인문학
사회과학
자연과학
공학
의약학
농수해양학
예술체육학
복합학
DBpia AI
AI 에이전트
AI 아이디어
AI 리더
AI 뷰어
Citeasy
크롬 서지관리 다운로드
지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
초록·키워드
The microbial polysaccharide α-1,3-glucan is an important component of fungal cell walls and dental plaque biofilms, contributing to microbial virulence and biofilm resilience. Glycoside hydrolase family 71 (GH71) includes α-1,3-glucan degrading enzymes which could be exploited for biotechnological applications; however, the family is presently poorly understood. To increase our understanding of GH71, we have performed a phylogenetic analysis of the family and detailed biochemical analysis of two of the five GH71 enzymes encoded by Aspergillus nidulans (AnGH71B and -C). Both are active on soluble α-1,3-glucooligosaccharides but surprisingly only minimally on water-insoluble α-1,3-glucan. Assays on intact and milled A. nidulans biomass indicate that the enzymes act on fungal cell wall glycosidic linkages, likely having roles in cell wall remodelling. Both enzymes utilize an inverting mechanism but differ in specificity and product profiles indicating exo- and endo-like activity for AnGH71B and AnGH71C, respectively. We present the first structure of a GH71 protein, AnGH71C, including structures with carbohydrate ligands. These structures revealed a conserved acidic dyad (DxxE), found to be crucial for activity, and active site water coordination consistent with a classical inverting GH mechanism. This work provides new insights into GH71, highlighting its functional diversity and the enzymes roles in fungal physiology.
인공지능 문자 인식 모델을 통해 추출된 텍스트로, 일부 오타나 오류가 포함될 수 있으나 지속적으로 개선 중입니다.
오류를 발견하셨다면 해당 부분을 드래그한 후 ' 를 통해 신고해주세요.
오류를 발견하셨다면 해당 부분을 드래그한 후 ' 를 통해 신고해주세요.
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