A trimodular bacterial enzyme combining hydrolytic activity with oxidative glycosidic bond cleavage efficiently degrades chitin

甲壳素 糖苷键 几丁质酶 糖苷水解酶 多糖 生物化学 水解 化学 生物 壳聚糖
作者
Sophanit Mekasha,Tina R. Tuveng,Fatemeh Askarian,Swati Choudhary,Claudia Schmidt‐Dannert,Axel Niebisch,Jan Modregger,Gustav Vaaje‐Kolstad,Vincent G. H. Eijsink
出处
期刊:Journal of Biological Chemistry [Elsevier BV]
卷期号:295 (27): 9134-9146 被引量:26
标识
DOI:10.1074/jbc.ra120.013040
摘要

Findings from recent studies have indicated that enzymes containing more than one catalytic domain may be particularly powerful in the degradation of recalcitrant polysaccharides such as chitin and cellulose. Some known multicatalytic enzymes contain several glycoside hydrolase domains and one or more carbohydrate-binding modules (CBMs). Here, using bioinformatics and biochemical analyses, we identified an enzyme, Jd1381 from the actinobacterium Jonesia denitrificans, that uniquely combines two different polysaccharide-degrading activities. We found that Jd1381 contains an N-terminal family AA10 lytic polysaccharide monooxygenase (LPMO), a family 5 chitin-binding domain (CBM5), and a family 18 chitinase (Chi18) domain. The full-length enzyme, which seems to be the only chitinase produced by J. denitrificans, degraded both α- and β-chitin. Both the chitinase and the LPMO activities of Jd1381 were similar to those of other individual chitinases and LPMOs, and the overall efficiency of chitin degradation by full-length Jd1381 depended on its chitinase and LPMO activities. Of note, the chitin-degrading activity of Jd1381 was comparable with or exceeded the activities of combinations of well-known chitinases and an LPMO from Serratia marcescens Importantly, comparison of the chitinolytic efficiency of Jd1381 with the efficiencies of combinations of truncated variants-JdLPMO10 and JdCBM5-Chi18 or JdLPMO10-CBM5 and JdChi18-indicated that optimal Jd1381 activity requires close spatial proximity of the LPMO10 and the Chi18 domains. The demonstration of intramolecular synergy between LPMOs and hydrolytic enzymes reported here opens new avenues toward the development of efficient catalysts for biomass conversion.
最长约 10秒,即可获得该文献文件

科研通智能强力驱动
Strongly Powered by AbleSci AI
更新
PDF的下载单位、IP信息已删除 (2025-6-4)

科研通是完全免费的文献互助平台,具备全网最快的应助速度,最高的求助完成率。 对每一个文献求助,科研通都将尽心尽力,给求助人一个满意的交代。
实时播报
kkmedici关注了科研通微信公众号
刚刚
爱听歌的树叶完成签到,获得积分10
1秒前
2秒前
不宁不令完成签到,获得积分10
3秒前
圆滚滚完成签到,获得积分10
4秒前
5秒前
唐_完成签到,获得积分10
6秒前
桐桐应助彳亍而行采纳,获得10
6秒前
7秒前
qiqi发布了新的文献求助10
7秒前
8秒前
JUdy完成签到,获得积分10
9秒前
lll完成签到,获得积分10
10秒前
10秒前
10秒前
小艾完成签到,获得积分10
11秒前
英姑应助含糊采纳,获得10
11秒前
柒月小鱼完成签到 ,获得积分10
11秒前
奋斗雁山发布了新的文献求助10
11秒前
11秒前
12秒前
这样很OK发布了新的文献求助10
12秒前
tay完成签到,获得积分20
15秒前
韦谷兰发布了新的文献求助10
16秒前
QQQ发布了新的文献求助10
16秒前
Bio应助哈哈采纳,获得30
16秒前
17秒前
17秒前
kkmedici发布了新的文献求助30
17秒前
叮咚完成签到,获得积分10
18秒前
不想完成签到,获得积分10
18秒前
这样很OK完成签到,获得积分10
19秒前
GXWFDC完成签到,获得积分10
19秒前
西瓜汁完成签到,获得积分10
19秒前
Lisa完成签到,获得积分20
20秒前
含糊发布了新的文献求助10
21秒前
QQQ完成签到,获得积分10
21秒前
21秒前
22秒前
23秒前
高分求助中
A new approach to the extrapolation of accelerated life test data 1000
ACSM’s Guidelines for Exercise Testing and Prescription, 12th edition 500
‘Unruly’ Children: Historical Fieldnotes and Learning Morality in a Taiwan Village (New Departures in Anthropology) 400
Indomethacinのヒトにおける経皮吸収 400
Phylogenetic study of the order Polydesmida (Myriapoda: Diplopoda) 370
基于可调谐半导体激光吸收光谱技术泄漏气体检测系统的研究 350
Robot-supported joining of reinforcement textiles with one-sided sewing heads 320
热门求助领域 (近24小时)
化学 材料科学 医学 生物 工程类 有机化学 生物化学 物理 内科学 纳米技术 计算机科学 化学工程 复合材料 遗传学 基因 物理化学 催化作用 冶金 细胞生物学 免疫学
热门帖子
关注 科研通微信公众号,转发送积分 3988838
求助须知:如何正确求助?哪些是违规求助? 3531250
关于积分的说明 11252914
捐赠科研通 3269838
什么是DOI,文献DOI怎么找? 1804820
邀请新用户注册赠送积分活动 881943
科研通“疑难数据库(出版商)”最低求助积分说明 809028