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

Birgit Eisenhaber; Stephan Eisenhaber; Toh Yew Kwang; Gerhard Grub̈er; Frank Eisenhaber

doi:10.4161/cc.28761

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

Birgit Eisenhaber, Stephan Eisenhaber, Toh Yew Kwang, Gerhard Grub̈er, Frank Eisenhaber^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

44 Citations (Scopus)

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.

Original language	English
Pages (from-to)	1912-1917
Number of pages	6
Journal	Cell Cycle
Volume	13
Issue number	12
DOIs	https://doi.org/10.4161/cc.28761
Publication status	Published - Jun 15 2014
Externally published	Yes

ASJC Scopus Subject Areas

Molecular Biology
Developmental Biology
Cell Biology

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title = "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",

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.",

author = "Birgit Eisenhaber and Stephan Eisenhaber and Kwang, {Toh Yew} and Gerhard Gru{\"b}er and Frank Eisenhaber",

year = "2014",

month = jun,

day = "15",

doi = "10.4161/cc.28761",

language = "English",

volume = "13",

pages = "1912--1917",

journal = "Cell Cycle",

issn = "1538-4101",

publisher = "Landes Bioscience",

number = "12",

}

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. / Eisenhaber, Birgit; Eisenhaber, Stephan; Kwang, Toh Yew et al.
In: Cell Cycle, Vol. 13, No. 12, 15.06.2014, p. 1912-1917.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

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AU - Eisenhaber, Birgit

AU - Eisenhaber, Stephan

AU - Kwang, Toh Yew

AU - Grub̈er, Gerhard

AU - Eisenhaber, Frank

PY - 2014/6/15

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AB - 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.

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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

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