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Literature summary for 2.3.1.43 extracted from

  • Gu, X.; Wu, Z.; Huang, Y.; Wagner, M.A.; Baleanu-Gogonea, C.; Mehl, R.A.; Buffa, J.A.; DiDonato, A.J.; Hazen, L.B.; Fox, P.L.; Gogonea, V.; Parks, J.S.; DiDonato, J.A.; Hazen, S.L.
    A systematic investigation of structure/function requirements for the apolipoprotein A-I - lecithin cholesterol acyltransferase interaction loop of HDL (2016), J. Biol. Chem., 291, 6386-6395.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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

Protein Variants

Protein Variants Comment Organism
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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 ?
-
?
phosphatidylcholine + cholesterol Homo sapiens
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1-acylglycerophosphocholine + cholesterol ester
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?

Organism

Organism UniProt Comment Textmining
Homo sapiens P04180 gene lcat
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
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?
phosphatidylcholine + cholesterol
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Homo sapiens 1-acylglycerophosphocholine + cholesterol ester
-
?

Synonyms

Synonyms Comment Organism
LCAT
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Homo sapiens
lecithin-cholesterol acyl transferase
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Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Homo sapiens

General Information

General Information Comment Organism
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