• 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

来自紫海胆的 DspA:首个具有生物化学特征的非微生物来源的卤代烷烃脱卤酶。

DspA from Strongylocentrotus purpuratus: The first biochemically characterized haloalkane dehalogenase of non-microbial origin.

机构信息

Loschmidt Laboratories, Department of Experimental Biology and Research Centre for Toxic Compounds in the Environment, Faculty of Science, Masaryk University, Kamenice 5/A13, 625 00 Brno, Czech Republic.

出版信息

Biochimie. 2013 Nov;95(11):2091-6. doi: 10.1016/j.biochi.2013.07.025. Epub 2013 Aug 11.

DOI:10.1016/j.biochi.2013.07.025
PMID:23939220
Abstract

Haloalkane dehalogenases are known as bacterial enzymes cleaving a carbon-halogen bond in halogenated compounds. Here we report the first biochemically characterized non-microbial haloalkane dehalogenase DspA from Strongylocentrotus purpuratus. The enzyme shows a preference for terminally brominated hydrocarbons and enantioselectivity towards β-brominated alkanes. Moreover, we identified other putative haloalkane dehalogenases of eukaryotic origin, representing targets for future experiments to discover dehalogenases with novel catalytic properties.

摘要

卤代烷烃脱卤酶是一类能够水解卤代化合物中碳卤键的细菌酶。本文首次报道了来自紫海胆的具有生物化学特征的非微生物卤代烷烃脱卤酶 DspA。该酶优先作用于末端溴代烃,且对β-溴代烷烃具有对映选择性。此外,我们还鉴定了其他可能具有真核起源的卤代烷烃脱卤酶,这些酶是未来发现具有新型催化特性的脱卤酶的潜在靶标。

相似文献

1
DspA from Strongylocentrotus purpuratus: The first biochemically characterized haloalkane dehalogenase of non-microbial origin.来自紫海胆的 DspA:首个具有生物化学特征的非微生物来源的卤代烷烃脱卤酶。
Biochimie. 2013 Nov;95(11):2091-6. doi: 10.1016/j.biochi.2013.07.025. Epub 2013 Aug 11.
2
The effect of a unique halide-stabilizing residue on the catalytic properties of haloalkane dehalogenase DatA from Agrobacterium tumefaciens C58.独特的卤化物稳定残基对根癌农杆菌 C58 卤代烷脱卤酶 DatA 催化特性的影响。
FEBS J. 2013 Jul;280(13):3149-59. doi: 10.1111/febs.12238. Epub 2013 Apr 8.
3
Cloning, biochemical properties, and distribution of mycobacterial haloalkane dehalogenases.分枝杆菌卤代烷脱卤酶的克隆、生化特性及分布
Appl Environ Microbiol. 2005 Nov;71(11):6736-45. doi: 10.1128/AEM.71.11.6736-6745.2005.
4
Two rhizobial strains, Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110, encode haloalkane dehalogenases with novel structures and substrate specificities.两种根瘤菌菌株,百脉根中生根瘤菌MAFF303099和大豆慢生根瘤菌USDA110,编码具有新颖结构和底物特异性的卤代烷脱卤酶。
Appl Environ Microbiol. 2005 Aug;71(8):4372-9. doi: 10.1128/AEM.71.8.4372-4379.2005.
5
Cloning, functional expression, biochemical characterization, and structural analysis of a haloalkane dehalogenase from Plesiocystis pacifica SIR-1.太平洋硫杆菌 SIR-1 中卤代烷烃脱卤酶的克隆、功能表达、生化特性和结构分析。
Appl Microbiol Biotechnol. 2011 Aug;91(4):1049-60. doi: 10.1007/s00253-011-3328-x. Epub 2011 May 21.
6
A Haloalkane Dehalogenase from Saccharomonospora viridis Strain DSM 43017, a Compost Bacterium with Unusual Catalytic Residues, Unique ()-Enantiopreference, and High Thermostability.一株堆肥细菌中具有独特催化残基、独特 ()-对映体选择性和高热稳定性的绿色糖单孢菌 Haloalkane 脱卤酶。
Appl Environ Microbiol. 2020 Aug 18;86(17). doi: 10.1128/AEM.02820-19.
7
Quantitative analysis of substrate specificity of haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26.少动鞘氨醇单胞菌UT26中卤代烷脱卤酶LinB底物特异性的定量分析
Biochemistry. 2005 Mar 8;44(9):3390-401. doi: 10.1021/bi047912o.
8
Cloning and expression of the haloalkane dehalogenase gene dhmA from Mycobacterium avium N85 and preliminary characterization of DhmA.鸟分枝杆菌N85中卤代烷脱卤酶基因dhmA的克隆与表达及DhmA的初步表征
Appl Environ Microbiol. 2002 Aug;68(8):3724-30. doi: 10.1128/AEM.68.8.3724-3730.2002.
9
Marine Rhodobacteraceae L-haloacid dehalogenase contains a novel His/Glu dyad that could activate the catalytic water.海洋红杆菌科 L-卤代酸脱卤酶含有一个新颖的 His/Glu 双联体,可激活催化水。
FEBS J. 2013 Apr;280(7):1664-80. doi: 10.1111/febs.12177. Epub 2013 Mar 8.
10
Functional and Catalytic Characterization of the Detoxifying Enzyme Haloalkane Dehalogenase from Rhizobium leguminosarum.来自豌豆根瘤菌的解毒酶卤代烷脱卤酶的功能和催化特性
Protein Pept Lett. 2017;24(7):599-608. doi: 10.2174/0929866524666170621094531.

