Characterization by molecular cloning and sequencing of the gene encoding an aminopeptidase from Listeria monocytogenes
| Autor: | D K, Winters, D M, Ivey, T P, Maloney, M G, Johnson |
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| Rok vydání: | 2001 |
| Předmět: |
DNA
Bacterial Base Sequence Sequence Homology Amino Acid Immunoblotting Molecular Sequence Data Antibodies Monoclonal Sequence Analysis DNA Regulatory Sequences Nucleic Acid Aminopeptidases Listeria monocytogenes Polymerase Chain Reaction DNA-Binding Proteins Repressor Proteins Bacterial Proteins Genes Bacterial Amino Acid Sequence Cloning Molecular Helix-Turn-Helix Motifs |
| Zdroj: | Antonie van Leeuwenhoek. 78(2) |
| ISSN: | 0003-6072 |
| Popis: | The pepC gene of Listeria monocytogenes encodes aminopeptidase C that is predicted to share 72% amino acid sequence similarity and 53% sequence identity with the cysteine aminopeptidase PepC from Lactococcus lactis. The gene product also shows strong similarity to aminopeptidase C from Streptococcus thermophilus and Lactobacillus helveticus, and to a cysteine proteinase/bleomycin hydrolase from Saccharomyces cerevisiae. The enzyme from L. monocytogenes displayed broad N-terminal hydrolytic activity, with a similar substrate specificity to its lactic acid bacterial counterpart. The inhibition spectrum shows a great deal of similarity with enzymes from the family of lactic acid bacteria. In addition, one of the clones studied contained DNA sequences that could encode a regulatory protein of the deoR helix-turn-helix DNA binding protein family. The organization of the locus, designated pep, is presented along with the characterization of the gene products of the pep locus. |
| Databáze: | OpenAIRE |
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