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

NWIPB OpenIR

	Oxalate decarboxylase from Agrobacterium tumefaciens C58 is translocated by a twin arginine translocation system
	Shen, Yu-Hu ; Liu, Rui-Juan ; Wang, Hai-Qing
	2008-07-01
发表期刊	JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY ; Shen YuHu,Liu RuiJuan,Wang HaiQing.Oxalate decarboxylase from Agrobacterium tumefaciens C58 is translocated by a twin arginine translocation system.JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY,2008,18(7):1245-1251
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.
文献类型	期刊论文
条目标识符	http://210.75.249.4/handle/363003/40516
专题	中国科学院西北高原生物研究所
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, Shen YuHu,Liu RuiJuan,Wang HaiQing.Oxalate decarboxylase from Agrobacterium tumefaciens C58 is translocated by a twin arginine translocation system.JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY,2008,18(7):1245-1251,2008.
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.
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 (2008).