• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验

铜基脂肪酶在木质纤维素类多糖向单糖转化过程中对氧的活化作用。

Oxygen Activation by Cu LPMOs in Recalcitrant Carbohydrate Polysaccharide Conversion to Monomer Sugars.

机构信息

Department of Chemistry , Stanford University , Stanford , California 94305 , United States.

DuPont Industrial Biosciences , 925 Page Mill Road , Palo Alto , California 94304 , United States.

出版信息

Chem Rev. 2018 Mar 14;118(5):2593-2635. doi: 10.1021/acs.chemrev.7b00421. Epub 2017 Nov 20.

DOI:10.1021/acs.chemrev.7b00421
PMID:29155571
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5982588/
Abstract

Natural carbohydrate polymers such as starch, cellulose, and chitin provide renewable alternatives to fossil fuels as a source for fuels and materials. As such, there is considerable interest in their conversion for industrial purposes, which is evidenced by the established and emerging markets for products derived from these natural polymers. In many cases, this is achieved via industrial processes that use enzymes to break down carbohydrates to monomer sugars. One of the major challenges facing large-scale industrial applications utilizing natural carbohydrate polymers is rooted in the fact that naturally occurring forms of starch, cellulose, and chitin can have tightly packed organizations of polymer chains with low hydration levels, giving rise to crystalline structures that are highly recalcitrant to enzymatic degradation. The topic of this review is oxidative cleavage of carbohydrate polymers by lytic polysaccharide mono-oxygenases (LPMOs). LPMOs are copper-dependent enzymes (EC 1.14.99.53-56) that, with glycoside hydrolases, participate in the degradation of recalcitrant carbohydrate polymers. Their activity and structural underpinnings provide insights into biological mechanisms of polysaccharide degradation.

摘要

天然碳水化合物聚合物,如淀粉、纤维素和几丁质,作为燃料和材料的来源,可以替代化石燃料,提供可再生资源。因此,人们对其转化为工业用途的兴趣相当大,这从这些天然聚合物衍生产品的现有和新兴市场就可以证明。在许多情况下,这是通过使用酶将碳水化合物分解为单体糖的工业过程来实现的。利用天然碳水化合物聚合物的大规模工业应用所面临的主要挑战之一源于这样一个事实,即天然存在的淀粉、纤维素和几丁质形式可能具有聚合物链紧密堆积的组织和低水合水平,导致对酶降解具有高度抗性的结晶结构。本文综述的主题是通过溶菌多糖单加氧酶(LPMO)对碳水化合物聚合物进行氧化裂解。LPMO 是依赖铜的酶(EC 1.14.99.53-56),与糖苷水解酶一起参与难降解碳水化合物聚合物的降解。它们的活性和结构基础为多糖降解的生物学机制提供了深入了解。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/a4318ef5a1fb/nihms969912f36.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/469f5615f422/nihms969912f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/b316d1dd65bd/nihms969912f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/76d54681f5b9/nihms969912f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/2640f837f949/nihms969912f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/0893af044427/nihms969912f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/6c080f14ec74/nihms969912f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/a92d49e239e8/nihms969912f7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/240553dbadf7/nihms969912f8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/c39fde8e5e41/nihms969912f9.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/58d517ae08b3/nihms969912f10.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/e6c25622d14a/nihms969912f11.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/db87603df949/nihms969912f12.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/a07796ab0f42/nihms969912f13.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/55d9d32bd0dd/nihms969912f14.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/dce0c1b4574f/nihms969912f15.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/cfe61c0ed1b6/nihms969912f16.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/13c35d282526/nihms969912f17.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/d43c144a997c/nihms969912f18.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/55226b3d4fe2/nihms969912f19.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/caf1ca20cd06/nihms969912f20.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/17050eec1ef2/nihms969912f21.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/628ebf2b4787/nihms969912f22.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/1d2e151d1dfe/nihms969912f23.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/390790ef4147/nihms969912f24.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/e4d743f50724/nihms969912f25.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/24810b220dac/nihms969912f26.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/e7e227dfb182/nihms969912f27.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/66053db7dbe2/nihms969912f28.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/32e17a36e70b/nihms969912f29.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/e96179e566f2/nihms969912f30.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/5debacc08803/nihms969912f31.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/3f0387f41521/nihms969912f32.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/0f4775f35acb/nihms969912f33.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/2a4974dee984/nihms969912f34.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/fc95bf91f09d/nihms969912f35.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/a4318ef5a1fb/nihms969912f36.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/469f5615f422/nihms969912f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/b316d1dd65bd/nihms969912f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/76d54681f5b9/nihms969912f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/2640f837f949/nihms969912f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/0893af044427/nihms969912f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/6c080f14ec74/nihms969912f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/a92d49e239e8/nihms969912f7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/240553dbadf7/nihms969912f8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/c39fde8e5e41/nihms969912f9.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/58d517ae08b3/nihms969912f10.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/e6c25622d14a/nihms969912f11.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/db87603df949/nihms969912f12.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/a07796ab0f42/nihms969912f13.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/55d9d32bd0dd/nihms969912f14.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/dce0c1b4574f/nihms969912f15.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/cfe61c0ed1b6/nihms969912f16.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/13c35d282526/nihms969912f17.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/d43c144a997c/nihms969912f18.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/55226b3d4fe2/nihms969912f19.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/caf1ca20cd06/nihms969912f20.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/17050eec1ef2/nihms969912f21.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/628ebf2b4787/nihms969912f22.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/1d2e151d1dfe/nihms969912f23.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/390790ef4147/nihms969912f24.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/e4d743f50724/nihms969912f25.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/24810b220dac/nihms969912f26.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/e7e227dfb182/nihms969912f27.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/66053db7dbe2/nihms969912f28.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/32e17a36e70b/nihms969912f29.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/e96179e566f2/nihms969912f30.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/5debacc08803/nihms969912f31.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/3f0387f41521/nihms969912f32.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/0f4775f35acb/nihms969912f33.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/2a4974dee984/nihms969912f34.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/fc95bf91f09d/nihms969912f35.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18c8/5982588/a4318ef5a1fb/nihms969912f36.jpg

