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Literature summary for 2.3.1.43 extracted from

  • Spahr, C.; Kim, J.J.; Deng, S.; Kodama, P.; Xia, Z.; Tang, J.; Zhang, R.; Siu, S.; Nuanmanee, N.; Estes, B.; Stevens, J.; Zhou, M.; Lu, H.S.
    Recombinant human lecithin-cholesterol acyltransferase Fc fusion: analysis of N- and O-linked glycans and identification and elimination of a xylose-based O-linked tetrasaccharide core in the linker region (2013), Protein Sci., 22, 1739-1753.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
additional information 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 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P04180 gene lcat
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Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein 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. Recombinant human lecithin-cholesterol acyltransferase Fc fusion chimeric protein 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. E416 (the C-terminus of LCAT) combined with the linker sequence is likely serving as a substrate for peptide O-xylosyltransferase Homo sapiens

Synonyms

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