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DOI | 10.1126/science.aau3744 |
Evolution of a highly active and enantiospecific metalloenzyme from short peptides | |
Studer, Sabine1; Hansen, Douglas A.1,5; Pianowski, Zbigniew L.1,6; Mittl, Peer R. E.2; Debon, Aaron1; Guffy, Sharon L.3; Der, Bryan S.3,7; Kuhlman, Brian3,4; Hilvert, Donald1 | |
2018-12-14 | |
发表期刊 | SCIENCE
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ISSN | 0036-8075 |
EISSN | 1095-9203 |
出版年 | 2018 |
卷号 | 362期号:6420页码:1285-+ |
文章类型 | Article |
语种 | 英语 |
国家 | Switzerland; USA; Germany |
英文摘要 | Primordial sequence signatures in modern proteins imply ancestral origins tracing back to simple peptides. Although short peptides seldom adopt unique folds, metal ions might have templated their assembly into higher-order structures in early evolution and imparted useful chemical reactivity. Recapitulating such a biogenetic scenario, we have combined design and laboratory evolution to transform a zinc-binding peptide into a globular enzyme capable of accelerating ester cleavage with exacting enantiospecificity and high catalytic efficiency (k(cat)/K-M similar to 10(6) M-1 s(-1)). The simultaneous optimization of structure and function in a naive peptide scaffold not only illustrates a plausible enzyme evolutionary pathway from the distant past to the present but also proffers exciting future opportunities for enzyme design and engineering. |
领域 | 地球科学 ; 气候变化 ; 资源环境 |
收录类别 | SCI-E |
WOS记录号 | WOS:000452994400051 |
WOS关键词 | ENZYME-LIKE PROTEINS ; COMPUTATIONAL DESIGN ; TRANSITION-STATE ; EFFICIENT ; SITE ; MECHANISM ; CATALYSIS ; MUTANTS ; LIBRARY ; MODEL |
WOS类目 | Multidisciplinary Sciences |
WOS研究方向 | Science & Technology - Other Topics |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://119.78.100.173/C666/handle/2XK7JSWQ/200311 |
专题 | 地球科学 资源环境科学 气候变化 |
作者单位 | 1.Swiss Fed Inst Technol, Lab Organ Chem, CH-8093 Zurich, Switzerland; 2.Univ Zurich, Dept Biochem, CH-8057 Zurich, Switzerland; 3.Univ N Carolina, Dept Biochem & Biophys, Chapel Hill, NC 27599 USA; 4.Univ N Carolina, Lineberger Comprehens Canc Ctr, Chapel Hill, NC 27599 USA; 5.Antheia Inc, Menlo Pk, CA 94025 USA; 6.KIT, Inst Organ Chem, D-76131 Karlsruhe, Germany; 7.Capital One, Henrico, VA 23238 USA |
推荐引用方式 GB/T 7714 | Studer, Sabine,Hansen, Douglas A.,Pianowski, Zbigniew L.,et al. Evolution of a highly active and enantiospecific metalloenzyme from short peptides[J]. SCIENCE,2018,362(6420):1285-+. |
APA | Studer, Sabine.,Hansen, Douglas A..,Pianowski, Zbigniew L..,Mittl, Peer R. E..,Debon, Aaron.,...&Hilvert, Donald.(2018).Evolution of a highly active and enantiospecific metalloenzyme from short peptides.SCIENCE,362(6420),1285-+. |
MLA | Studer, Sabine,et al."Evolution of a highly active and enantiospecific metalloenzyme from short peptides".SCIENCE 362.6420(2018):1285-+. |
条目包含的文件 | 条目无相关文件。 |
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