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2.3.1.26: sterol O-acyltransferase

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

Word Map on EC 2.3.1.26

Reaction

a long-chain acyl-CoA
+
a sterol
=
CoA
+
a long-chain 3-hydroxysterol ester

Synonyms

A2, ACAT, ACAT-1, ACAT-2, ACAT1, ACAT2, acyl coenzyme A-cholesterol-O-acyltransferase, acyl coenzyme A: cholesteryl acyltransferase, acyl-CoA cholesterol acyltransferase, acyl-CoA cholesterol O-acyltransferase, acyl-CoA: cholesterol acyltransferase, acyl-CoA:cholesterol acyltransferase, acyl-CoA:cholesterol acyltransferase 1, acyl-CoA:cholesterol acyltransferase 2, acyl-coA:cholesterol o-acyl transferase 2, acyl-coenzyme A: cholesterol acyltransferase, acyl-coenzyme A:cholesterol acyltransferase, acyl-coenzyme A:cholesterol acyltransferase 1, acyl-coenzyme A:cholesterol acyltransferase 2, acyl-coenzyme A:cholesterol acyltransferase-1, acyl-coenzyme A:cholesterol O-acyltransferase, acyl-coenzymeA cholesterol acyltransferase, acyl-coenzymeA:cholesterol acyl-transferase, acylcoenzyme A:cholesterol O-acyltransferase, acyltransferase, cholesterol, AsAT, cholesterol acyltransferase, cholesterol acyltransferase 2, cholesterol ester synthase, cholesterol ester synthetase, cholesteryl ester synthetase, hACAT, hACAT-1, hACAT-2, hACAT1, SOAT, SOAT!, Soat1, Soat2, sterol O-acyltransferase 2, sterol-ester synthase, sterol-ester synthetase, steroyl O-acyltransferase 1, steroyl O-acyltransferase 2

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.26 sterol O-acyltransferase

Purification

Purification on EC 2.3.1.26 - sterol O-acyltransferase

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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
based on solubilization in CHAPS, preparative free-flow isotachophoresis, and further separation of the protein showing enzyme activity by preparative free-flow IEF, followed by removal of nonglycosylated proteins by ConA-affinity chromatography and preparative SDS-PAGE
-
liver microsomes are prepared
-
microsomal fractions are prepared
microsomal fractions of CHO cells are prepared
-
microsomal fractions of Hi5 cells containing baculovirally expressed hACAT-1 are prepared and used as the source for the enzyme
microsomal fractions of Hi5 cells containing baculovirally expressed hACAT-1 are used as sources of the enzyme
-
microsomal fractions of Hi5 cells containing baculovirally expressed hACAT-2 are prepared and used as the source for the enzyme
microsomal fractions of Hi5 cells containing baculovirally expressed hACAT-2 are used as sources of the enzyme
-
microsomes are prepared
microsomes from AC29 cells are prepared
microsomes prepared from monocyte-derived macrophagesare are used as an enzyme source
-
of the glutathione S-transferase-ACAT1 peptide fusion protein using chromatography on glutathione-Sepharose 4B column and of various recombinant HisACAT1s expressed in infected H5 cells using a Talon Superflow resin
-
of the recombinant enzyme using solubilization with CHAPS und KCl, chromatography on cobalt column and chromatography on monoclonal antibody affinity column
-
partial, using ammonium acetate fractionation and Sepharose 4B column chromatography
-
recombinant 50-kDa human ACAT1 to homogeneity with full retention in enzymatic activity
when solubilized in the detergent CHAPS, ACAT1 can be purified to homogeneity with full enzyme activity and behaves as a homotetrameric protein. Treating ACAT1 with non-ionic detergent, Triton X-100 or octyl glucoside, leads to a two-fold monomer without any enzymatic activity. Detergent exchange of Triton X-100 with CHAPS restores ACAT1 to a two-fold dimer but fails to restore its enzymatic activity