Literature summary for 2.3.1.26 extracted from

Neumann, B.; Chang, C.C.Y.; Chang, T.Y.
Triton X-100 or octyl glucoside inactivates acyl-CoA cholesterol acyltransferase 1 by dissociating it from a two-fold dimer to a two-fold monomer (2019), Arch. Biochem. Biophys., 671, 103-110 .

Inhibitors

Inhibitors	Comment	Organism	Structure
octyl beta-D-glucopyranoside	presence of octylglucoside dissociates ACAT1 to form a dimeric species	Homo sapiens
Triton X-100	presence of Triton X-100 dissociates ACAT1 to form a dimeric species	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
endoplasmic reticulum	-	Homo sapiens	5783	-

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
80000	150000	sucrose density gradient centrifugation, protein solubilized by Triton X-100 or octylglucoside	Homo sapiens
200000	250000	sucrose density gradient centrifugation, protein solubilized by CHAPS	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P35610	-	-

Purification (Commentary)

Purification (Comment)	Organism
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	Homo sapiens

Purification (Comment)

Organism

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

Homo sapiens

Subunits

Subunits	Comment	Organism
More	ACAT1 contains two dimerization motifs. The first motif is located near the N-terminus and is not conserved. Deletion of the N-terminal dimerization domain converts ACAT1 to a dimer with full catalytic activity, i.e. ACAT1 is a two-fold dimer. The second dimerization domain, located near the C-terminus, is conserved	Homo sapiens
tetramer	4 * 56000, SDS-PAGE, His- and FLAG-tagged protein	Homo sapiens

Synonyms

Synonyms	Comment	Organism
ACAT1	-	Homo sapiens