EC Number   |
Protein Variants |
Reference |
|---|
   2.3.1.43 | C31Y |
site-directed mutagenesis, the mutation renders the enzyme more stable and active than the native form |
737191 |
| 2.3.1.43 | C31Y |
the mutant has an about 10fold higher cholesterol esterification activity compared with wild type |
757166 |
| 2.3.1.43 | E149A |
site-directed mutagenesis, mutation alters the human enzyme residue to the corresponding residue of the rat sequence, 2.9fold increased cholesteryl ester formation activity, 5.5fold increased phospholipase A2 activity in the mutant compared to the wild-type enzyme |
661064 |
| 2.3.1.43 | E149A/Y292H/W294F |
site-directed mutagenesis, mutation alters the human enzyme residues to the corresponding residues of the rat sequence, increased cholesteryl ester formation activity and phospholipase A2 activity with 1-palmitoyl-2-20:4-sn-glycero-3-phosphocholine, decreased activities with 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine compared to the wild-type enzyme |
661064 |
| 2.3.1.43 | more |
a frameshift mutation, insertion of an adenine identified at codon 178 generating a Tsp 509 I restriction site, s AATT, in exon 5 of the LCAT gene is associated with renal failure with proteinuria, corneal opacity, and anemia in familial LCAT deficiency |
673128 |
| 2.3.1.43 | more |
construction of a recombinant human lecithin-cholesterol acyltransferase Fc fusion (huLCAT-Fc), a chimeric protein produced by fusing human Fc to the C-terminus of the human enzyme via a linker sequence. The huLCAT-Fc homodimer contains five N-linked glycosylation sites per monomer. The heterogeneity and site-specific distribution of the various glycans are examined using enzymatic digestion and LC-MS/MS, followed by automatic processing. Almost all of the N-linked glycans in human LCAT are fucosylated and sialylated. The predominant LCAT N-linked glycoforms are biantennary glycans, followed by triantennary sugars, whereas the level of tetraantennary glycans is much lower. Glycans at the Fc N-linked site exclusively contain typical asialobiantennary structures. HuLCAT-Fc is also confirmed to have mucin-type glycans attached at T407 and S409. When LCAT-Fc fusions are constructed using a G-S-G-G-G-G linker, an unexpected 1632 Da xylose-based glycosaminoglycan (GAG) tetrasaccharide core of Xyl-Gal-Gal-GlcA is attached to S418. Several minor intermediate species including Xyl, Xyl-Gal, Xyl-Gal-Gal, and a phosphorylated GAG core are also present. GAG incorporation can be eliminated through engineering by shifting the linker Ser residue downstream in the linker sequence |
737203 |
| 2.3.1.43 | more |
construction of enzyme knockout and overexpressing strains, the loss of TgLCAT expression leads to an egress defect, and its overexpression confers an egress advantage, phenotype, overview |
-, 736505 |
| 2.3.1.43 | more |
deleterious LCAT mutants show low HDL-cholesterol levels |
705010 |
| 2.3.1.43 | more |
deletion of the first residue of the enzyme's N-terminus lead to 95% reduced alpha-enzyme activity and slightly increased beta-enzyme activity, deletion of the first 2 residues lead to abolished alpha-enzyme activity and reduced beta-enzyme activity, respectively, but the mutant enzymes are still able to bind the substrates, mutants with deletion of 3-5 N-terminal residues show no alpha-enzyme activity and residual or no beta-enzyme activity, overview |
661231 |
| 2.3.1.43 | more |
enzyme deficiency phenotypes, overview. Generation of transgenic mice, monkeys, or rabbits overexpressing the human LCAT |
703346 |
