Biochemical and structural characterization of the intracellular mannanase aamana of alicyclobacillus acidocaldarius reveals a novel glycoside hydrolase family belonging to clan gh-a
文献类型：期刊论文
| 作者 | Zhang, Yueling1,2; Ju, Jiansong1; Peng, Hao1; Gao, Feng1; Zhou, Cheng1,2; Zeng, Yan1; Xue, Yanfen1; Li, Yin1; Henrissat, Bernard3,4,5; Gao, George F.1 |
| 刊名 | Journal of biological chemistry
 |
| 出版日期 | 2008-11-14 |
| 卷号 | 283期号:46页码:31551-31558 |
| ISSN号 | 0021-9258 |
| DOI | 10.1074/jbc.m803409200 |
| 通讯作者 | Ma, yanhe(mayanhe@im.ac.cn) |
| 英文摘要 | An intracellular mannanase was identified from the thermoacidophile alicyclobacillus acidocaldarius tc-12-31. this enzyme is particularly interesting, because it shows no significant sequence similarity to any known glycoside hydrolase. gene cloning, biochemical characterization, and structural studies of this novel mannanase are reported in this paper. the gene consists of 963 bp and encodes a 320-amino acid protein, aamana. based on its substrate specificity and product profile, aamana is classified as an endo-beta-1,4-mannanase that is capable of transglycosylation. kinetic analysis studies revealed that the enzyme required at least five subsites for efficient hydrolysis. the crystal structure at 1.9 a resolution showed that aamana adopted a (beta/alpha)8-barrel fold. two catalytic residues were identified: glu(151) at thecterminus of beta-stand beta 4 and glu(231) at the c terminus of beta 7. based on the structure of the enzyme and evidence of its transglycosylation activity, aamana is placed in clan gh-a. superpositioning of its structure with that of other clan gh-a enzymes revealed that six of the eight gh-a key residues were functionally conserved in aamana, with the exceptions being residues thr(95) and cys(150). we propose a model of substrate binding in aamanain which glu(282) interacts with the axial oh-c(2) in -2 subsites. based on sequence comparisons, the enzyme was assigned to a new glycoside hydrolase family (gh113) that belongs to clan gh-a. |
| WOS关键词 | PRELIMINARY-X-RAY ; MUSSEL MYTILUS-EDULIS ; BETA-MANNANASE ; 3-DIMENSIONAL STRUCTURE ; CRYSTAL-STRUCTURE ; GENE CLONING ; BACILLUS SP ; SEQUENCE ; ENZYMES ; CRYSTALLIZATION |
| WOS研究方向 | Biochemistry & Molecular Biology |
| WOS类目 | Biochemistry & Molecular Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:000260760800034 |
| 出版者 | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
| URI标识 | http://www.irgrid.ac.cn/handle/1471x/2388479 |
| 专题 | 中国科学院大学 |
| 通讯作者 | Ma, Yanhe |
| 作者单位 | 1.Chinese Acad Sci, Inst Microbiol, State Key Lab Microbial Resources, Beijing 100101, Peoples R China 2.Chinese Acad Sci, Grad Sch, Beijing 100049, Peoples R China 3.CNRS, UMR6098, F-13288 Marseille, France 4.Univ Aix Marseille 1, F-13288 Marseille, France 5.Univ Aix Marseille 2, F-13288 Marseille, France |
| 推荐引用方式 GB/T 7714 | Zhang, Yueling,Ju, Jiansong,Peng, Hao,et al. Biochemical and structural characterization of the intracellular mannanase aamana of alicyclobacillus acidocaldarius reveals a novel glycoside hydrolase family belonging to clan gh-a[J]. Journal of biological chemistry,2008,283(46):31551-31558. |
| APA | Zhang, Yueling.,Ju, Jiansong.,Peng, Hao.,Gao, Feng.,Zhou, Cheng.,...&Ma, Yanhe.(2008).Biochemical and structural characterization of the intracellular mannanase aamana of alicyclobacillus acidocaldarius reveals a novel glycoside hydrolase family belonging to clan gh-a.Journal of biological chemistry,283(46),31551-31558. |
| MLA | Zhang, Yueling,et al."Biochemical and structural characterization of the intracellular mannanase aamana of alicyclobacillus acidocaldarius reveals a novel glycoside hydrolase family belonging to clan gh-a".Journal of biological chemistry 283.46(2008):31551-31558. |
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来源：中国科学院大学
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