Inactivation mechanism of the beta-ketoacyl-[acyl carrier protein] reductase of bacterial type-ii fatty acid synthase by epigallocatechin gallate | |
Li, Bing-Hui; Zhang, Rui; Du, Ya-Tao; Sun, Ying-Hui; Tian, Wei-Xi | |
刊名 | Biochemistry and cell biology-biochimie et biologie cellulaire
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2006-10-01 | |
卷号 | 84期号:5页码:755-762 |
关键词 | Fabg Egcg Segregation Inactivation |
ISSN号 | 0829-8211 |
DOI | 10.1139/o06-047 |
通讯作者 | Tian, wei-xi(tianweixi@gucas.ac.cn) |
英文摘要 | Epipilocatechin gallate (egcg), a major compound from green tea, reversibly inhibits beta-ketoacyl-[acyl carrier protein] reductase (fabg) from escherichia coli. in this study, we found that egcg exhibited an atypical time-dependent inhibition of fabg, which possibly resulted from the egcg-induced aggregation of fabg. it was observed that fabg inactivation and aggregation occurred nearly simultaneously, with a lag time that decreased with increasing egcg concentration. these results suggest that some chemical reactions, required for aggregation and inactivation, occurred during the lag time. since egc was detected by hplc after the incubation of egcg with fabg, egcg probably covalently modified fabg. these further results showed that i tetramer of fabg must be modified by several, possibly 4, egcg molecules before the formation of fabg aggregates. fabg aggregation was a first-order reaction independent of protein concentration. due to an initial lag time, the first-order rate of aggregation gradually increased, reaching a maximal and constant value. the effect of increasing concentration of egcg on the first-order rate constant for aggregation indicated that egcg bound to fabg by affinity labeling. based on the results, we propose a mechanism for the interaction of egcg with fab-g:egcg first binds reversibly to each subunit of fabg, followed by covalent modification and then aggregation of the 4 egcg-modified subunits. |
WOS关键词 | ESCHERICHIA-COLI ; PROTEIN REDUCTASE ; BRASSICA-NAPUS ; BIOSYNTHESIS ; POLYPHENOLS ; TYPHIMURIUM ; ELONGATION ; FABG |
WOS研究方向 | Biochemistry & Molecular Biology ; Cell Biology |
WOS类目 | Biochemistry & Molecular Biology ; Cell Biology |
语种 | 英语 |
出版者 | NATL RESEARCH COUNCIL CANADA-N R C RESEARCH PRESS |
WOS记录号 | WOS:000242894900011 |
内容类型 | 期刊论文 |
URI标识 | http://www.corc.org.cn/handle/1471x/2378995 |
专题 | 中国科学院大学 |
通讯作者 | Tian, Wei-Xi |
作者单位 | Grad Univ, Chinese Acad Sci, Dept Biol, Beijing 100049, Peoples R China |
推荐引用方式 GB/T 7714 | Li, Bing-Hui,Zhang, Rui,Du, Ya-Tao,et al. Inactivation mechanism of the beta-ketoacyl-[acyl carrier protein] reductase of bacterial type-ii fatty acid synthase by epigallocatechin gallate[J]. Biochemistry and cell biology-biochimie et biologie cellulaire,2006,84(5):755-762. |
APA | Li, Bing-Hui,Zhang, Rui,Du, Ya-Tao,Sun, Ying-Hui,&Tian, Wei-Xi.(2006).Inactivation mechanism of the beta-ketoacyl-[acyl carrier protein] reductase of bacterial type-ii fatty acid synthase by epigallocatechin gallate.Biochemistry and cell biology-biochimie et biologie cellulaire,84(5),755-762. |
MLA | Li, Bing-Hui,et al."Inactivation mechanism of the beta-ketoacyl-[acyl carrier protein] reductase of bacterial type-ii fatty acid synthase by epigallocatechin gallate".Biochemistry and cell biology-biochimie et biologie cellulaire 84.5(2006):755-762. |
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