期刊
CELL CYCLE
卷 13, 期 12, 页码 1912-1917出版社
TAYLOR & FRANCIS INC
DOI: 10.4161/cc.28761
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- A*STAR-NKTH [10/1/06/24635, IAF311010]
- A*STAR IMAGIN [IAF311011]
The transamidase subunit GAA1/GPAA1 is predicted to be the enzyme that catalyzes the attachment of the glycosylphosphatidyl (GPI) lipid anchor to the carbonyl intermediate of the substrate protein at the omega-site. Its similar to 300-amino acid residue lumenal domain is a M28 family metallo-peptide-synthetase with an alpha/beta hydrolase fold, including a central 8-strand beta-sheet and a single metal (most likely zinc) ion coordinated by 3 conserved polar residues. Phosphoethanolamine is used as an adaptor to make the non-peptide GPI lipid anchor look chemically similar to the N terminus of a peptide.
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