Oxalate decarboxylase from Agrobacterium tumefaciens C58 is translocated by a twin arginine translocation system

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	Oxalate decarboxylase from Agrobacterium tumefaciens C58 is translocated by a twin arginine translocation system
	Shen, Yu-Hu 1,2; Liu, Rui-Juan 1; Wang, Hai-Qing 1
	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	被引频次：8[WOS] [WOS记录] [WOS相关记录]
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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