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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

Engineering

Engineering on EC 2.3.1.26 - sterol O-acyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A1:1-123
-
chimeric protein A1(1-123)-A2(105-526)
A1:1-385
-
chimeric protein A1(1-385)-A2(364-440)-A1(463-550)
A1:1-71
-
chimeric protein A1(1-71)-A2(70-562)
A1D400N
-
mutant, evaluation of conserved aspartic acid residues
A1D406A
-
mutant, evaluation of conserved aspartic acid residues
A1H386N
-
mutant, identification of essential histidines required for activity
A1H425A
-
mutant, identification of essential histidines required for activity
A1H460A
-
mutant, identification of essential histidines required for activity
A1S128A
-
mutant, identification of the role of conserved serine residues in determination of the activity
A1S194A
-
mutant, identification of the role of conserved serine residues in determination of the activity
A1S269A
-
mutant, identification of the role of conserved serine residues in determination of the activity
A1S410A
-
mutant, identification of the role of conserved serine residues in determination of the activity
A1S412A
-
mutant, identification of the role of conserved serine residues in determination of the activity
A1S414L
-
mutant, identification of the role of conserved serine residues in determination of the activity
A1S456A
-
mutant, identification of the role of conserved serine residues in determination of the activity
A1Y142F
-
mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
A1Y308F
-
mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
A1Y312F
-
mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
A1Y322F
-
mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
A1Y404F
-
mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
A1Y433F
-
mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
A1Y518F
-
mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
A2:1-227
-
chimeric protein A2(1-227)-A1(248-489)-A2(468-526)
A2:1-249
-
chimeric protein A2(1-249)-A1(270-362)-A2(341-526)
A2:1-363
-
chimeric protein A2(1-363)-A1(386-462)-A2(441-526)
A2:1-428
-
chimeric protein A2(1-428)-A1(444-550)
A2:1-440
-
chimeric protein A2(1-440)-A1(463-502)-A2(480-526)
A2:1-479
-
chimeric protein A2(1-479)-A1(502-550)
A2C497S
-
A2 mutant
A2I491V
-
A2 mutant
A2L480M
-
A2 mutant
A2L495F
-
A2 mutant
A2M484S
-
A2 mutant
A2Q489N
-
A2 mutant
A2Q492L
-
A2 mutant
A2R504Q
-
A2 mutant
A2S494C
-
A2 mutant
A2V493L
-
A2 mutant
Ch1
-
chimeric protein A2(1-428)-A1(451-462)-A2(441-526)
CT504
-
A2(1-504)
A2D378E
-
mutant, evaluation of conserved aspartic acid residues
A2D384A
-
mutant, evaluation of conserved aspartic acid residues
A2H364N
-
mutant, identification of essential histidines required for activity
A2H403A
-
mutant, identification of essential histidines required for activity
A2H438A
-
mutant, identification of essential histidines required for activity
A2S109A
-
mutant, identification of the role of conserved serine residues in determination of the activity
A2S176A
-
mutant, identification of the role of conserved serine residues in determination of the activity
A2S249A
-
mutant, identification of the role of conserved serine residues in determination of the activity
A2S388A
-
mutant, identification of the role of conserved serine residues in determination of the activity
A2S390A
-
mutant, identification of the role of conserved serine residues in determination of the activity
A2S392A
-
mutant, identification of the role of conserved serine residues in determination of the activity
A2S434A
-
mutant, identification of the role of conserved serine residues in determination of the activity
A2Y124F
-
mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
A2Y286F
-
mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
A2Y290F
-
mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
A2Y300F
-
mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
A2Y382F
-
mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
A2Y411F
-
mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
A2Y496F
-
mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
C333A
-
expressed in H5 cells, the mutant retains a significant amount of activity, Cys-333 is not essential for ACAT1 catalysis, the mutant is expressed as a single, undegraded 50-kDA band
C333A/C345A/C365A
-
expressed in H5 cells, the mutant contains essentially the same activity as the wild-type ACAT1. Sensitive to p-chloromercuribenzene sulfonic acid inhibition
C345A
-
expressed in H5 cells, the mutant retains a significant amount of activity, Cys-345 is not essential for ACAT1 catalysis, the mutant is expressed as a single, undegraded 50-kDA band
C345A/C467A
-
insensitive to p-chloromercuribenzene sulfonic acid
C365A
-
expressed in H5 cells, the mutant retains a significant amount of activity, Cys-365 is not essential for ACAT1 catalysis, the mutant is expressed as a single, undegraded 50-kDA band
C387A
-
expressed in H5 cells, the mutant retains a significant amount of activity, Cys-387 is not essential for ACAT1 catalysis, the mutant is expressed as a single, undegraded 50-kDA band
C467A
-
expressed in H5 cells, the mutant retains a significant amount of activity, Cys-467 is not essential for ACAT1 catalysis, the mutant is expressed as a single, undegraded 50-kDA band
C516A
-
expressed in H5 cells, the mutant retains a significant amount of activity, Cys-516 is not essential for ACAT1 catalysis, the mutant is expressed as a single, undegraded 50-kDA band
C528A
-
expressed in H5 cells, the mutant retains a significant amount of activity, Cys-528 is not essential for ACAT1 catalysis, the mutant is expressed as a single, undegraded 50-kDA band
C546A
-
expressed in H5 cells, the mutant retains a significant amount of activity , Cys-546 is not essential for ACAT1 catalysis, the mutant is expressed as a single, undegraded 50-kDA band
C92A
-
expressed in H5 cells, the mutant retains a significant amount of activity, Cys-92 is not essential for ACAT1 catalysis, the mutant is expressed as a single, undegraded 50-kDA band
C92A/C333A/C345A/C365A/C387A/C467A/C516A
-
resistant to p-chloromercuribenzene sulfonic acid inhibition
C92A/C333A/C345A/C365A/C387A/C467A/C516A/C528A/C54
C92A/C333A/C345A/C365A/C387A/C467A/C516A/C546A
C92A/C333A/C345A/C365A/C387A/C516A/C528A/C546A
-
sensitive to p-chloromercuribenzene sulfonic acid inhibition
C92A/C333A/C345A/C365A/C467A/C516A/C546A
-
expressed in H5 cells or in ACAT-deficient Chinese hamster ovary cells: both mutants retain partial enzyme activity. Resistant to p-chloromercuribenzene sulfonic acid inhibition
C92A/C333A/C365A/C387A/C467A/C516A/C528A/C546A
-
insensitive to p-chloromercuribenzene sulfonic acid
C92A/C467A/C516A/C546A
E14G
naturally occuring polymorphism, the enzymatic activity of the mutant is approximately two times higher than the wild-type activity
H360A
complete loss of activity
H386A
complete loss of activity. Enzymatic activity is restored to values below 37% of the level of the wild-type activity when cholesterol is replaced by 25-hydroxycholesterol as substrate
H399A
complete loss of activity
H425A
59% of the wild-type activity, inhibitory sensitivity against oleic acid anilide ias decreased about 3fold
H434A
-
almost complete loss of activity
H434N
-
almost complete loss of activity
H460A
complete loss of activity
H501A
75% of the wild-type activity, inhibitory sensitivity against oleic acid anilide ias decreased about 10fold
H527A
96% of the wild-type activity, inhibitory sensitivity against oleic acid anilide ias decreased about 10fold
S245A
-
no loss of activity
S245L
-
about 40% loss of activity
T254I
naturally occuring polymorphism, the mutant shows enzyme the same enzyme activity as the wild-type
additional information