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

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 wi...

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Autores principales: Eisenhaber, Birgit, Eisenhaber, Stephan, Kwang, Toh Yew, Grüber, Gerhard, Eisenhaber, Frank
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Landes Bioscience 2014
Materias:
Report
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4111754/
https://www.ncbi.nlm.nih.gov/pubmed/24743167
http://dx.doi.org/10.4161/cc.28761
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author Eisenhaber, Birgit
Eisenhaber, Stephan
Kwang, Toh Yew
Grüber, Gerhard
Eisenhaber, Frank
author_facet Eisenhaber, Birgit
Eisenhaber, Stephan
Kwang, Toh Yew
Grüber, Gerhard
Eisenhaber, Frank
author_sort Eisenhaber, Birgit
collection PubMed
description 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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spelling pubmed-41117542015-06-15 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 Grüber, Gerhard Eisenhaber, Frank Cell Cycle Report 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. Landes Bioscience 2014-06-15 2014-04-17 /pmc/articles/PMC4111754/ /pubmed/24743167 http://dx.doi.org/10.4161/cc.28761 Text en Copyright © 2014 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
spellingShingle Report
Eisenhaber, Birgit
Eisenhaber, Stephan
Kwang, Toh Yew
Grüber, Gerhard
Eisenhaber, Frank
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
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
title_full 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
title_fullStr 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
title_full_unstemmed 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
title_short 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
title_sort 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
topic Report
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4111754/
https://www.ncbi.nlm.nih.gov/pubmed/24743167
http://dx.doi.org/10.4161/cc.28761
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