Natural mutations of apolipoprotein A-I impairing activation of lecithin:cholesterol acyltransferase.
Five natural mutations of apolipoprotein A-I (apoA-I), apoA-I(A95D), apoA-I(Y100H), apoA-I(E110K), apoA-I(V156E) and apoA-I(H162Q), were studied for their ability to activate lecithin:cholesterol acyltransferase (LCAT). Mutants apoA-I(E110K), apoA-I(V156E) and apoA-I(H162Q) had an impaired ability to activate LCAT. Combined with data on other apoA-I mutants this finding is consistent with the idea that the central region between amino acids 110 and 160 is likely to be the "active site" of apoA-I involved in the interaction with LCAT and that a specific sequence of apoA-I is required for activation of the enzyme.
Hoang
Anh
A
Wynn Domain, Baker Medical Research Institute, PO Box 6492 St Kilda Rd Central, Melbourne Vic 8008, Australia.
Huang
Wei
W
Sasaki
Jun
J
Sviridov
Dmitri
D
D000595:Amino Acid Sequence; D016632:Apolipoprotein A-I / Q000737:chemistry / Q000235:genetics* / Q000494:pharmacology; D001665:Binding Sites; D004305:Dose-Response Relationship, Drug; D004789:Enzyme Activation / Q000187:drug effects; D006801:Humans; D009154:Mutation; D007862:Phosphatidylcholine-Sterol O-Acyltransferase / Q000378:metabolism*; D017354:Point Mutation
D016632:Apolipoprotein A-I; D007862:Phosphatidylcholine-Sterol O-Acyltransferase