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Literature summary for 2.3.1.43 extracted from

  • Glukhova, A.; Hinkovska-Galcheva, V.; Kelly, R.; Abe, A.; Shayman, J.A.; Tesmer, J.J.
    Structure and function of lysosomal phospholipase A2 and lecithin:cholesterol acyltransferase (2015), Nat. Commun., 6, 6250.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.43

Application

Application Comment Organism
drug development rational development of therapeutics to treat enzyme LCAT deficiency, atherosclerosis and acute coronary syndrome Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
lysosome
-
 Homo sapiens 5764
-

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
LCAT
-
 Homo sapiens
lecithin:cholesterol acyltransferase
-
 Homo sapiens

General Information

General Information Comment Organism
evolution lysosomal phospholipase A2 (LPLA2) and lecithin:cholesterol acyltransferase (LCAT) belong to a structurally uncharacterized family of key lipid-metabolizing enzymes responsible for lung surfactant catabolism and for reverse cholesterol transport, respectively. LCAT has a close structural relationship to LPLA2, construction of an LPLA2-based homology model corresponding to the catalytic, membrane binding and cap domains of LCAT, structure comparisons, overview. Lys202 in the alpha3 helix and Thr329 in the catalytic domain are invariant in LPLA2 and LCAT, but are conserved as hydrophobic residues in bacterial lipases. Although LPLA2 exhibits structural homology with bacterial lipases, their substrates are fundamentally different in that LPLA2 and LCAT hydrolyse glycerophospholipids, which contain polar, charged head groups, instead of triacylglycerol Homo sapiens
malfunction enzyme mutations and loss of enzyme activity are involved in several diseases, e.g. atherosclerosis and acute coronary syndrome Homo sapiens