Hydrolases: The most Diverse Class of Enzymes

E. Shukla, Ameya D. Bendre, Sushama M. Gaikwad
{"title":"Hydrolases: The most Diverse Class of Enzymes","authors":"E. Shukla, Ameya D. Bendre, Sushama M. Gaikwad","doi":"10.5772/intechopen.102350","DOIUrl":null,"url":null,"abstract":"Being the largest and most diverse class of enzymes, hydrolases offer an opportunity to explore the conformational diversity which forms the basis of their differential biological functions. In recent times, there is an urge to re-evaluate and update our existing knowledge on functional and conformational transitions of these enzymes, in the context of emerging scientific trends. In this chapter, we discuss hydrolases in terms of their diversity, classification, and different nomenclature styles that exist. Further, the concepts of protein stability and significance of studying the structure–function relationship of hydrolases are mentioned in detail taking serine protease as an example. The chapter talks about multiple ways by which an enzyme’s structure and function can be explored. The available information and literature survey on hydrolases have been systematically summarized for an easy understanding. Various experimental methods and techniques involving artificial intelligence are introduced in the later sections. The knowledge obtained by these strategies contributes to our current knowledge of the interplay between the stability, structure, and function of these enzymes. This, in turn, can help in designing and engineering these proteins with improved functional and structural features toward the goal of increasing their applicability in biotechnology.","PeriodicalId":222480,"journal":{"name":"Hydrolases [Working Title]","volume":"48 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"2022-01-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"4","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Hydrolases [Working Title]","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.5772/intechopen.102350","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 4

Abstract

Being the largest and most diverse class of enzymes, hydrolases offer an opportunity to explore the conformational diversity which forms the basis of their differential biological functions. In recent times, there is an urge to re-evaluate and update our existing knowledge on functional and conformational transitions of these enzymes, in the context of emerging scientific trends. In this chapter, we discuss hydrolases in terms of their diversity, classification, and different nomenclature styles that exist. Further, the concepts of protein stability and significance of studying the structure–function relationship of hydrolases are mentioned in detail taking serine protease as an example. The chapter talks about multiple ways by which an enzyme’s structure and function can be explored. The available information and literature survey on hydrolases have been systematically summarized for an easy understanding. Various experimental methods and techniques involving artificial intelligence are introduced in the later sections. The knowledge obtained by these strategies contributes to our current knowledge of the interplay between the stability, structure, and function of these enzymes. This, in turn, can help in designing and engineering these proteins with improved functional and structural features toward the goal of increasing their applicability in biotechnology.
水解酶:最多样化的一类酶
作为最大和最多样化的酶类,水解酶提供了一个探索构象多样性的机会,这些构象多样性构成了它们差异生物学功能的基础。近年来,在新兴科学趋势的背景下,迫切需要重新评估和更新我们对这些酶的功能和构象转变的现有知识。在这一章中,我们讨论水解酶的多样性,分类和不同的命名风格存在。并以丝氨酸蛋白酶为例,详细介绍了蛋白质稳定性的概念和研究水解酶结构-功能关系的意义。本章讨论了探索酶的结构和功能的多种方法。为了便于理解,本文系统总结了有关水解酶的现有资料和文献综述。涉及人工智能的各种实验方法和技术将在后面的章节中介绍。通过这些策略获得的知识有助于我们目前对这些酶的稳定性、结构和功能之间相互作用的了解。反过来,这可以帮助设计和工程这些蛋白质具有改进的功能和结构特征,以增加其在生物技术中的适用性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信