标题:Unusual Activities of the Thioesterase Domain for the Biosynthesis of the Polycyclic Tetramate Macrolactam HSAF in Lysobacter enzymogenes C3
作者:Lou, Lili; Chen, Haotong; Cerny, Ronald L.; Li, Yaoyao; Shen, Yuemao; Du, Liangcheng
作者机构:[Lou, Lili; Chen, Haotong; Cerny, Ronald L.; Du, Liangcheng] Univ Nebraska, Dept Chem, Lincoln, NE 68588 USA.; [Li, Yaoyao; Shen, Yuemao] Shandong U 更多
通讯作者:Du, L
通讯作者地址:[Du, LC]Univ Nebraska, Dept Chem, Lincoln, NE 68588 USA.
来源:BIOCHEMISTRY
出版年:2012
卷:51
期:1
页码:4-6
DOI:10.1021/bi2015025
摘要:HSAF is an antifungal natural product with a new mode of action. A rare bacterial iterative PKS-NRPS assembles the HSAF skeleton. The biochemical characterization of the NRPS revealed that the thioesterase (TE) domain possesses the activities of both a protease and a peptide ligase. Active site mutagenesis, circular dichroism spectra, and homology modeling of the TE structure suggested that the TE may possess uncommon features that may lead to the unusual activities. The iterative PKS-NRPS is found in all polycyclic tetramate macrolactam gene clusters, and the unusual activities of the TE may be common to this type of hybrid PKS-NRPS.
收录类别:EI;SCOPUS;SCIE
WOS核心被引频次:27
Scopus被引频次:28
资源类型:期刊论文
原文链接:https://www.scopus.com/inward/record.uri?eid=2-s2.0-84863028981&doi=10.1021%2fbi2015025&partnerID=40&md5=f65562fc512a863c56b3961f67873582
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