ProGlycProt V3.0: updated insights into prokaryotic glycoproteins and their glycosyltransferases

Janhvi, Shreya and Saini, Sikha and Singh, Vaidhvi and Sharma, Tarun Kumar and Rao, Alka (2023) ProGlycProt V3.0: updated insights into prokaryotic glycoproteins and their glycosyltransferases. Glycobiology, 34 (3). ISSN 1460-2423

Full text not available from this repository. (Request a copy)
Official URL: https://academic.oup.com/glycob/article/34/3/cwad1...

Abstract

ProGlycProt is a comprehensive database of experimentally validated information about protein glycosylation in prokaryotes, including the glycoproteins, glycosyltransferases, and their accessory enzymes. The first release of ProGlycProt featured experimentally validated information on glycoproteins only. For the second release in 2019, the size and scope of the database were expanded twofold, and experimental data on cognate glycosyltransferases and their accessory proteins was incorporated. The growing research and technology interest in microbial glycoproteins and their enzymes is evident from the steady rise in academic publications and patents in this area. Accordingly, the third update comprises a new section on patents related to glycosylation methods, novel glycosyltransferases, and technologies developed therefrom. The structure gallery is reorganized, wherein the number and quality of the models are upgraded with the help of AlphaFold2. Over the years, the influx of experimental proteomics data into public repositories like PRIDE has surged. Harnessing this legacy data for in-silico glycoprotein identification is a smart approach. Version 3.0 adds 45 N-glycoprotein entries annotated from MS datasets available on PRIDE and reviewed by independent research groups. With a 67% rise in entries corresponding to 119 genera of prokaryotes, the ProGlycProt continues to be the exclusive database of experimentally validated comprehensive information about protein glycosylation in prokaryotes.

Item Type: Article
Additional Information: The copyright of this article belongs to Oxford University Press
Uncontrolled Keywords: archaea; bacteria; glycoproteins; glycosylation; glycosyltransferase
Subjects: Q Science > QR Microbiology
Depositing User: Dr. K.P.S.Sengar
Date Deposited: 16 Jul 2024 05:00
Last Modified: 16 Jul 2024 05:00
URI: http://crdd.osdd.net/open/id/eprint/3178

Actions (login required)

View Item View Item