TAILIEUCHUNG - Báo cáo khoa học: Expression and characterization of the biofilm-related and carnosine-hydrolyzing aminoacylhistidine dipeptidase from Vibrio alginolyticus

The biofilm-related and carnosine-hydrolyzing aminoacylhistidine dipepti-dase (pepD) gene from Vibrio alginolyticuswas cloned and sequenced. The recombinant PepD protein was produced and biochemically characterized and the putative active-site residues responsible for metal binding and catalysis were identified. | ỊFEBS Journal Expression and characterization of the biofilm-related and carnosine-hydrolyzing aminoacylhistidine dipeptidase from Vibrio alginolyticus Ting-Yi Wang Yi-Chin Chen Liang-Wei Kao Chin-Yuan Chang Yu-Kuo Wang Yen-Hsi Liu Jen-Min Feng and Tung-Kung Wu Department of BiologicalScience and Technology NationalChiao Tung University Hsin-Chu Taiwan China Keywords aminoacylhistidine dipeptidase biofilm carnosinase metallopeptidase H clan Vibrio alginolyticus Correspondence . Wu Department of BiologicalScience and Technology NationalChiao Tung University Hsin-Chu Taiwan China Fax 886 3 5725700 Tel 886 3 5729287 E-mail tkwmll@ These authors contributed equally to this work Received 1 May 2008 revised 5 August 2008 accepted 11 August 2008 doi The biofilm-related and carnosine-hydrolyzing aminoacylhistidine dipeptidase pepD gene from Vibrio alginolyticus was cloned and sequenced. The recombinant PepD protein was produced and biochemically characterized and the putative active-site residues responsible for metal binding and catalysis were identified. The recombinant enzyme which was identified as a homodimeric dipeptidase in solution exhibited broad substrate specificity for Xaa-His and His-Xaa dipeptides with the highest activity for the His-His dipeptide. Sequence and structural homologies suggest that the enzyme is a member of the metal-dependent metallopeptidase family. Indeed the purified enzyme contains two zinc ions per monomer. Reconstitution of His-Tag-cleaved native apo-PepD with various metal ions indicated that enzymatic activity could be optimally restored when Zn2 was replaced with other divalent metal ions including Mn2 Co2 Ni2 Cu2 and Cd2 and partially restored when Zn2 was replaced with Mg2 . Structural homology modeling of PepD also revealed a catalytic domain and a lid domain similar to those of the Lactobacillus delbrueckii PepV protein. Mutational analysis of the putative active-site residues .

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