ArticleBMC evolutionary biology2012
Evolution, substrate specificity and subfamily classification of glycoside hydrolase family 5 (GH5).
Article in BMC evolutionary biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 238 papers.
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238 citing papers in PubMed.
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- Genomic and transcriptomic insights into Trichomonascus vanleenenianus, a xylan-degrading yeast isolated from saproxylic insect larvae.BMC genomics · 2026Article
- Catalyzing Carbohydrate Cleavage: Glycosidases and Their Mechanisms.Chemical reviews · 2026Review
- Dual-Activity Mannosyltransferase Phosphorylases in Family 130 of Glycoside Hydrolases.ACS catalysis · 2026Article
- Deletion of theeLife · 2026Article
- Expression and characterization of an endo-β-1,6-galactanase from Arabidopsis thaliana.The Biochemical journal · 2025Article
- Article
- Soil microbial adaptation to carbon deprivation: shifts in lignocellulolytic gene profiles following long-term plant exclusion.Environmental microbiome · 2025Article
- Cloning and Characterization of the Novel Endoglucanase Identified in Deep Subsurface Thermal Well of Biragzang (North Ossetia) by Metagenomic Analysis.Biomolecules · 2025Article
- High-quality genome assembly and annotation of Porodaedalea mongolica and Porodaedalea schrenkiana provide insights into potential industrial and medical application.G3 (Bethesda, Md.) · 2025Article
- Characterization of a Rice GH5_11 Gene Associated with Endosperm and Seed Traits.Plants (Basel, Switzerland) · 2025Article
- Structural and biochemical basis for activity of Aspergillus nidulans α-1,3-glucanases from glycoside hydrolase family 71.Communications biology · 2025Article
- Artificial cellulose derivatives are metabolized by select human gut Bacteroidota upon priming with common plant β-glucans.Journal of bacteriology · 2025Article
178 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe large Glycoside Hydrolase family 5 (GH5) groups together a wide range of enzymes acting on β-linked oligo- and polysaccharides, and glycoconjugates from a large spectrum of organisms. The long and complex evolution of this family of enzymes and its broad sequence diversity limits functional prediction. With the objective of improving the differentiation of enzyme specificities in a knowledge-based context, and to obtain new evolutionary insights, we present here a new, robust subfamily classification of family GH5.
resultsAbout 80% of the current sequences were assigned into 51 subfamilies in a global analysis of all publicly available GH5 sequences and associated biochemical data. Examination of subfamilies with catalytically-active members revealed that one third are monospecific (containing a single enzyme activity), although new functions may be discovered with biochemical characterization in the future. Furthermore, twenty subfamilies presently have no characterization whatsoever and many others have only limited structural and biochemical data. Mapping of functional knowledge onto the GH5 phylogenetic tree revealed that the sequence space of this historical and industrially important family is far from well dispersed, highlighting targets in need of further study. The analysis also uncovered a number of GH5 proteins which have lost their catalytic machinery, indicating evolution towards novel functions.
conclusionOverall, the subfamily division of GH5 provides an actively curated resource for large-scale protein sequence annotation for glycogenomics; the subfamily assignments are openly accessible via the Carbohydrate-Active Enzyme database at http://www.cazy.org/GH5.html.
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