基因组
功能多样性
计算生物学
多样性(政治)
生物
进化生物学
生态学
遗传学
基因
人类学
社会学
作者
Tomoki Sumida,Satoshi Hiraoka,Keiko Usui,Akihiro Ishiwata,Toru Sengoku,Keith A. Stubbs,Katsunori Tanaka,Shigeru Deguchi,Shinya Fushinobu,Takuro Nunoura
标识
DOI:10.1038/s41467-024-47653-2
摘要
Abstract β- N -Acetylgalactosamine-containing glycans play essential roles in several biological processes, including cell adhesion, signal transduction, and immune responses. β- N -Acetylgalactosaminidases hydrolyze β- N -acetylgalactosamine linkages of various glycoconjugates. However, their biological significance remains ambiguous, primarily because only one type of enzyme, exo-β- N -acetylgalactosaminidases that specifically act on β- N -acetylgalactosamine residues, has been documented to date. In this study, we identify four groups distributed among all three domains of life and characterize eight β- N -acetylgalactosaminidases and β- N -acetylhexosaminidase through sequence-based screening of deep-sea metagenomes and subsequent searching of public protein databases. Despite low sequence similarity, the crystal structures of these enzymes demonstrate that all enzymes share a prototype structure and have diversified their substrate specificities (oligosaccharide-releasing, oligosaccharide/monosaccharide-releasing, and monosaccharide-releasing) through the accumulation of mutations and insertional amino acid sequences. The diverse β- N -acetylgalactosaminidases reported in this study could facilitate the comprehension of their structures and functions and present evolutionary pathways for expanding their substrate specificity.
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