Functional and structural studies of pullulanase from Anoxybacillus sp. LM18-11
文献类型：期刊论文
| 作者 | Xu, Jianyong1; Ren, Feifei1; Huang, Chun-Hsiang1; Zheng, Yingying1; Zhen, Jie1; Sun, Hong1; Ko, Tzu-Ping2; He, Miao1; Chen, Chun-Chi1; Chan, Hsiu-Chien1 |
| 刊名 | PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
 |
| 出版日期 | 2014-09-01 |
| 卷号 | 82期号:9页码:1685-1693 |
| 关键词 | pullulanase crystal structure thermostable carbohydrate-binding motif complex structure |
| 英文摘要 | Pullulanase is a debranching enzyme that specifically hydrolyzes the alpha-1,6 glycosidic linkage of alpha-glucans, and has wide industrial applications. Here, we report structural and functional studies of a new thermostable pullulanase from Anoxybacillus sp. LM18-11 (PulA). Based on the hydrolysis products, PulA was classified as a type I pullulanase. It showed maximum activity at 60 degrees C and pH 6.0. Kinetic study showed that the specific activity and K-m for pullulan of PulA are 750 U mg(-1) and 16.4 mu mol L-1, respectively. PulA has a half-life of 48 h at 60 degrees C. The remarkable thermostability makes PulA valuable for industrial usage. To further investigate the mechanism of the enzyme, we solved the crystal structures of PulA and its complexes with maltotriose and maltotetraose at 1.75-2.22 angstrom resolution. The PulA structure comprises four domains (N1, N2, A, and C). A is the catalytic domain, in which three conserved catalytic residues were identified (D413, E442, and D526). Two molecules of oligosaccharides were seen in the catalytic A domain in a parallel binding mode. Interestingly, another two oligosaccharides molecules were found between the N1 domain and the loop between the third beta-strand and the third alpha-helix in the A domain. Based on sequence alignment and the ligand binding pattern, the N1 domain is identified as a new type of carbohydrate-binding motif and classified to the CBM68 family. The structure solved here is the first structure of pullulanase which has carbohydrate bound to the N1 domain. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 研究领域[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 关键词[WOS] | ALPHA-AMYLASE FAMILY ; GLYCOSYL HYDROLASES ; CRYSTAL-STRUCTURES ; ENZYMES ; SEQUENCE ; BINDING ; SPECIFICITY ; RESIDUES ; SERVER ; SITE |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000340940300001 |
| 公开日期 | 2014-12-23 |
| 源URL | [http://124.16.173.210/handle/311007/547]  |
| 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 |
| 推荐引用方式 GB/T 7714 | Xu, Jianyong,Ren, Feifei,Huang, Chun-Hsiang,et al. Functional and structural studies of pullulanase from Anoxybacillus sp. LM18-11[J]. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS,2014,82(9):1685-1693. |
| APA | Xu, Jianyong.,Ren, Feifei.,Huang, Chun-Hsiang.,Zheng, Yingying.,Zhen, Jie.,...&Ma, Yanhe.(2014).Functional and structural studies of pullulanase from Anoxybacillus sp. LM18-11.PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS,82(9),1685-1693. |
| MLA | Xu, Jianyong,et al."Functional and structural studies of pullulanase from Anoxybacillus sp. LM18-11".PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS 82.9(2014):1685-1693. |
入库方式： OAI收割
来源：天津工业生物技术研究所
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