EC Number | Cloned (Comment) | Organism |
---|---|---|
2.3.1.43 | gene lcat, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS, recombinant expression of the enzyme in apoI-deficient mice, recombinant expression in CHO cells | Homo sapiens |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.3.1.43 | additional information | generation of human LCAT transgenic mice that are apoA-I deficient by breeding hLCATTg/Tg mice on C57Bl/6J background with apoA-I-/- mice on C57Bl/6J background, both over more than 10 generations | Homo sapiens |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.43 | additional information | Homo sapiens | structure/function requirements for the apolipoprotein A-I and lecithin cholesterol acyltransferase interaction loop of HDL, binding studies with recombinant wild/type apoA-I and apoA-I mutants P165A, Y166A, Y166E, Y166F, Y166N, S167A, D168A, Y192F, and Y192L. Loss of LCAT activation caused by apoA-I Y166A or Y166F mutations is at least partially due to the weaker binding between LCAT and apoA-I within these rHDL. Both Vmax of Y166F and Y166A are 20% lower than that of wild-type apoA-I, and the apparent Km are about 2-6fold higher than wild-type. rHDL formed with either apoA-I Y192F or Y192L mutants show normal LCAT activity. Incubation of hLCAT with rHDL formed using the apoA-I mutants P165A, Y166A, Y166F, S167A and D168A all show significant decreases in LCAT activity of 40%-60% compared with the wild-type | ? | - |
? | |
2.3.1.43 | phosphatidylcholine + cholesterol | Homo sapiens | - |
1-acylglycerophosphocholine + cholesterol ester | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.1.43 | Homo sapiens | P04180 | gene lcat | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.3.1.43 | recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography | Homo sapiens |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.43 | additional information | structure/function requirements for the apolipoprotein A-I and lecithin cholesterol acyltransferase interaction loop of HDL, binding studies with recombinant wild/type apoA-I and apoA-I mutants P165A, Y166A, Y166E, Y166F, Y166N, S167A, D168A, Y192F, and Y192L. Loss of LCAT activation caused by apoA-I Y166A or Y166F mutations is at least partially due to the weaker binding between LCAT and apoA-I within these rHDL. Both Vmax of Y166F and Y166A are 20% lower than that of wild-type apoA-I, and the apparent Km are about 2-6fold higher than wild-type. rHDL formed with either apoA-I Y192F or Y192L mutants show normal LCAT activity. Incubation of hLCAT with rHDL formed using the apoA-I mutants P165A, Y166A, Y166F, S167A and D168A all show significant decreases in LCAT activity of 40%-60% compared with the wild-type | Homo sapiens | ? | - |
? | |
2.3.1.43 | phosphatidylcholine + cholesterol | - |
Homo sapiens | 1-acylglycerophosphocholine + cholesterol ester | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.1.43 | LCAT | - |
Homo sapiens |
2.3.1.43 | lecithin-cholesterol acyl transferase | - |
Homo sapiens |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.3.1.43 | 37 | - |
assay at | Homo sapiens |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.3.1.43 | 7.4 | - |
assay at | Homo sapiens |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.3.1.43 | physiological function | the interaction of lecithin-cholesterol acyl transferase with apolipoprotein A-I plays a critical role in high-density lipoprotein HDL maturation. A highly solvent-exposed apoA-I loop domain (L159-L170) in nascent HDL, the socalled solar flare region, and proposed it serves as an lecithin-cholesterol acyl transferase docking site | Homo sapiens |