Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Genome-Wide Analysis of Whole Human Glycoside Hydrolases by Data-Driven Analysis in Silico

Version 1 : Received: 20 November 2019 / Approved: 21 November 2019 / Online: 21 November 2019 (04:46:13 CET)

A peer-reviewed article of this Preprint also exists.

Nakamura, T.; Fahmi, M.; Tanaka, J.; Seki, K.; Kubota, Y.; Ito, M. Genome-Wide Analysis of Whole Human Glycoside Hydrolases by Data-Driven Analysis in Silico. Int. J. Mol. Sci. 2019, 20, 6290. Nakamura, T.; Fahmi, M.; Tanaka, J.; Seki, K.; Kubota, Y.; Ito, M. Genome-Wide Analysis of Whole Human Glycoside Hydrolases by Data-Driven Analysis in Silico. Int. J. Mol. Sci. 2019, 20, 6290.

Journal reference: Int. J. Mol. Sci. 2019, 20, 6290
DOI: 10.3390/ijms20246290

Abstract

Glycans are involved in various metabolic processes via the functions of glycosyltransferases and glycoside hydrolases. Analysing the evolution of these enzymes is essential for improving the understanding of glycan metabolism and function. Based on our previous study of glycosyltransferases, we performed a genome-wide analysis of whole human glycoside hydrolases using the UniProt, BRENDA, CAZy, and KEGG databases. Using cluster analysis, 319 human glycoside hydrolases were classified into four clusters based on their similarity to enzymes conserved in chordates or metazoans (Class 1), metazoans (Class 2), metazoans and plants (Class 3), and eukaryotes (Class 4). The eukaryote and metazoan clusters included N- and O-glycoside hydrolases, respectively. The significant abundance of disordered regions within the most conserved cluster indicated a role for disordered regions in the evolution of glycoside hydrolases. These results suggest that the biological diversity of multicellular organisms is related to the acquisition of N- and O-linked glycans.

Subject Areas

glycoside hydrolase; glycan; phylogenetic profiling

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