Literature DB >> 681326

Unusual COOH-terminal structure of staphylococcal protease.

G R Drapeau.   

Abstract

The extracellular enzyme, staphylococcal protease, carries a COOH-terminal tryptic peptide of 43 amino acid residues most of which are aspartic acid, asparagine, and proline. This peptide might have a function equivalent to that of a similar segment previously observed at the NH2-terminal end of the membrane-bound penicillinase precursor of Bacillus licheniformis (Yamamoto, S., and Lampen, J. O. (1976) Proc. Natl. Acad. Sci. U. S. A. 73, 1457-1461). These observations would suggest that bacterial exoproteins which are secreted in the form of precursors differ from extracellular proteins by the presence of an extra segment at their NH2- and/or COOH-terminal ends.

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Year:  1978        PMID: 681326

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  4 in total

1.  Nucleotide sequence of the serine protease gene of Staphylococcus aureus, strain V8.

Authors:  C Carmona; G L Gray
Journal:  Nucleic Acids Res       Date:  1987-08-25       Impact factor: 16.971

2.  Characterization of an extracellular metalloprotease with elastase activity from Staphylococcus epidermidis.

Authors:  P Teufel; F Götz
Journal:  J Bacteriol       Date:  1993-07       Impact factor: 3.490

3.  Comparison of bovine and mouse pituitary glycoprotein hormone pre-alpha subunits synthesized in vitro.

Authors:  L C Giudice; M J Waxdal; B D Weintraub
Journal:  Proc Natl Acad Sci U S A       Date:  1979-10       Impact factor: 11.205

4.  Genetic and biochemical properties of an extracellular neutral metalloprotease from Staphylococcus hyicus subsp. hyicus.

Authors:  S Ayora; F Götz
Journal:  Mol Gen Genet       Date:  1994-02
  4 in total

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