin-like small subdomain as in acylphosphatases
crystal structure of MCAT is determined to 2.3 A
crystal structure of Mycobacterium tuberculosis MCAT (mtFabD) is determined to 3.0 A resolution by multi-wavelength anomalous dispersion. Phasing is facilitated by Ni2+ ions bound to the 20-residue N-terminal affinity tag, which packed between the two independent copies of mtFabD
crystal structures of MCAT from Staphylococcus aureus and Streptococcus pneumoniae are determined at 1.46 and 2.1 A resolution, respectively. In the SaMCAT structure, the N-terminal expression peptide of a neighboring molecule running in the opposite direction of malonyl-CoA makes extensive interactions with the highly conserved Gly-Gln-Gly-Ser-Gln stretch, suggesting a new design platform
crystal structures of MCAT from Staphylococcus aureus and Streptococcus pneumoniae are determined at 1.46 and 2.1 A resolution, respectively
-
recombinant purified enzyme, 3 mg/ml protein in 10 mM Tris-HCl, pH 7.4, 1 mM 2-mercaptoethanol, hanging drop vapoir diffusion method, 3 days, room temperature, soaking of crystals in 30% PEG 4000, 100 mM sodium acetate, pH 4.8, 200 mM ammonium acetate, and 20% glycerol for cryoprotection, X-ray diffraction structure determination and analysis at 2.0 A resolution, macromolecular docking simulation with K47A/K190A/R287A/K293A mutant actinorhodin ACP structure, overview
-
purified recombinant enzyme, X-ray diffraction structure determination and analysis
the crystal structure of malonyl CoA-acyl carrier protein transacylase (XoMCAT) is determined at 2.3 A resolution in complex with N-cyclohexyl-2-aminoethansulfonic acid
-
to 1.9 A resolution, space group P212121