Purification and characterization of the acetyl-coa synthetase from mycobacterium tuberculosis | |
Li, Ru2,3; Gu, Jing2; Chen, Peng4; Zhang, Zhiping2; Deng, Jiaoyu1; Zhang, XianEn2 | |
刊名 | Acta biochimica et biophysica sinica
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2011-11-01 | |
卷号 | 43期号:11页码:891-899 |
关键词 | Acetyl-coa synthetase Acetate Auto-acetylation Deacetylase Mycobacterium tuberculosis |
ISSN号 | 1672-9145 |
DOI | 10.1093/abbs/gmr076 |
通讯作者 | Deng, jiaoyu(dengjy@wh.iov.cn) |
英文摘要 | Acetyl-coa (accoa) synthetase (acs) catalyzes the conversion of acetate into accoa, which is involved in many catabolic and anabolic pathways. although this enzyme has been studied for many years in many organisms, the properties of mycobacterium tuberculosis acs and the regulation of its activity remain unknown. here, the putative acs gene of m. tuberculosis h37rv (mt-acs) was expressed as a fusion protein with 6xhis-tag on the c-terminus in escherichia coli. the recombinant mt-acs protein was successfully purified and then its enzymatic characteristics were analyzed. the optimal ph and temperature, and the kinetic parameters of mt-acs were determined. to investigate whether mt-acs is regulated by lysine acetylation as reported for salmonella enterica acs, its mutant k617r was also generated. determination of the enzymatic activity suggests that lys-617 is critical for its function. we further demonstrated that mt-acs underwent auto-acetylation with acetate but not with accoa as the acetyl donor, which resulted in the decrease of its activity. coa, the substrate for accoa formation, inhibited the auto-acetylation. furthermore, the silent information regulator (sir2) of m. tuberculosis (mt-sir2) could catalyze mt-acs deacetylation, which resulted in activation of acs. these results may provide more insights into the physiological roles of mt-acs in m. tuberculosis central metabolism. |
WOS关键词 | COENZYME-A SYNTHETASE ; RESPONSE REGULATOR CHEY ; ESCHERICHIA-COLI ; SALMONELLA-ENTERICA ; AUTO-ACETYLATION ; ACYL ADENYLATES ; ENZYME ; ACETATE ; ACTIVATION ; LYSINE |
WOS研究方向 | Biochemistry & Molecular Biology ; Biophysics |
WOS类目 | Biochemistry & Molecular Biology ; Biophysics |
语种 | 英语 |
出版者 | OXFORD UNIV PRESS |
WOS记录号 | WOS:000296291000008 |
内容类型 | 期刊论文 |
URI标识 | http://www.corc.org.cn/handle/1471x/2375967 |
专题 | 武汉病毒研究所 |
通讯作者 | Deng, Jiaoyu |
作者单位 | 1.Chinese Acad Sci, Wuhan Inst Virol, Key Lab Agr & Environm Microbiol, Wuhan 430071, Peoples R China 2.Chinese Acad Sci, Wuhan Inst Virol, State Key Lab Virol, Wuhan 430071, Peoples R China 3.Guangxi Univ, Coll Life Sci & Technol, Nanning 530004, Peoples R China 4.Guangxi Univ, Coll Agr, Nanning 530004, Peoples R China |
推荐引用方式 GB/T 7714 | Li, Ru,Gu, Jing,Chen, Peng,et al. Purification and characterization of the acetyl-coa synthetase from mycobacterium tuberculosis[J]. Acta biochimica et biophysica sinica,2011,43(11):891-899. |
APA | Li, Ru,Gu, Jing,Chen, Peng,Zhang, Zhiping,Deng, Jiaoyu,&Zhang, XianEn.(2011).Purification and characterization of the acetyl-coa synthetase from mycobacterium tuberculosis.Acta biochimica et biophysica sinica,43(11),891-899. |
MLA | Li, Ru,et al."Purification and characterization of the acetyl-coa synthetase from mycobacterium tuberculosis".Acta biochimica et biophysica sinica 43.11(2011):891-899. |
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