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从E264中发现并分析泰国蛋白酶A至F（强效组蛋白去乙酰化酶抑制剂）的活性。

Discovery and activity profiling of thailandepsins A through F, potent histone deacetylase inhibitors, from E264.

作者信息

Wang Cheng, Flemming Creston J, Cheng Yi-Qiang

机构信息

Department of Biological Sciences, University of Wisconsin-Milwaukee, PO Box 413, Milwaukee, WI 53201, USA.

出版信息

Medchemcomm. 2012 Aug 1;3(8):976-981. doi: 10.1039/C2MD20024D.

DOI:10.1039/C2MD20024D
PMID:23997923
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3755959/
Abstract

Three new bicyclic depsipeptides, which are related to the previously reported thailandepsins A (), B () and C (), were discovered from the culture broth of E264 when supplemented with amino acid precursors, and were subsequently named as thailandepsins D (), E () and F (), respectively. Enzyme assays showed that are potent histone deacetylase (HDAC) inhibitors, particularly toward HDAC1 which represents class I human HDACs.

摘要

当向E264的培养液中添加氨基酸前体时，从其培养液中发现了三种新的双环缩肽，它们与先前报道的泰国缩肽A（）、B（）和C（）相关，随后分别命名为泰国缩肽D（）、E（）和F（）。酶活性测定表明，它们是有效的组蛋白脱乙酰酶（HDAC）抑制剂，特别是对代表I类人类HDAC的HDAC1。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ef9d/3755959/8b72bd7c6f5a/nihms459405f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ef9d/3755959/4af4178b0a74/nihms459405f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ef9d/3755959/8b72bd7c6f5a/nihms459405f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ef9d/3755959/4af4178b0a74/nihms459405f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ef9d/3755959/8b72bd7c6f5a/nihms459405f2.jpg

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Thailandepsin a.泰国胃蛋白酶a
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Histone deacetylase inhibitors from Burkholderia thailandensis.从泰国伯克霍尔德菌中分离得到的组蛋白去乙酰化酶抑制剂。
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