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A1:1-123
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chimeric protein A1(1-123)-A2(105-526)
A1:1-385
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chimeric protein A1(1-385)-A2(364-440)-A1(463-550)
A1:1-71
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chimeric protein A1(1-71)-A2(70-562)
A1D400N
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mutant, evaluation of conserved aspartic acid residues
A1D406A
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mutant, evaluation of conserved aspartic acid residues
A1H386N
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mutant, identification of essential histidines required for activity
A1H425A
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mutant, identification of essential histidines required for activity
A1H460A
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mutant, identification of essential histidines required for activity
A1S128A
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mutant, identification of the role of conserved serine residues in determination of the activity
A1S194A
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mutant, identification of the role of conserved serine residues in determination of the activity
A1S269A
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mutant, identification of the role of conserved serine residues in determination of the activity
A1S410A
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mutant, identification of the role of conserved serine residues in determination of the activity
A1S412A
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mutant, identification of the role of conserved serine residues in determination of the activity
A1S414L
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mutant, identification of the role of conserved serine residues in determination of the activity
A1S456A
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mutant, identification of the role of conserved serine residues in determination of the activity
A1Y142F
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mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
A1Y308F
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mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
A1Y312F
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mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
A1Y322F
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mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
A1Y404F
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mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
A1Y433F
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mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
A1Y518F
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mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
A2:1-227
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chimeric protein A2(1-227)-A1(248-489)-A2(468-526)
A2:1-249
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chimeric protein A2(1-249)-A1(270-362)-A2(341-526)
A2:1-363
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chimeric protein A2(1-363)-A1(386-462)-A2(441-526)
A2:1-428
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chimeric protein A2(1-428)-A1(444-550)
A2:1-440
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chimeric protein A2(1-440)-A1(463-502)-A2(480-526)
A2:1-479
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chimeric protein A2(1-479)-A1(502-550)
Ch1
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chimeric protein A2(1-428)-A1(451-462)-A2(441-526)
A2D378E
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mutant, evaluation of conserved aspartic acid residues
A2D384A
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mutant, evaluation of conserved aspartic acid residues
A2H364N
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mutant, identification of essential histidines required for activity
A2H403A
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mutant, identification of essential histidines required for activity
A2H438A
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mutant, identification of essential histidines required for activity
A2S109A
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mutant, identification of the role of conserved serine residues in determination of the activity
A2S176A
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mutant, identification of the role of conserved serine residues in determination of the activity
A2S249A
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mutant, identification of the role of conserved serine residues in determination of the activity
A2S388A
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mutant, identification of the role of conserved serine residues in determination of the activity
A2S390A
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mutant, identification of the role of conserved serine residues in determination of the activity
A2S392A
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mutant, identification of the role of conserved serine residues in determination of the activity
A2S434A
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mutant, identification of the role of conserved serine residues in determination of the activity
A2Y124F
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mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
A2Y286F
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mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
A2Y290F
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mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
A2Y300F
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mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
A2Y382F
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mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
A2Y411F
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mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
A2Y496F
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mutant, evaluation of the role of conserved tyrosine residues as a requirement for the activity
C333A
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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
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expressed in H5 cells, the mutant contains essentially the same activity as the wild-type ACAT1. Sensitive to p-chloromercuribenzene sulfonic acid inhibition
C345A
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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
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insensitive to p-chloromercuribenzene sulfonic acid
C365A
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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
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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
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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
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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
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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
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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
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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
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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
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sensitive to p-chloromercuribenzene sulfonic acid inhibition
C92A/C333A/C345A/C365A/C467A/C516A/C546A
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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
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insensitive to p-chloromercuribenzene sulfonic acid
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
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almost complete loss of activity
H434N
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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
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no loss of activity
S245L
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about 40% loss of activity
T254I
naturally occuring polymorphism, the mutant shows enzyme the same enzyme activity as the wild-type
C92A/C333A/C345A/C365A/C387A/C467A/C516A/C528A/C54
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expressed in H5 cells or in ACAT-deficient Chinese hamster ovary cells: both mutants retain partial enzyme activity
C92A/C333A/C345A/C365A/C387A/C467A/C516A/C528A/C54
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this mutant is localized in endoplasmic reticulum in Chinese hamster ovary cells, homotetramer. Insensitive to p-chloromercuribenzene sulfonic acid
C92A/C333A/C345A/C365A/C387A/C467A/C516A/C546A
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this mutant is localized in endoplasmic reticulum in Chinese hamster ovary cells
C92A/C333A/C345A/C365A/C387A/C467A/C516A/C546A
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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/C467A/C516A/C546A
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expressed in H5 cells or in ACAT-deficient Chinese hamster ovary cells: both mutants retain partial enzyme activity
C92A/C467A/C516A/C546A
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this mutant is localized in endoplasmic reticulum in Chinese hamster ovary cells
additional information
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production of double or single proline mutants derived from glutathione S-transferase-ACAT1 fusion proteins shows that the dimer-forming domain is within ACAT1 amino acids 30 to 94. Production of mutants derived from the recombinant plasmid pHisACAT1 to test the effect of mutagenizing or deleting the N-terminal peptide on the oligomerization state of ACAT1
additional information
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insertion of two different antigenic tags at various hydrophilic regions flanking each of the predicted transmembrane domains, analysis indicates that the enzyme contains only 2 detectable transmembrane domains, located near the N-terminal region
additional information
generation of enzyme knockout SOAT2-/- mice
additional information
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generation of enzyme knockout SOAT2-/- mice
additional information
generation of tissue-specific SOAT2 knockouts in liver and small intestine, i.e. SOAT2L-/L- and SOAT2SI-/SI- mice, phenotypes, overview. Floxed mice (LoxP sites flanked exons 11 through 13 of the SOAT2 gene on chromosome 15) are designated as SOAT2fl/fl. SOAT2 wild-type control mice (SOAT2+/+LDLr?/?) and SOAT2 floxed mice (SOAT2fl/flLDLr?/?) have similar levels of cholesterol absorption. SOAT2 total body knockout mice (SOAT2?/?LDLr?/?) and intestinal SOAT2 knockout mice (SOAT2SI?/SI?LDLr?/?) have significantly decreased levels of cholesterol absorption, overview. SOAT2 knockout mice have lower plasma VLDL and LDL cholesterol concentrations