引用本文的文献

1
Violet bioluminescent Polycirrus sp. (Annelida: Terebelliformia) discovered in the shallow coastal waters of the Noto Peninsula in Japan.日本能登半岛浅海海域发现的紫色生物发光多毛虫 Polycirrus sp. (环节动物门:须腕目)。
Sci Rep. 2021 Sep 27;11(1):19097. doi: 10.1038/s41598-021-98105-6.
2
A putative chordate luciferase from a cosmopolitan tunicate indicates convergent bioluminescence evolution across phyla.一种来自世界性被囊动物的假定脊索动物荧光素表明了跨门生物发光进化的趋同。
Sci Rep. 2020 Oct 20;10(1):17724. doi: 10.1038/s41598-020-73446-w.
3
A Haloalkane Dehalogenase from Saccharomonospora viridis Strain DSM 43017, a Compost Bacterium with Unusual Catalytic Residues, Unique ()-Enantiopreference, and High Thermostability.
一株堆肥细菌中具有独特催化残基、独特 ()-对映体选择性和高热稳定性的绿色糖单孢菌 Haloalkane 脱卤酶。
Appl Environ Microbiol. 2020 Aug 18;86(17). doi: 10.1128/AEM.02820-19.
4
Dehalogenases: From Improved Performance to Potential Microbial Dehalogenation Applications.脱卤酶:从提高性能到潜在的微生物脱卤应用。
Molecules. 2018 May 7;23(5):1100. doi: 10.3390/molecules23051100.
5
A Haloalkane Dehalogenase from a Marine Microbial Consortium Possessing Exceptionally Broad Substrate Specificity.一种具有极其广泛底物特异性的海洋微生物共生物中的卤代烷脱卤酶。
Appl Environ Microbiol. 2018 Jan 2;84(2). doi: 10.1128/AEM.01684-17. Print 2018 Jan 15.
6
Ylehd, an epoxide hydrolase with promiscuous haloalkane dehalogenase activity from tropical marine yeast Yarrowia lipolytica is induced upon xenobiotic stress.来源于热带海洋酵母解脂假丝酵母的环氧化物水解酶 Ylehd 具有杂环卤代烷脱卤酶活性,在异生物质胁迫下被诱导。
Sci Rep. 2017 Sep 19;7(1):11887. doi: 10.1038/s41598-017-12284-9.
7
A puzzling homology: a brittle star using a putative cnidarian-type luciferase for bioluminescence.一个令人费解的同源性:一种脆星使用假定的刺胞动物型荧光素酶进行生物发光。
Open Biol. 2017 Apr;7(4). doi: 10.1098/rsob.160300.
8
Discovery of Novel Haloalkane Dehalogenase Inhibitors.新型卤代烷脱卤酶抑制剂的发现
Appl Environ Microbiol. 2016 Jan 15;82(6):1958-1965. doi: 10.1128/AEM.03916-15.