相似文献

1
Oxygen Activation by Cu LPMOs in Recalcitrant Carbohydrate Polysaccharide Conversion to Monomer Sugars.铜基脂肪酶在木质纤维素类多糖向单糖转化过程中对氧的活化作用。
Chem Rev. 2018 Mar 14;118(5):2593-2635. doi: 10.1021/acs.chemrev.7b00421. Epub 2017 Nov 20.
2
Polysaccharide degradation by lytic polysaccharide monooxygenases.溶菌多糖单加氧酶对多糖的降解作用。
Curr Opin Struct Biol. 2019 Dec;59:54-64. doi: 10.1016/j.sbi.2019.02.015. Epub 2019 Apr 1.
3
Characterization of a bacterial copper-dependent lytic polysaccharide monooxygenase with an unusual second coordination sphere.一种具有不寻常第二配位层的细菌铜依赖性溶菌多糖单加氧酶的特性。
FEBS J. 2020 Aug;287(15):3298-3314. doi: 10.1111/febs.15203. Epub 2020 Jan 24.
4
The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases.溶菌多糖单加氧酶催化多糖裂解的分子基础。
Nat Chem Biol. 2016 Apr;12(4):298-303. doi: 10.1038/nchembio.2029. Epub 2016 Feb 29.
5
Cellulose degradation by polysaccharide monooxygenases.多糖单加氧酶对纤维素的降解。
Annu Rev Biochem. 2015;84:923-46. doi: 10.1146/annurev-biochem-060614-034439. Epub 2015 Mar 12.
6
Lytic polysaccharide monooxygenases and other histidine-brace copper proteins: structure, oxygen activation and biotechnological applications.裂解多糖单加氧酶和其他组氨酸框铜蛋白:结构、氧活化及生物技术应用。
Biochem Soc Trans. 2021 Feb 26;49(1):531-540. doi: 10.1042/BST20201031.
7
The interplay between lytic polysaccharide monooxygenases and glycoside hydrolases.裂解多糖单加氧酶与糖苷水解酶的相互作用。
Essays Biochem. 2023 Apr 18;67(3):551-559. doi: 10.1042/EBC20220156.
8
Discovery and industrial applications of lytic polysaccharide mono-oxygenases.裂解多糖单加氧酶的发现与工业应用
Biochem Soc Trans. 2016 Feb;44(1):143-9. doi: 10.1042/BST20150204.
9
Crystal structure and computational characterization of the lytic polysaccharide monooxygenase GH61D from the Basidiomycota fungus Phanerochaete chrysosporium.真菌黄孢原毛平革菌 GH61D 溶菌多糖单加氧酶的晶体结构和计算特征。
J Biol Chem. 2013 May 3;288(18):12828-39. doi: 10.1074/jbc.M113.459396. Epub 2013 Mar 22.
10
Structural and functional characterization of a conserved pair of bacterial cellulose-oxidizing lytic polysaccharide monooxygenases.保守型细菌纤维素氧化裂解多糖单加氧酶对的结构与功能表征。
Proc Natl Acad Sci U S A. 2014 Jun 10;111(23):8446-51. doi: 10.1073/pnas.1402771111. Epub 2014 May 27.

