Molecular mechanism of lytic polysaccharide monooxygenases
Author:
Affiliation:
1. Department of Theoretical Chemistry
2. Lund University
3. Lund
4. Sweden
Abstract
The lytic polysaccharide monooxygenases (LPMOs) are copper metalloenzymes that can enhance polysaccharide depolymerization through an oxidative mechanism and hence boost generation of biofuel from e.g. cellulose. By employing density functional theory in a combination of quantum mechanics and molecular mechanics (QM/MM), we report a complete description of the molecular mechanism of LPMOs.
Funder
Vetenskapsrådet
Carlsbergfondet
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2018/SC/C8SC00426A
Reference73 articles.
1. Harnessing energy from plant biomass
2. Biomass Recalcitrance: Engineering Plants and Enzymes for Biofuels Production
3. The First Structure of a Glycoside Hydrolase Family 61 Member, Cel61B from Hypocrea jecorina, at 1.6 Å Resolution
4. Stimulation of Lignocellulosic Biomass Hydrolysis by Proteins of Glycoside Hydrolase Family 61: Structure and Function of a Large, Enigmatic Family
5. An Oxidative Enzyme Boosting the Enzymatic Conversion of Recalcitrant Polysaccharides
Cited by 81 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. On the pH Dependency of the Catalysis by a Lytic Polysaccharide Monooxygenase from the Fungus Trichoderma reesei;ACS Catalysis;2024-08-23
2. Impact of the Copper Second Coordination Sphere on Catalytic Performance and Substrate Specificity of a Bacterial Lytic Polysaccharide Monooxygenase;ACS Omega;2024-05-15
3. Mutational dissection of a hole hopping route in a lytic polysaccharide monooxygenase (LPMO);Nature Communications;2024-05-10
4. The rotamer of the second-sphere histidine in AA9 lytic polysaccharide monooxygenase is pH dependent;Biophysical Journal;2024-05
5. Coordination and hydrogen bonding diversity of OOH ligand in crystalline organoelement and inorganic hydroperoxides;Mendeleev Communications;2024-03
1.学者识别学者识别
2.学术分析学术分析
3.人才评估人才评估
"同舟云学术"是以全球学者为主线，采集、加工和组织学术论文而形成的新型学术文献查询和分析系统，可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容，当前同舟云学术共收录了国内外主流学术期刊6万余种，收集的期刊论文及会议论文总量共计约1.5亿篇，并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询！咨询电话：010-8811{复制后删除}0370
www.globalauthorid.com
TOP
Copyright © 2019-2024 北京同舟云网络信息技术有限公司 京公网安备11010802033243号 京ICP备18003416号-3