Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

2.3.1.16: acetyl-CoA C-acyltransferase

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

Word Map on EC 2.3.1.16

Reaction

acyl-CoA
+
acetyl-CoA
=
CoA
 +
3-oxoacyl-CoA

Synonyms

2-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase/3-oxoacyl-CoA thiolase, 3-KAT, 3-ketoacyl CoA thiolase, 3-ketoacyl coenzyme A thiolase, 3-ketoacyl coenzyme-A thiolase, 3-ketoacyl thiolase, 3-ketoacyl-CoA thiolase, 3-ketothiolase, 3-oxoacyl-CoA thiolase, 3-oxoacyl-coenzyme A thiolase, 3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase, 6-oxoacyl-CoA thiolase, ACAA2, acetoacetyl-CoA beta-ketothiolase, acetyl-CoA acyltransferase, acyl-CoA-thiolase, acyltransferase, acetyl coenzyme A, beta-ketoacyl coenzyme A thiolase, beta-ketoacyl-CoA thiolase, beta-ketoadipyl coenzyme A thiolase, beta-ketoadipyl-CoA thiolase, beta-ketothiolase, BktB, ELo1, Elovl-5, Elovl-6, ELOVL5, Elovl6, enoyl-coenzyme A (CoA) hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein, FadA, fatty acid elongase 5, KAT, KAT-1, KAT2, ketoacyl-CoA acyltransferase, ketoacyl-coenzyme A thiolase, long-chain 3-oxoacyl-CoA thiolase, mitochondrial 3-ketoacyl-CoA thiolase, oxoacyl-coenzyme A thiolase, PaaJ, pro-3-ketoacyl-CoA thiolase, PUFA elongase, SCP2/3-oxoacyl-CoA thiolase, SCPx, sterol carrier protein 2/3-oxoacyl-CoA thiolase, TFE-beta subunit, Thb, thiloase B, thiolase A, thiolase I, thiolase II, thiolase III

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.16 acetyl-CoA C-acyltransferase

Crystallization

Crystallization on EC 2.3.1.16 - acetyl-CoA C-acyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, hanging drop vapour diffusion method, 0.002 ml of protein solution is mixed with 0.002 ml reservoir solution containing 0.1 M Tris–HCl, pH 8.5, 300 mM MgCl2, and 25% w/v polyethylene glycol 4000, X-ray diffraction structure determination and analysis at 2.1-2.4 A resolution
to 1.5 A resolution. The dimeric structure exhibits a typical thiolase-like fold. Dimer formation and active site conformation appear in an open, active, reduced state
modeling of the heterotetrameric alpha2beta2 complex
to 1.8 A resolution. The dimeric structure exhibits a typical thiolase-like fold. Dimer formation and active site conformation appear in an open, active, reduced state
purified recombinant wild-type and mutant enzymes in apoform and in complex with CoA, hanging drop vapour diffusion method, mixing of 0.002 ml of 4.4 mg/ml protein in 25 mM Tris-HCl pH 8.0, 1 mM DTT, with 0.002 ml of reservoir solution containing 100 mM MES, pH 6.6, or MOPS, pH 7.2, and 14-15% PEG MME 5000, equilibration against 1 ml of reservoir solution, 22°C, method optimization, X-ray diffraction structure determination and analysis at 2.0-3.3 A resolution, modeling