引用本文的文献

1
Controlling outer-sphere solvent reorganization energy to turn on or off the function of artificial metalloenzymes.控制外层溶剂重组能以开启或关闭人工金属酶的功能。
Nat Commun. 2025 Mar 28;16(1):3048. doi: 10.1038/s41467-025-57904-5.
2
Theoretical study of the formation of HO by lytic polysaccharide monooxygenases: the reaction mechanism depends on the type of reductant.裂解多糖单加氧酶形成HO的理论研究:反应机制取决于还原剂的类型。
Chem Sci. 2025 Jan 10;16(7):3173-3186. doi: 10.1039/d4sc06906d. eCollection 2025 Feb 12.
3
Mimicking the Reactivity of LPMOs with a Mononuclear Cu Complex.

本文引用的文献

1
Multiscale Modelling of Lytic Polysaccharide Monooxygenases.裂解多糖单加氧酶的多尺度建模
ACS Omega. 2017 Feb 13;2(2):536-545. doi: 10.1021/acsomega.6b00521. eCollection 2017 Feb 28.
2
High-resolution structure of a lytic polysaccharide monooxygenase from reveals a predicted linker as an integral part of the catalytic domain.溶菌多糖单加氧酶的高分辨率结构揭示了一个预测的连接子是催化结构域的一个组成部分。
J Biol Chem. 2017 Nov 17;292(46):19099-19109. doi: 10.1074/jbc.M117.799767. Epub 2017 Sep 12.
3
Oxidative cleavage of polysaccharides by monocopper enzymes depends on HO.
用单核铜配合物模拟木质素过氧化物酶的反应活性。
Eur J Inorg Chem. 2024 May 22;27(15). doi: 10.1002/ejic.202300774. Epub 2024 Jan 8.
4
Cu-Promoted -Hydroxylation of sp Bonds with Concomitant Aromatic 1,2-Rearrangement Involving a Cu-oxyl-hydroxo Species.铜促进的sp键羟基化反应及伴随的涉及铜氧基-氢氧基物种的芳香族1,2-重排反应。
Inorg Chem. 2024 Oct 28;63(43):20675-20688. doi: 10.1021/acs.inorgchem.4c03304. Epub 2024 Oct 18.
5
Synthetic Copper-(Di)oxygen Complex Generation and Reactivity Relevant to Copper Protein O-Processing.与铜蛋白O-加工相关的合成铜-(二)氧配合物的生成及反应活性
Bull Jpn Soc Coord Chem. 2024;83:16-27. doi: 10.4019/bjscc.83.16. Epub 2024 Jun 20.
6
A Four-Coordinate End-On Superoxocopper(II) Complex: Probing the Link between Coordination Number and Reactivity.一种四配位端基超氧铜(II)配合物:探究配位数与反应活性之间的联系。
J Am Chem Soc. 2024 Aug 28;146(34):23704-23716. doi: 10.1021/jacs.3c12268. Epub 2024 Aug 14.
7
Heterologous Expression and Biochemical Characterization of a Novel Lytic Polysaccharide Monooxygenase from CSC-1.来自CSC-1的新型裂解多糖单加氧酶的异源表达及生化特性分析
Microorganisms. 2024 Jul 8;12(7):1381. doi: 10.3390/microorganisms12071381.
8
Copper-oxygen adducts: new trends in characterization and properties towards C-H activation.铜-氧加合物:C-H活化表征与性质的新趋势
Chem Sci. 2024 May 13;15(27):10308-10349. doi: 10.1039/d4sc01762e. eCollection 2024 Jul 10.
