Expanded analyses of the functional correlations within structural classifications of glycoside hydrolases

Glycoside hydrolases (GHs) are greatly diverse in sequences and functions, but systematic studies of GH relationships based on structural information are lacking. Here, we report that GHs have multiple evolutionary origins and are structurally derived from 27 homologous superfamilies and 16 folds, b...

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Autores principales:	Dan-dan Li, Jin-lan Wang, Ya Liu, Yue-zhong Li, Zheng Zhang
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	Glycoside hydrolase Superfamily Fold Sequence–structure–function Evolution Biotechnology TP248.13-248.65
Acceso en línea:	https://doaj.org/article/ff25b11261e842b78c333cfe59f70d63
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spelling	oai:doaj.org-article:ff25b11261e842b78c333cfe59f70d632021-11-12T04:30:27ZExpanded analyses of the functional correlations within structural classifications of glycoside hydrolases2001-037010.1016/j.csbj.2021.10.039https://doaj.org/article/ff25b11261e842b78c333cfe59f70d632021-01-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S200103702100461Xhttps://doaj.org/toc/2001-0370Glycoside hydrolases (GHs) are greatly diverse in sequences and functions, but systematic studies of GH relationships based on structural information are lacking. Here, we report that GHs have multiple evolutionary origins and are structurally derived from 27 homologous superfamilies and 16 folds, but GHs are highly biased to distribute in a few superfamilies and folds. Six of these superfamilies are widely encoded by archaea, bacteria, and eukaryotes, indicating that they may be the most ancient in origin. Most superfamilies vary in enzyme function, and some, such as the superfamilies of (β/α)8-barrel and (α/α)6-barrel structures, exhibit extreme functional diversity; this is highly positively correlated with sequence diversity. More than one-third of glycosidase activities show a phenomenon of convergent evolution, especially the degradation functions of GHs on polysaccharides. The GHs of most superfamilies have relatively narrow environmental distributions, normally with the highest abundance in host-associated environments and a distribution preference for moderate low-temperature and acidic environments. Overall, our expanded analysis facilitates an understanding of complex GH sequence–structure–function relationships and may guide our screening and engineering of GHs.Dan-dan LiJin-lan WangYa LiuYue-zhong LiZheng ZhangElsevierarticleGlycoside hydrolaseSuperfamilyFoldSequence–structure–functionEvolutionBiotechnologyTP248.13-248.65ENComputational and Structural Biotechnology Journal, Vol 19, Iss , Pp 5931-5942 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Glycoside hydrolase Superfamily Fold Sequence–structure–function Evolution Biotechnology TP248.13-248.65
spellingShingle	Glycoside hydrolase Superfamily Fold Sequence–structure–function Evolution Biotechnology TP248.13-248.65 Dan-dan Li Jin-lan Wang Ya Liu Yue-zhong Li Zheng Zhang Expanded analyses of the functional correlations within structural classifications of glycoside hydrolases
description	Glycoside hydrolases (GHs) are greatly diverse in sequences and functions, but systematic studies of GH relationships based on structural information are lacking. Here, we report that GHs have multiple evolutionary origins and are structurally derived from 27 homologous superfamilies and 16 folds, but GHs are highly biased to distribute in a few superfamilies and folds. Six of these superfamilies are widely encoded by archaea, bacteria, and eukaryotes, indicating that they may be the most ancient in origin. Most superfamilies vary in enzyme function, and some, such as the superfamilies of (β/α)8-barrel and (α/α)6-barrel structures, exhibit extreme functional diversity; this is highly positively correlated with sequence diversity. More than one-third of glycosidase activities show a phenomenon of convergent evolution, especially the degradation functions of GHs on polysaccharides. The GHs of most superfamilies have relatively narrow environmental distributions, normally with the highest abundance in host-associated environments and a distribution preference for moderate low-temperature and acidic environments. Overall, our expanded analysis facilitates an understanding of complex GH sequence–structure–function relationships and may guide our screening and engineering of GHs.
format	article
author	Dan-dan Li Jin-lan Wang Ya Liu Yue-zhong Li Zheng Zhang
author_facet	Dan-dan Li Jin-lan Wang Ya Liu Yue-zhong Li Zheng Zhang
author_sort	Dan-dan Li
title	Expanded analyses of the functional correlations within structural classifications of glycoside hydrolases
title_short	Expanded analyses of the functional correlations within structural classifications of glycoside hydrolases
title_full	Expanded analyses of the functional correlations within structural classifications of glycoside hydrolases
title_fullStr	Expanded analyses of the functional correlations within structural classifications of glycoside hydrolases
title_full_unstemmed	Expanded analyses of the functional correlations within structural classifications of glycoside hydrolases
title_sort	expanded analyses of the functional correlations within structural classifications of glycoside hydrolases
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/ff25b11261e842b78c333cfe59f70d63
work_keys_str_mv	AT dandanli expandedanalysesofthefunctionalcorrelationswithinstructuralclassificationsofglycosidehydrolases AT jinlanwang expandedanalysesofthefunctionalcorrelationswithinstructuralclassificationsofglycosidehydrolases AT yaliu expandedanalysesofthefunctionalcorrelationswithinstructuralclassificationsofglycosidehydrolases AT yuezhongli expandedanalysesofthefunctionalcorrelationswithinstructuralclassificationsofglycosidehydrolases AT zhengzhang expandedanalysesofthefunctionalcorrelationswithinstructuralclassificationsofglycosidehydrolases
_version_	1718431327457378304

Expanded analyses of the functional correlations within structural classifications of glycoside hydrolases

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