Literature summary for 2.3.1.43 extracted from

Casteleijn, M.G.; Parkkila, P.; Viitala, T.; Koivuniemi, A.
Interaction of lecithin cholesterol acyltransferase with lipid surfaces and apolipoprotein A-I-derived peptides (2018), J. Lipid Res., 59, 670-683 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular dynamics simulation. LCAT anchors itself to lipoprotein surfaces by utilizing nonpolar amino acids located in the membrane-binding domain and the active site tunnel opening. The membrane-anchoring hydrophobic amino acids attract cholesterol molecules next to them. The apolipoprotein A-I-derived peptides from the LCAT-activating region bind to LCAT and promote its lipid surface interactions, although some of these peptides do not bind lipids individually. The transfer free-energy of phospholipid from the lipid bilayer into the active site is consistent with the activation energy of LCAT	Homo sapiens

Crystallization (Comment)

Organism

molecular dynamics simulation. LCAT anchors itself to lipoprotein surfaces by utilizing nonpolar amino acids located in the membrane-binding domain and the active site tunnel opening. The membrane-anchoring hydrophobic amino acids attract cholesterol molecules next to them. The apolipoprotein A-I-derived peptides from the LCAT-activating region bind to LCAT and promote its lipid surface interactions, although some of these peptides do not bind lipids individually. The transfer free-energy of phospholipid from the lipid bilayer into the active site is consistent with the activation energy of LCAT

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P04180	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
commercial preparation	-	Homo sapiens	-

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Release 2023.1 (January 2023)