| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 262, Issue 7, 3086-3091, 03, 1987
CY Yang, D Manoogian, Q Pao, FS Lee, RD Knapp, AM Gotto Jr and HJ Pownall
The amino acid sequence of human lecithin:cholesterol acyltransferase has
been determined by degradation and alignment of peptides obtained from
tryptic and staphylococcal digestions and the cleavage with cyanogen
bromide and consisted of 416 amino acid residues. All of the tryptic
peptides of lecithin:cholesterol acyltransferase were isolated and
sequenced. Peptides resulting from digestion by staphylococcal protease,
cyanogen bromide cleavage, or the combination of the two methods were
employed to find overlapping segments. The N terminus of human
lecithin:cholesterol acyltransferase was determined to be phenylalanine by
sequencing the whole protein up to 40 residues while the C terminus was
identified as glutamic acid through carboxypeptidase Y cleavage. Cys50 and
Cys74 and Cys313 and Cys356 were identified as the two disulfide bridges
while the free sulfhydryl groups were located at positions 31 and 184. The
N-glycosylated sites of the protein were assigned to asparagines at
positions 20, 84, 272, and 384. The active site of lecithin:cholesterol
acyltransferase was identified as serine on position 181 according to its
homology with other serine-type esterases which have a common structure of
glycine-variable amino acid- active serine-variable amino acid-glycine
(Gly-X-Ser-X-Gly) with the variable amino acids disrupting the homology. No
long internal repeats or homologies with apolipoproteins were found. The
secondary structure is consistent with the results of predictive
algorithms. A simple model of the enzyme is proposed on the basis of
available chemical data and predictive methods.
Lecithin:cholesterol acyltransferase. Functional regions and a structural model of the enzyme
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  M. Hiraoka, A. Abe, and J. A. Shayman Structure and function of lysosomal phospholipase A2: identification of the catalytic triad and the role of cysteine residues J. Lipid Res., November 1, 2005; 46(11): 2441 - 2447. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
K. Kobori, K. Saito, S. Ito, K. Kotani, M. Manabe, and T. Kanno A new enzyme-linked immunosorbent assay with two monoclonal antibodies to specific epitopes measures human lecithin-cholesterol acyltransferase J. Lipid Res., February 1, 2002; 43(2): 325 - 334. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. Ruiz, M. H. Kuehn, J. L. Andorf, E. Stone, G. S. Hageman, and D. Bok Genomic Organization and Mutation Analysis of the Gene Encoding Lecithin Retinol Acyltransferase in Human Retinal Pigment Epithelium Invest. Ophthalmol. Vis. Sci., January 1, 2001; 42(1): 31 - 37. [Abstract] [Full Text]
|
|
|
|
|
|
J. W. Chisholm, A. K. Gebre, and J. S. Parks Characterization of C-terminal histidine-tagged human recombinant lecithin:cholesterol acyltransferase J. Lipid Res., August 1, 1999; 40(8): 1512 - 1519. [Abstract] [Full Text]
|
|
|
|
 |
|
 F. Peelman, B. Vanloo, O. Perez-Mendez, A. Decout, J.-L. Verschelde, C. Labeur, N. Vinaimont, A. Verhee, N. Duverger, R. Brasseur, et al. Characterization of functional residues in the interfacial recognition domain of lecithin cholesterol acyltransferase (LCAT) Protein Eng. Des. Sel., January 1, 1999; 12(1): 71 - 78. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
G. Argyropoulos, A. Jenkins, R. L. Klein, T. Lyons, B. Wagenhorst, J. St. Armand, S. M. Marcovina, J. J. Albers, P. H. Pritchard, and W. T. Garvey Transmission of two novel mutations in a pedigree with familial lecithin:cholesterol acyltransferase deficiency: structure–function relationships and studies in a compound heterozygous proband J. Lipid Res., September 1, 1998; 39(9): 1870 - 1876. [Abstract] [Full Text]
|
|
|
|
|
|
A. G. Lacko, A. J. Reason, C. Nuckolls, B. J. Kudchodkar, M. P. Nair, G. Sundarrajan, P. H. Pritchard, H. R. Morris, and A. Dell Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties J. Lipid Res., April 1, 1998; 39(4): 807 - 820. [Abstract] [Full Text]
|
|
|
|
 |
|
 H.E. Miettinen, H. Gylling, J. Tenhunen, J. Virtamo, M. Jauhiainen, J.K. Huttunen, I. Kantola, T.A. Miettinen, and K. Kontula Molecular Genetic Study of Finns With Hypoalphalipoproteinemia and Hyperalphalipoproteinemia : A Novel Gly230Arg Mutation (LCATFin) of Lecithin:Cholesterol Acyltransferase (LCAT) Accounts for 5% of Cases With Very Low Serum HDL Cholesterol Levels Arterioscler. Thromb. Vasc. Biol., April 1, 1998; 18(4): 591 - 598. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. Wang, J. A. DeLozier, A. K. Gebre, P. J. Dolphin, and J. S. Parks Role of glutamic acid residues 154, 155, and 165 of lecithin:cholesterol acyltransferase in cholesterol esterification and phospholipase A2 activities J. Lipid Res., January 1, 1998; 39(1): 51 - 58. [Abstract] [Full Text]
|
|
|
|
 |
|
 H.-G. Klein, N. Duverger, J. J. Albers, S. Marcovina, H. B. Brewer Jr., and S. Santamarina-Fojo In Vitro Expression of Structural Defects in the Lecithin-Cholesterol Acyltransferase Gene J. Biol. Chem., April 21, 1995; 270(16): 9443 - 9447. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
H. Miettinen, H. Gylling, I. Ulmanen, T. A. Miettinen, and K. Kontula Two Different Allelic Mutations in a Finnish Family With Lecithin:Cholesterol Acyltransferase Deficiency Arterioscler. Thromb. Vasc. Biol., April 1, 1995; 15(4): 460 - 467. [Abstract] [Full Text]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
