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  4. 期刊论文
Crystal structures of S-adenosylhomocysteine hydrolase from the thermophilic bacterium Thermotoga maritima

文献类型：期刊论文

作者Zheng, Yingying1; Chen, Chun-Chi1; Ko, Tzu-Ping2; Xiao, Xiansha1; Yang, Yunyun1; Huang, Chun-Hsiang1; Qian, Guojun3; Shao, Weilan3; Guo, Rey-Ting1
刊名JOURNAL OF STRUCTURAL BIOLOGY
出版日期2015-05-01
卷号190期号:2页码:135-142
关键词S-adenosylhomocysteine hydrolase Hyperthermophilic enzyme NAD(+)-binding domain Thermostability C-terminal loop
英文摘要S-adenosylhomocysteine (SAH) hydrolase catalyzes the reversible hydrolysis of SAH into adenosine and homocysteine by using NAD(+) as a cofactor. The enzyme from Thermotoga maritima (tmSAHH) has great potentials in industrial applications because of its hyperthermophilic properties. Here, two crystal structures of tmSAHH in complex with NAD(+) show both open and closed conformations despite the absence of bound substrate. Each subunit of the tetrameric enzyme is composed of three domains, namely the catalytic domain, the NAD(+)-binding domain and the C-terminal domain. The NAD(+) binding mode is clearly observed and a substrate analogue can also be modeled into the active site, where two cysteine residues in mesophilic enzymes are replaced by serine and threonine in tmSAHH. Notably, the C-terminal domain of tmSAHH lacks the second loop region of mesophilic SAHH, which is important in NAD(+) binding, and thus exposes the bound cofactor to the solvent. The difference explains the higher NAD(+) requirement of tmSAHH because of the reduced affinity. Furthermore, the feature of missing loop is consistently observed in thermophilic bacterial and archaeal SAHHs, and may be related to their thermostability. (C) 2015 Elsevier Inc. All rights reserved.
WOS标题词Science & Technology ; Life Sciences & Biomedicine
类目[WOS]Biochemistry & Molecular Biology ; Biophysics ; Cell Biology
研究领域[WOS]Biochemistry & Molecular Biology ; Biophysics ; Cell Biology
关键词[WOS]SITE-DIRECTED MUTAGENESIS ; L-HOMOCYSTEINE HYDROLASE ; RAT-LIVER ; COFACTOR REGENERATION ; COENZYME BINDING ; GENE-TRANSFER ; SEQUENCE ; ENZYME ; PURIFICATION ; ERITADENINE
收录类别SCI
语种英语
WOS记录号WOS:000353753900004
源URL[http://124.16.173.210/handle/834782/1461]  
专题天津工业生物技术研究所_结构生物学与蛋白酶学实验室 郭瑞庭_期刊论文
作者单位1.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Ind Enzymes Natl Engn Lab, Tianjin 300308, Peoples R China
2.Acad Sinica, Inst Biol Chem, Taipei 11529, Taiwan
3.Jiangsu Univ, Sch Environm, Biofuels Inst, Zhenjiang 212013, Peoples R China
推荐引用方式
GB/T 7714		 Zheng, Yingying,Chen, Chun-Chi,Ko, Tzu-Ping,et al. Crystal structures of S-adenosylhomocysteine hydrolase from the thermophilic bacterium Thermotoga maritima[J]. JOURNAL OF STRUCTURAL BIOLOGY,2015,190(2):135-142.
APA Zheng, Yingying.,Chen, Chun-Chi.,Ko, Tzu-Ping.,Xiao, Xiansha.,Yang, Yunyun.,...&Guo, Rey-Ting.(2015).Crystal structures of S-adenosylhomocysteine hydrolase from the thermophilic bacterium Thermotoga maritima.JOURNAL OF STRUCTURAL BIOLOGY,190(2),135-142.
MLA Zheng, Yingying,et al."Crystal structures of S-adenosylhomocysteine hydrolase from the thermophilic bacterium Thermotoga maritima".JOURNAL OF STRUCTURAL BIOLOGY 190.2(2015):135-142.

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来源：天津工业生物技术研究所

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