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Literature summary for 2.3.1.43 extracted from

  • Manthei, K.A.; Patra, D.; Wilson, C.J.; Fawaz, M.V.; Piersimoni, L.; Shenkar, J.C.; Yuan, W.; Andrews, P.C.; Engen, J.R.; Schwendeman, A.; Ohi, M.D.; Tesmer, J.J.G.
    Structural analysis of lecithin cholesterol acyltransferase bound to high density lipoprotein particles (2020), Commun. Biol., 3, 28 .
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Homo sapiens P04180
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General Information

General Information Comment Organism
physiological function enzyme esterifies cholesterol in high density lipoprotein particles. LCAT preferentially binds to the edge of discoidal high density lipoprotein near the boundary between helix 5 and 6 of apolipoprotein ApoA-I creating a path from the lipid bilayer to the active site of LCAT. Results support for the anti-parallel double belt model of high density lipoprotein, with LCAT binding preferentially to the helix 4/6 region Homo sapiens