Structural Bioinformatics of Vibrio cholerae Aminopeptidase A (PepA) Monomer
| Autor: | Ghosia Lutfullah, Khalida Shouqat, Rizwan Ali, Farhat Amin, M. Kamran Azim, Noreen Azhar, Sajid Noor, Zahid Hussain Khan |
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| Rok vydání: | 2009 |
| Předmět: |
Models
Molecular Molecular Sequence Data Protein degradation Glutamyl Aminopeptidase medicine.disease_cause Biochemistry Microbiology chemistry.chemical_compound Structural Biology Catalytic Domain medicine Amino Acid Sequence Vibrio cholerae Escherichia coli chemistry.chemical_classification Metalloexopeptidase PEPA biology Computational Biology Active site General Medicine Enzyme chemistry biology.protein Sequence Alignment DNA |
| Zdroj: | Protein & Peptide Letters. 16:36-45 |
| ISSN: | 0929-8665 |
| Popis: | Aminopeptidase A (PepA) is a metalloexopeptidase found in Vibrio cholerae .It functions as a transcriptional repressor in regulatory cascade that controls virulence gene expression in V. cholerae. It is involved in protein degradation and in the metabolism of biologically active peptides. We proposed a 3D model of PepA based upon the crystal structure of PepA from Escherichia coli (E. coli) with an intention to evaluate the active site of the enzyme and to predict the properties of this enzyme, study of its 3D structure will help in understanding its role in DNA binding. |
| Databáze: | OpenAIRE |
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