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2.3.1.9: acetyl-CoA C-acetyltransferase

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

Word Map on EC 2.3.1.9

Reaction

2 acetyl-CoA =

CoA
+
acetoacetyl-CoA

Synonyms

2-methylacetoacetyl-CoA thiolase, 3-ketoacyl-CoA (T1)-like thiolase, 3-ketoacyl-CoA thiolase, 3-ketoacyl-coenzyme A thiolase, 3-oxothiolase, A1887, AACT, AACT1, AACT2, ACAT, ACAT1, ACAT2, ACCT, acetoacetyl CoA thiolase, acetoacetyl-CoA acetyltransferase, acetoacetyl-CoA C-acetyltransferase, acetoacetyl-CoA thiolase, acetoacetyl-CoA thiolase T2, acetyl coenzyme A thiolase, acetyl-CoA acetyltransferase, acetyl-CoA C-acetyltransferase, acetyl-CoA:N-acetyltransferase, acetyltransferase, acetyl coenzyme A, ACOAT, ACTRANS, AFUB_000550, AtoB, beta-acetoacetyl coenzyme A thiolase, beta-ketoacyl-CoA thiolase, beta-ketothiolase, CT, cytosolic acetoacetyl-CoA thiolase, cytosolic acetoacetyl-CoA thiolase 1, cytosolic acetoacetyl-CoA thiolase 2, ERG10, Erg10A, HFX_1022, HFX_1023, HFX_6003, HFX_6004, KACT, MmgA, Msed_0656, MSM-13 thiolase, OsAT1, phaA, ReH16_B0759, thiolase II, ThL, Tneu_0249, type II thiolase

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.9 acetyl-CoA C-acetyltransferase

Crystallization

Crystallization on EC 2.3.1.9 - acetyl-CoA C-acetyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of Erg10A and its complex with CoA, four substitutions within the CoA binding site are different from human orthologues
hanging drop vapor diffusion method, using 100 mM phosphate-citrate pH 4.2, 10% (w/v) polyethylene glycol 3350, 200 mM sodium chloride
purified recombinant enzyme in apoform and with bound CoA, hanging drop vapor diffusion method, mixing 0.001 ml of 40 mg/ml protein in 40 mM Tris-HCl, pH 8.0, and 5 mM 2-mercaptoethanol, with 0.001 ml of reservoir solution containing 1.0 M ammonium sulfate, 0.1 M HEPES, pH 7.25, and equilibration against 0.5 ml of reservoir solution, 20°C, 3 days, X-ray diffraction structure determination and analysis at 2.0-2.3 A resolution, molecular replacement method using the structure of Mycobacterium tuberculosis thiolase Mttt0182, PDB ID1ULQ, as a search model, structure modeling
purified recombinant enzyme in apoform or with bound CoA, hanging drop vapor diffusion method, mixing 0.0012 ml of 25 mg/ml protein in 40 mM Tris-HCl, pH 8.0, with 0.0012 ml of reservoir solution containing 17% PEG 8000, 0.1 M HEPES pH 7.0, and equilibration against 0.5 ml of reservoir solution, 20-22°C, 7 days, X-ray diffraction structure determination and analysis at 1.4-1.5 A resolution, molecular replacement method using the structure of Mycobacterium tuberculosis thiolase MtFadA5, PDB ID 4UBU as a search model, structure modeling
purified recombinant enzyme, sitting drop vapour diffusion method, mixing of 0.001 ml of 140 mg/ml protein in 40 mM Tris-HCl, pH 8.0, with 0.001 ml of reservoir solution containing 17% PEG 8000, 0.1 M HEPES pH 7.0, and equilibration against 0.5 ml of reservoir solution, 20°C, 7 days, X-ray diffraction structure determination and analysis at 1.4 A resolution
native enzyme at 1.8 A resolution, in complex with acetyl-CoA, at 1.9 A resolution
hanging drop vapor diffusion method at 4°C. Unliganded and liganded (with CoA and with K+) structures of the human mitochondrial recombinant tetrameric thiolase
-
only successful in the presence of CoA
acetoacetyl-CoA thiolase and 3-hydroxy-3-methylglutaryl -CoA synthase HMGCS form a complex. HMGCS catalyzes the second reaction in the mevalonate pathway. The 380-kDa crystal structure reveals that both enzymes are held together by a third protein (DUF35) with so-far-unknown function. The active-site clefts of thiolase and HMGCS form a fused CoA-binding site, which allows for efficient coupling of the endergonic thiolase reaction with the exergonic HMGCS reaction. The thiolase/HMGCS complex alone is able to convert acetyl-CoA to HMG-CoA. The tripartite complex is found in almost all archaeal genomes and in some bacterial ones
sitting drop method, 18-20°C. The crystal structure of the native complex revealed a unique, shared CoA-binding site formed by both the acetoacetyl-CoA thiolase and 3-hydroxy-3-methylglutaryl (HMG)-CoA synthase subunits thiolases (thiolases). A small scaffold protein connects the two enzymes
microbatch method, using either 20% (w/v) PEG 3350, 0.15 M calcium chloride dehydrate, or 45% (w/v) PEG 200, 0.1 M MES monohydrate pH 6.0, 0.07 M calcium chloride dehydrate or 0.2 M sodium acetate trihydrate, 0.1 M sodium cacodylate trihydrate pH 6.5, 30% (w/v) PEG 8000, 5% (v/v) n-octyl-beta-D-glucoside
-
structures of apo ERG10 and its Cys91Ala variant, at resolutions of 2.2 and 1.95 A, respectively. ERG10 shares the characteristic thiolase superfamily fold, apart from Ala159 at the entrance to the pantetheine-binding cavity, which appears to be a determinant of the poor binding ability of the substrate
hangig-drop vapor diffusion at 21°C, crystal structure at 2.0 A resolution
-
wild-type thiolase and acetylated thiolase complexed with CoA, C89A mutant thiolase complexed with acetyl-CoA and acetoacetyl-CoA, Q64A mutant thiolase