The Potential Active Site of the Lipoprotein-specific (Type II) Signal Peptidase of Bacillus subtilis
| Autor: | Geeske Zanen, Sierd Bron, Gerhardus Venema, van Jan Maarten Dijl, H Tjalsma |
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| Přispěvatelé: | Molecular Genetics, Faculty of Science and Engineering, Translational Immunology Groningen (TRIGR) |
| Rok vydání: | 1999 |
| Předmět: |
PROTEIN SECRETION
Signal peptide BACTERIUM MYCOPLASMA-PNEUMONIAE Proteases Lipoproteins TEMPORALLY CONTROLLED EXPRESSION Molecular Sequence Data Bacillus subtilis medicine.disease_cause Biochemistry NUCLEOTIDE-SEQUENCE CATALYTIC MECHANISM medicine COMPLETE GENOME SEQUENCE Amino Acid Sequence Molecular Biology Escherichia coli Conserved Sequence DNA Primers chemistry.chemical_classification LSP GENE Binding Sites Base Sequence biology RETROVIRAL PROTEASES Serine Endopeptidases Nucleic acid sequence ASPARTIC PROTEASES Membrane Proteins Active site Cell Biology biology.organism_classification Amino acid Secretory protein Models Chemical chemistry ESCHERICHIA-COLI Mutagenesis Site-Directed biology.protein |
| Zdroj: | The Journal of Biological Chemistry, 274(40), 28191-28197. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
| ISSN: | 0021-9258 |
| Popis: | Type II signal peptidases (SPase II) remove signal peptides from lipid-modified preproteins of eubacteria. As the catalytic mechanism employed by type II SPases was not known, the present studies were aimed at the identification of their potential active site residues. Comparison of the deduced amino acid sequences of 19 known type II SPases revealed the presence of five conserved domains. The importance of the 15 best conserved residues in these domains was investigated using the type II SPase of Bacillus subtilis, which, unlike SPase II of Escherichia coli, is not essential for viability. The results showed that only six residues are important for SPase II activity. These are Asp-14, Asn-99, Asp-102, Asn-126, Ala-128, and Asp-129, Only Asp-14 was required for stability of SPase II, indicating that the other five residues are required for catalysis, the active site geometry, or the specific recognition of lipid-modified preproteins. As Asp-102 and Asp-129 are the only residues invoked in the known catalytic mechanisms of proteases, me hypothesize that these two residues are directly involved in SPase II-mediated catalysis, This implies that type II SPases belong to a novel family of aspartic proteases. |
| Databáze: | OpenAIRE |
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