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Cell Cycle. 2014;13(12):1912-7. doi: 10.4161/cc.28761. Epub 2014 Apr 17.

Transamidase subunit GAA1/GPAA1 is a M28 family metallo-peptide-synthetase that catalyzes the peptide bond formation between the substrate protein's omega-site and the GPI lipid anchor's phosphoethanolamine.

Author information

1
Bioinformatics Institute (BII); A*STAR; Singapore, Republic of Singapore.
2
Department of Physical Chemistry; University of Vienna; Wien/Vienna, Republic of Austria.
3
Bioinformatics Institute (BII); A*STAR; Singapore, Republic of Singapore; Nanyang Technological University; School of Biological Sciences; Singapore, Republic of Singapore.
4
Bioinformatics Institute (BII); A*STAR; Singapore, Republic of Singapore; Department of Biological Sciences (DBS); National University of Singapore (NUS); Singapore, Republic of Singapore; School of Computer Engineering (SCE); Nanyang Technological University (NTU); Singapore, Republic of Singapore.

Abstract

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 ω-site. Its ~300-amino acid residue lumenal domain is a M28 family metallo-peptide-synthetase with an α/β hydrolase fold, including a central 8-strand β-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.

KEYWORDS:

GAA1; GPAA1; GPI lipid anchor; GPI transamidase; M28 peptidase; metallo-peptide-synthetase; protein sequence; sequence analysis

PMID:
24743167
PMCID:
PMC4111754
DOI:
10.4161/cc.28761
[Indexed for MEDLINE]
Free PMC Article

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