Molecular cloning of a phospholipid-cholesterol acyltransferase from Aeromonas hydrophila. Sequence homologies with lecithin-cholesterol acyltransferase and other lipases.
We have determined the nucleotide sequence of a gene encoding Aeromonas hydrophila phospholipid-cholesterol acyltransferase, an enzyme which shares many properties with mammalian lecithin:cholesterol acyltransferase. The derived amino acid sequence of the protein contains two regions which are homologous to the proposed active sites and binding sites of the plasma acyltransferase and to similar sequences in other interfacially acting lipolytic enzymes. The amino terminus is preceded by a typical 18 amino acid signal sequence. The protein, which is released into the culture supernatant by Aeromonas hydrophila, is confined to the periplasm of Escherichia coli.
Thornton
J
J
Department of Biochemistry and Microbiology, University of Victoria, Canada.
Howard
S P
SP
Buckley
J T
JT
D000217:Acyltransferases / Q000235:genetics*; D000333:Aeromonas / Q000201:enzymology / Q000235:genetics*; D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004926:Escherichia coli; D008049:Lipase / Q000235:genetics; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid; D002785:Sterol O-Acyltransferase / Q000235:genetics*
D000217:Acyltransferases; C020597:glycerophospholipid-cholesterol acyltransferase; D002785:Sterol O-Acyltransferase; D008049:Lipase