| Chao SH |
------>authors3_c=None ------>paper_class1=1 ------>Impact_Factor=3.810 ------>paper_class3=2 ------>paper_class2=1 ------>vol=72 ------>confirm_bywho=chlin ------>insert_bywho=microbes ------>Jurnal_Rank=20.2 ------>authors4_c=None ------>comm_author= ------>patent_EDate=None ------>authors5_c=None ------>publish_day=None ------>paper_class2Letter=None ------>page2=971 ------>medlineContent= ------>unit=E0200 ------>insert_date=20060104 ------>iam=5 ------>update_date=None ------>author=??? ------>change_event=4 ------>ISSN=None ------>authors_c=None ------>score=500 ------>journal_name=Applied and Envirnmental Microbiology ------>paper_name=Characterization of a Novel PepF-Like Oligopeptidase Secreted by Bacillus amyloliquefaciens 23-7A ------>confirm_date=20060503 ------>tch_id=084001 ------>pmid=16391147 ------>page1=986 ------>fullAbstract=An oligopeptidase from Bacillus amyloliquefaciens 23-7A was characterized along with its biochemical activities and structural gene. The protein~s amino acid sequence and enzymatic activities were similar to those of other bacterial PepFs, which belong to metallopeptidase family M3. While most bacterial PepFs are cytoplasmic endopeptidases, the identified PepFBa oligopeptidase is a secreted protein and may facilitate the process of sporulation. ------>tmu_sno=None ------>sno=12405 ------>authors2=Cheng TH ------>authors3=Shaw CY ------>authors4=Lee MH ------>authors5=Hsu YH ------>authors6=Tsai YC ------>authors6_c=None ------>authors=Chao SH ------>delete_flag=0 ------>SCI_JNo=None ------>authors2_c=None ------>publish_area=None ------>updateTitle=Characterization of a novel PepF-like oligopeptidase secreted by Bacillus amyloliquefaciens 23-7A. ------>language=2 ------>check_flag=None ------>submit_date=None ------>country=None ------>no=1 ------>patent_SDate=None ------>update_bywho=None ------>publish_year=2006 ------>submit_flag=None ------>publish_month=None |