Expression and characterization of the biofilm-related and carnosine-hydrolyzing aminoacylhistidine dipeptidase from Vibrio alginolyticus

Keyphrases

• Dipeptidase 100%
• L-carnitine 100%
• Vibrio Alginolyticus 100%
• Biofilm 100%
• Enzymatic Activity 66%
• Zn2+ 66%
• Zinc Ion 66%
• Dipeptide 66%
• Binding Residues 66%
• Metal Binding 66%
• Ni2+ 33%
• Mn2+ 33%
• Cd2+ 33%
• Co2+ 33%
• Cu2+ 33%
• Mg2+ 33%
• Metal Ions 33%
• Water Molecule 33%
• Purified Enzymes 33%
• Lid Domain 33%
• Mutational Analysis 33%
• Metallopeptidase 33%
• Catalytic Domain 33%
• Divalent Metal Ions 33%
• High Activity 33%
• Recombinant Enzyme 33%
• Functional Role 33%
• Broad Substrate Specificity 33%
• Recombinant 33%
• Homodimeric 33%
• Reconstitution 33%
• Aspartic Acid 33%
• Structural Homology Modelling 33%
• Sequence Homology 33%
• Metal Catalysis 33%
• Tetrahedral Intermediate 33%
• His-tag 33%
• Adept 33%
• Substrate Enzyme 33%
• Partial Retention 33%
• Lactobacillus Delbrueckii 33%
• Catalytic Water 33%
• Antimicrobial Antibodies 33%
• Antimicrobial Therapy 33%
• Metal-dependent 33%
• Structural Homology 33%

Biochemistry, Genetics and Molecular Biology

• Enzyme 100%
• Dipeptidase 100%
• Vibrio alginolyticus 100%
• Carnosine 100%
• Biofilm 100%
• Enzyme Activity 50%
• Active Site 50%
• Zinc Ion 50%
• Structural Homology 50%
• Metal Binding 50%
• Dipeptide 50%
• Metalloproteinase 25%
• Enzyme Specificity 25%
• Metalloendopeptidase 25%
• Enzyme Active Site 25%
• Homology Modeling 25%
• Solution and Solubility 25%
• Sequence Homology 25%
• Enzyme Substrate 25%
• Lactobacillus delbrueckii 25%
• Aspartic Acid 25%