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Information on EC 2.3.1.26 - sterol O-acyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P53629

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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.26 sterol O-acyltransferase
IUBMB Comments
The enzyme catalyses the formation of sterol esters from a sterol and long-chain fatty acyl-coenzyme A. The enzyme from yeast, but not from mammals, prefers monounsaturated acyl-CoA. In mammals the enzyme acts mainly on cholesterol and forms cholesterol esters that are stored in cytosolic droplets, which may serve to protect cells from the toxicity of free cholesterol. In macrophages, the accumulation of cytosolic droplets of cholesterol esters results in the formation of `foam cells', a hallmark of early atherosclerotic lesions. In hepatocytes and enterocytes, cholesterol esters can be incorporated into apolipoprotein B-containing lipoproteins for secretion from the cell.
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Saccharomyces cerevisiae
UNIPROT: P53629
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Synonyms
hacat, acat1, acat2, acyl-coa:cholesterol acyltransferase, acat-1, acyl-coa cholesterol acyltransferase, soat1, cholesterol acyltransferase, acyl-coenzyme a:cholesterol acyltransferase, acat-2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACAT
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acyl coenzyme A-cholesterol-O-acyltransferase
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acyl-CoA:cholesterol acyltransferase
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acylcoenzyme A:cholesterol O-acyltransferase
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acyltransferase, cholesterol
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cholesterol acyltransferase
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cholesterol ester synthase
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cholesterol ester synthetase
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cholesteryl ester synthetase
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sterol-ester synthase
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sterol-ester synthetase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
long-chain acyl-CoA:sterol O-acyltransferase
The enzyme catalyses the formation of sterol esters from a sterol and long-chain fatty acyl-coenzyme A. The enzyme from yeast, but not from mammals, prefers monounsaturated acyl-CoA. In mammals the enzyme acts mainly on cholesterol and forms cholesterol esters that are stored in cytosolic droplets, which may serve to protect cells from the toxicity of free cholesterol. In macrophages, the accumulation of cytosolic droplets of cholesterol esters results in the formation of `foam cells', a hallmark of early atherosclerotic lesions. In hepatocytes and enterocytes, cholesterol esters can be incorporated into apolipoprotein B-containing lipoproteins for secretion from the cell.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-63-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
oleoyl-CoA + cholesterol
CoA + cholesteryl oleate
show the reaction diagram
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-
?
oleoyl-CoA + ergosterol
CoA + ergosteryl oleate
show the reaction diagram
endogenous ergosterol as substrate or exogenous ergosterol in the form of ergosterol/phosphatidylcholine vesicles as substrate
-
?
acetyl-CoA + cholesterol
CoA + cholesteryl acetate
show the reaction diagram
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16% of the activity with oleoyl-CoA
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?
acyl-CoA + cholesterol
CoA + cholesterol ester
show the reaction diagram
lauroyl-CoA + cholesterol
CoA + cholesteryl laurate
show the reaction diagram
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62% of the activity with oleoyl-CoA
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?
myristoyl-CoA + cholesterol
CoA + cholesteryl myristate
show the reaction diagram
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37% of the activity with oleoyl-CoA
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?
oleoyl-CoA + cholesterol
CoA + cholesteryl oleate
show the reaction diagram
oleoyl-CoA + episterol
CoA + episteryl oleate
show the reaction diagram
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62% of the activity with cholesterol
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?
oleoyl-CoA + ergosterol
CoA + ergosteryl oleate
show the reaction diagram
oleoyl-CoA + fecosterol
CoA + fecosteryl oleate
show the reaction diagram
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48% of the activity with cholesterol
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?
oleoyl-CoA + lanosterol
CoA + lanosteryl oleate
show the reaction diagram
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65% of the activity with cholesterol
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?
oleoyl-CoA + zymosterol
CoA + zymosteryl oleate
show the reaction diagram
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93% of the activity with cholesterol
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?
palmitoleoyl-CoA + cholesterol
CoA + cholesteryl palmitoleate
show the reaction diagram
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91% of the activity with oleoyl-CoA
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?
palmitoyl-CoA + cholesterol
CoA + cholesteryl palmitate
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CoA
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required by the in-situ acyl-CoA production
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CI-976
cell-free extract of wild-type cells: approximately 90% inhibition at 0.1 mM and more than 95% inhibition at 0.2 mM, intact wild-type cells: approximately 75-80% inhibition at 0.2 mM
DuP 128
approximately 50% inhibition at 0.03-0.04 mM
acetone
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about 40% inhibition at a final concentration of 1% v/v
butanol
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about 40% inhibition at a final concentration of 1% v/v
ethanol
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about 40% inhibition at a final concentration of 1% v/v
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06
cholesterol
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with oleoyl-CoA
0.069
oleoyl-CoA
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
71600
deduced from amino acid sequence data
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
there are six potential N-linked glycosylation sites in sat1, two of which are conserved in sat2
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, stable for several weeks
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
two genes, SAT1 and SAT2 encode isozymes of the enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Taketani, S.; Nishino, T.; Katsuki, H.
Characterization of sterol-ester synthetase in Saccharomyces cerevisiae
Biochim. Biophys. Acta
575
148-155
1979
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Billheimer, J.T.
Cholesterol acyltransferase
Methods Enzymol.
111
286-293
1985
Saccharomyces cerevisiae, Helicoverpa zea, Homo sapiens, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Yu, C.; Kennedy, N.J.; Chang, C.C.Y.; Rothblatt, J.A.
Molecular cloning and characterization of two isoforms of Saccharomyces cerevisiae acyl-CoA:sterol acyltransferase
J. Biol. Chem.
271
24157-24163
1996
Homo sapiens, Saccharomyces cerevisiae (P53629), Saccharomyces cerevisiae
Manually annotated by BRENDA team