Knowledge Management System of Northwest Institute of Plateau Biology, CAS
Oxalate decarboxylase from Agrobacterium tumefaciens C58 is translocated by a twin arginine translocation system | |
Shen, Yu-Hu1,2; Liu, Rui-Juan1; Wang, Hai-Qing1 | |
2008-07-01 | |
发表期刊 | JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY |
卷号 | 18期号:7页码:1245-1251 |
文章类型 | Article |
摘要 | Oxalate decarboxylases (OXDCs) (E.C. 4.1.1.2) are enzymes catalyzing the conversion of oxalate to formate and CO2. The OXDCs found in fungi and bacteria belong to a functionally diverse protein superfamily known as the cupins. Fungi-originated OXDCs are secretory enzymes. However, most bacterial OXDCs are localized in the cytosol, and may be involved in energy metabolism. In Agrobacterium tumefaciens C58, a locus for a putative oxalate decarboxylase is present. In the study reported here, an enzyme was overexpressed in Escherichia coli and showed oxalate decarboxylase activity. Computational analysis revealed the A. tumefaciens C58 OXDC contains a signal peptide mediating translocation of the enzyme into the periplasm that was supported by expression of signal-peptideless and full-length versions of the enzyme in A. tumefaciens C58. Further site-directed mutagenesis experiment demonstrated that the A. tumefaciens C58 OXDC is most likely translocated by a twin-arginine translocation (TAT) system.; Oxalate decarboxylases (OXDCs) (E.C. 4.1.1.2) are enzymes catalyzing the conversion of oxalate to formate and CO2. The OXDCs found in fungi and bacteria belong to a functionally diverse protein superfamily known as the cupins. Fungi-originated OXDCs are secretory enzymes. However, most bacterial OXDCs are localized in the cytosol, and may be involved in energy metabolism. In Agrobacterium tumefaciens C58, a locus for a putative oxalate decarboxylase is present. In the study reported here, an enzyme was overexpressed in Escherichia coli and showed oxalate decarboxylase activity. Computational analysis revealed the A. tumefaciens C58 OXDC contains a signal peptide mediating translocation of the enzyme into the periplasm that was supported by expression of signal-peptideless and full-length versions of the enzyme in A. tumefaciens C58. Further site-directed mutagenesis experiment demonstrated that the A. tumefaciens C58 OXDC is most likely translocated by a twin-arginine translocation (TAT) system. |
关键词 | Oxalate Decarboxylase Agrobacterium Tumfaciens Prokaryotic Expression Enzymatic Activity Assay Signal Peptide Twin-arginine Translocation System |
WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
学科领域 | 微生物学 |
关键词[WOS] | FUNCTIONALLY DIVERSE SUPERFAMILY ; GREEN FLUORESCENT PROTEIN ; BACILLUS-SUBTILIS YVRK ; SEED STORAGE PROTEINS ; ESCHERICHIA-COLI ; COLLYBIA-VELUTIPES ; MICROBIAL RELATIVES ; EXPORT ; OVEREXPRESSION ; LOCALIZATION |
收录类别 | SCI |
语种 | 英语 |
WOS研究方向 | Biotechnology & Applied Microbiology ; Microbiology |
WOS类目 | Biotechnology & Applied Microbiology ; Microbiology |
WOS记录号 | WOS:000257993800007 |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://210.75.249.4/handle/363003/1200 |
专题 | 中国科学院西北高原生物研究所 |
作者单位 | 1.Chinese Acad Sci, NW Plateau Inst Biol, Xining 810001, Peoples R China 2.Lanzhou Univ, Sch Life Sci, Lanzhou 730000, Peoples R China |
推荐引用方式 GB/T 7714 | Shen, Yu-Hu,Liu, Rui-Juan,Wang, Hai-Qing. Oxalate decarboxylase from Agrobacterium tumefaciens C58 is translocated by a twin arginine translocation system[J]. JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY,2008,18(7):1245-1251. |
APA | Shen, Yu-Hu,Liu, Rui-Juan,&Wang, Hai-Qing.(2008).Oxalate decarboxylase from Agrobacterium tumefaciens C58 is translocated by a twin arginine translocation system.JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY,18(7),1245-1251. |
MLA | Shen, Yu-Hu,et al."Oxalate decarboxylase from Agrobacterium tumefaciens C58 is translocated by a twin arginine translocation system".JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY 18.7(2008):1245-1251. |
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