9
Understanding the initial events of the oxidative damage and protection mechanisms of the AA9 lytic polysaccharide monooxygenase family.了解AA9裂解多糖单加氧酶家族氧化损伤的初始事件及保护机制。
Chem Sci. 2024 Jan 9;15(7):2558-2570. doi: 10.1039/d3sc05933b. eCollection 2024 Feb 14.
10
Assessing the role of redox partners in TthLPMO9G and its mutants: focus on HO production and interaction with cellulose.评估氧化还原伙伴在嗜热栖热菌LPMO9G及其突变体中的作用:聚焦于过氧化氢的产生及与纤维素的相互作用。
Biotechnol Biofuels Bioprod. 2024 Feb 1;17(1):19. doi: 10.1186/s13068-024-02463-y.
单铜酶通过 HO 实现多糖的氧化裂解。
Nat Chem Biol. 2017 Oct;13(10):1123-1128. doi: 10.1038/nchembio.2470. Epub 2017 Aug 28.
4
Reactivity of the copper(iii)-hydroxide unit with phenols.氢氧化铜(III)单元与酚类的反应活性。
Chem Sci. 2017 Feb 1;8(2):1075-1085. doi: 10.1039/c6sc03039d. Epub 2016 Sep 27.
5
A quantitative indicator diagram for lytic polysaccharide monooxygenases reveals the role of aromatic surface residues in HjLPMO9A regioselectivity.一种用于裂解多糖单加氧酶的定量指标图揭示了芳香族表面残基在HjLPMO9A区域选择性中的作用。
PLoS One. 2017 May 31;12(5):e0178446. doi: 10.1371/journal.pone.0178446. eCollection 2017.
6
Boosting LPMO-driven lignocellulose degradation by polyphenol oxidase-activated lignin building blocks.通过多酚氧化酶激活的木质素构建单元促进LPMO驱动的木质纤维素降解
Biotechnol Biofuels. 2017 May 10;10:121. doi: 10.1186/s13068-017-0810-4. eCollection 2017.
7
Neutron and Atomic Resolution X-ray Structures of a Lytic Polysaccharide Monooxygenase Reveal Copper-Mediated Dioxygen Binding and Evidence for N-Terminal Deprotonation.一种裂解多糖单加氧酶的中子和原子分辨率X射线结构揭示了铜介导的双氧结合以及N端去质子化的证据。
Biochemistry. 2017 May 23;56(20):2529-2532. doi: 10.1021/acs.biochem.7b00019. Epub 2017 May 11.
8
Unliganded and substrate bound structures of the cellooligosaccharide active lytic polysaccharide monooxygenase LsAA9A at low pH.纤维寡糖活性溶菌多糖单加氧酶LsAA9A在低pH下的未结合配体和结合底物结构。
Carbohydr Res. 2017 Aug 7;448:187-190. doi: 10.1016/j.carres.2017.03.010. Epub 2017 Mar 24.
9
On the formation and role of reactive oxygen species in light-driven LPMO oxidation of phosphoric acid swollen cellulose.关于活性氧物种在光驱动磷酸溶胀纤维素的LPMO氧化中的形成及作用
Carbohydr Res. 2017 Aug 7;448:182-186. doi: 10.1016/j.carres.2017.03.013. Epub 2017 Mar 18.
10
The Role of the Secondary Coordination Sphere in a Fungal Polysaccharide Monooxygenase.二级配位层在真菌多糖单加氧酶中的作用
ACS Chem Biol. 2017 Apr 21;12(4):1095-1103. doi: 10.1021/acschembio.7b00016. Epub 2017 Mar 3.