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

IF 3.4 3区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY
Shreya Janhvi, Shikha Saini, Vaidhvi Singh, Tarun Sharma, Alka Rao
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引用次数: 0

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.

ProGlycProt V3.0:原核生物糖蛋白及其糖基转移酶的最新见解。
ProGlycProt 是一个综合数据库,收录了经实验验证的原核生物蛋白质糖基化信息,包括糖蛋白、糖基转移酶及其附属酶。ProGlycProt的第一个版本仅提供经实验验证的糖蛋白信息。在 2019 年发布的第二个版本中,数据库的规模和范围扩大了两倍,并增加了有关同源糖基转移酶及其附属蛋白的实验数据。微生物糖蛋白及其酶的研究和技术兴趣与日俱增,这从该领域学术出版物和专利的稳步增长中可见一斑。因此,第三次更新新增了与糖基化方法、新型糖基转移酶以及由此开发的技术相关的专利部分。结构图库也进行了更新,在 AlphaFold2 的帮助下,模型的数量和质量都得到了提升。多年来,涌入 PRIDE 等公共存储库的实验蛋白质组学数据激增。利用这些遗留数据进行室内糖蛋白鉴定是一种明智的方法。3.0 版增加了 45 个 N-糖蛋白条目,这些条目是在 PRIDE 上公开的 MS 数据集中发现的,并由不同的研究小组进行了审查,从而使数据集更加完整可靠。目前的更新版对应 119 个原核生物属的条目增加了 67%,继续成为经实验验证的原核生物蛋白质糖基化综合信息的独家数据库。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
Glycobiology
Glycobiology 生物-生化与分子生物学
CiteScore
7.50
自引率
4.70%
发文量
73
审稿时长
3 months
期刊介绍: Established as the leading journal in the field, Glycobiology provides a unique forum dedicated to research into the biological functions of glycans, including glycoproteins, glycolipids, proteoglycans and free oligosaccharides, and on proteins that specifically interact with glycans (including lectins, glycosyltransferases, and glycosidases). Glycobiology is essential reading for researchers in biomedicine, basic science, and the biotechnology industries. By providing a single forum, the journal aims to improve communication between glycobiologists working in different disciplines and to increase the overall visibility of the field.
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