| Chang RC, Chen JC and ShawJF |
------>authors3_c=None ------>paper_class1=1 ------>Impact_Factor=None ------>paper_class3=2 ------>paper_class2=1 ------>vol=221 ------>confirm_bywho=tzengcr ------>insert_bywho=??? ------>Jurnal_Rank=None ------>authors4_c=None ------>comm_author=0 ------>patent_EDate=None ------>authors5_c=None ------>publish_day=None ------>paper_class2Letter=None ------>page2=483 ------>medlineContent= ------>unit=G0200 ------>insert_date=19991209 ------>iam=3 ------>update_date= ------>author=??? ------>change_event=5 ------>ISSN=None ------>authors_c=None ------>score=500 ------>journal_name=Biochem. Biophys. Res. Commun. ------>paper_name=Site-directed mutagenesis of a novel serine arylesterase from Vibrio mimicus identifies residues essential for catalysis. ------>confirm_date=20030509 ------>tch_id=086069 ------>pmid=8619880 ------>page1=477 ------>fullAbstract=Site-directed mutagenesis (SDM) of an arylesterase (the arylesterase) from Vibrio mimicus revealed that residues S29, H153, and D96 constituted a catalytic triad. The use of a serine residue for ester hydrolysis by the arylesterase proves that the enzyme is a novel serine arylesterase. SDM also showed that D28 was necessary for the esterase activity; to our knowledge it is the first time that a residue immediately preceding the active-site serine in esterases was shown biochemically to possess such a property. The results further suggest that D28 plays a role in substrate-binding. Residue 31 was firmly shown to participate in the binding of N-acetyl-D, L-phenylalanine beta-naphthyl ester (NAPNE), an artificial substrate for chymotrypsin. The S31G enzyme showed a 4 fold decrease in the Km for NAPNE over that of wild type enzyme, proving residue 31 is important for substrate-specificity. A mechanism for binding and catalysis of esters by the arylesterase is proposed, which includes the unique role of S31 for aromatic (hydrophobic) acyl-binding. The biochemical properties of the arylesterase suggest that the enzyme stands out as a member of a distinct subfamily within a recently proposed, lipolytic enzyme family. ------>tmu_sno=None ------>sno=83 ------>authors2=None ------>authors3=None ------>authors4=None ------>authors5=None ------>authors6=None ------>authors6_c=None ------>authors=Chang RC, Chen JC and ShawJF ------>delete_flag=0 ------>SCI_JNo=None ------>authors2_c=None ------>publish_area=None ------>updateTitle=Site-directed mutagenesis of a novel serine arylesterase from Vibrio mimicus identifies residues essential for catalysis. ------>language= ------>check_flag=0 ------>submit_date= ------>country=None ------>no=2 ------>patent_SDate=None ------>update_bywho= ------>publish_year=1996 ------>submit_flag= ------>publish_month=None |