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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
Source PublicationJOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
Volume18Issue:7Pages:1245-1251
SubtypeArticle
AbstractOxalate 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.
KeywordOxalate Decarboxylase Agrobacterium Tumfaciens Prokaryotic Expression Enzymatic Activity Assay Signal Peptide Twin-arginine Translocation System
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
Subject Area微生物学
WOS KeywordFUNCTIONALLY DIVERSE SUPERFAMILY ; GREEN FLUORESCENT PROTEIN ; BACILLUS-SUBTILIS YVRK ; SEED STORAGE PROTEINS ; ESCHERICHIA-COLI ; COLLYBIA-VELUTIPES ; MICROBIAL RELATIVES ; EXPORT ; OVEREXPRESSION ; LOCALIZATION
Indexed BySCI
Language英语
WOS Research AreaBiotechnology & Applied Microbiology ; Microbiology
WOS SubjectBiotechnology & Applied Microbiology ; Microbiology
WOS IDWOS:000257993800007
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Cited Times:5[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://210.75.249.4/handle/363003/1200
Collection中国科学院西北高原生物研究所
Affiliation1.Chinese Acad Sci, NW Plateau Inst Biol, Xining 810001, Peoples R China
2.Lanzhou Univ, Sch Life Sci, Lanzhou 730000, Peoples R China
Recommended Citation
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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