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Literature summary for 2.3.1.26 extracted from

  • Yu, C.; Zhang, Y.; Lu, X.; Chen, J.; Chang, C.C.Y.; Chang, T.
    Role of the N-terminal hydrophilic domain of acyl-coenzyme A:cholesterol acyltransferase 1 on the enzymes's quaternary structure and catalytic efficiency (2002), Biochemistry, 41, 3762-3769.
    View publication on PubMed
Search for more literature for 2.3.1.26

Cloned(Commentary)

Cloned (Comment) Organism
production of glutathione S-transferase-ACAT1 fusion proteins, expression of fusion proteins in Escherichia coli and expression of various recombinant HisACAT1s in infected H5 cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information 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 Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
DuP 128 50% inhibition at 0.00013 mM for HisACAT1, 50% inhibition at 0.0001 mM for the mutants HisACAT1/p64 and HisACAT1/1-65 Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0072
-
 oleoyl-CoA HisACAT1, mutant HisACAT1/P64 Homo sapiens
0.0154
-
 oleoyl-CoA mutant HisACAT1/1-65 Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 expected monomer molecular masses of different fusion proteins range between 33000 and 41000 Da, sucrose density gradient velocity ultracentrifugation shows molecular masses of different fusion proteins ranging from 70000 to 160000 Da, thus some fusion proteins behave as tetramers in solution and other behave as dimers in solution Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
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 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oleoyl-CoA + cholesterol the dimeric enzyme responds to cholesterol in essentially the same manner as the tetrameric enzyme Homo sapiens CoA + cholesteryl oleate
-
 ?

Subunits

Subunits Comment Organism
homotetramer HisACAT1 Homo sapiens
More deleting a dimer-forming motif from the full-length ACAT1 converts the enzyme from a homotetramer to a homodimer that is more catalytically active than the native homotetramer Homo sapiens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 apparent t1/2 of activity loss: approximately 12 min for HisACAT1 and 20 min for the mutant HisACAT1/1-65, for the mutant HisACAT1/P64 the heat inactivation curve falls between the curves for HisACAT1 and HisACAT/1-65 and its shape seems to be biphasic Homo sapiens