Literature DB >> 18026858

Regulation of bacterial protease activity.

Benedykt Władyka1, Katarzyna Pustelny.   

Abstract

Proteases, also referred to as peptidases, are the enzymes that catalyse the hydrolysis of peptide bonds in polipeptides. A variety of biological functions and processes depend on their activity. Regardless of the organism's complexity, peptidases are essential at every stage of life of every individual cell, since all protein molecules produced must be proteolytically processed and eventually recycled. Protease inhibitors play a crucial role in the required strict and multilevel control of the activity of proteases involved in processes conditioning both the physiological and pathophysiological functioning of an organism, as well as in host-pathogen interactions. This review describes the regulation of activity of bacterial proteases produced by dangerous human pathogens, focusing on the Staphylococcus genus.

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Year:  2008        PMID: 18026858      PMCID: PMC6275810          DOI: 10.2478/s11658-007-0048-4

Source DB:  PubMed          Journal:  Cell Mol Biol Lett        ISSN: 1425-8153            Impact factor:   5.787


  78 in total

1.  Three-dimensional structures of the human alpha 2-macroglobulin-methylamine and chymotrypsin complexes.

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2.  Two allelic forms of the aureolysin gene (aur) within Staphylococcus aureus.

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Journal:  Infect Immun       Date:  2000-02       Impact factor: 3.441

3.  The molecular architecture of the sar locus in Staphylococcus aureus.

Authors:  M G Bayer; J H Heinrichs; A L Cheung
Journal:  J Bacteriol       Date:  1996-08       Impact factor: 3.490

4.  Characterization of the sar locus and its interaction with agr in Staphylococcus aureus.

Authors:  J H Heinrichs; M G Bayer; A L Cheung
Journal:  J Bacteriol       Date:  1996-01       Impact factor: 3.490

5.  Role of metalloprotease in activation of the precursor of staphylococcal protease.

Authors:  G R Drapeau
Journal:  J Bacteriol       Date:  1978-11       Impact factor: 3.490

Review 6.  Type I signal peptidase: an overview.

Authors:  Renu Tuteja
Journal:  Arch Biochem Biophys       Date:  2005-09-15       Impact factor: 4.013

7.  Molecular characterization of a novel Staphylococcus aureus serine protease operon.

Authors:  S B Reed; C A Wesson; L E Liou; W R Trumble; P M Schlievert; G A Bohach; K W Bayles
Journal:  Infect Immun       Date:  2001-03       Impact factor: 3.441

Review 8.  Role of bacterial proteases in pseudomonal and serratial keratitis.

Authors:  Koki Matsumoto
Journal:  Biol Chem       Date:  2004-11       Impact factor: 3.915

9.  Stabilization vs. degradation of Staphylococcus aureus metalloproteinase.

Authors:  J Potempa; Z Porwit-Bobr; J Travis
Journal:  Biochim Biophys Acta       Date:  1989-12-08

10.  Inhibition by alpha-macroglobulin and other serum proteins.

Authors:  P M Starkey; A J Barrett
Journal:  Biochem J       Date:  1973-04       Impact factor: 3.857

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  8 in total

1.  Specific protease activity indicates the degree of Pseudomonas aeruginosa infection in chronic infected wounds.

Authors:  D Wildeboer; K E Hill; F Jeganathan; D W Williams; A D Riddell; P E Price; D W Thomas; P Stephens; R A Abuknesha; R G Price
Journal:  Eur J Clin Microbiol Infect Dis       Date:  2012-01-26       Impact factor: 3.267

2.  Cotranslational proteolysis dominates glutathione homeostasis to support proper growth and development.

Authors:  Frédéric Frottin; Christelle Espagne; José A Traverso; Caroline Mauve; Benoît Valot; Caroline Lelarge-Trouverie; Michel Zivy; Graham Noctor; Thierry Meinnel; Carmela Giglione
Journal:  Plant Cell       Date:  2009-10-23       Impact factor: 11.277

3.  Transcription factor PrtT controls expression of multiple secreted proteases in the human pathogenic mold Aspergillus fumigatus.

Authors:  Haim Sharon; Shelly Hagag; Nir Osherov
Journal:  Infect Immun       Date:  2009-06-29       Impact factor: 3.441

4.  Staphylococcal SplB serine protease utilizes a novel molecular mechanism of activation.

Authors:  Katarzyna Pustelny; Michal Zdzalik; Natalia Stach; Justyna Stec-Niemczyk; Przemyslaw Cichon; Anna Czarna; Grzegorz Popowicz; Pawel Mak; Marcin Drag; Guy S Salvesen; Benedykt Wladyka; Jan Potempa; Adam Dubin; Grzegorz Dubin
Journal:  J Biol Chem       Date:  2014-04-08       Impact factor: 5.157

5.  RC1339/APRc from Rickettsia conorii is a novel aspartic protease with properties of retropepsin-like enzymes.

Authors:  Rui Cruz; Pitter Huesgen; Sean P Riley; Alexander Wlodawer; Carlos Faro; Christopher M Overall; Juan J Martinez; Isaura Simões
Journal:  PLoS Pathog       Date:  2014-08-21       Impact factor: 6.823

6.  Enterohemorrhagic Escherichia coli O157:H7 gene expression profiling in response to growth in the presence of host epithelia.

Authors:  Narveen Jandu; Nathan K L Ho; Kevin A Donato; Mohamed A Karmali; Mariola Mascarenhas; Simon P Duffy; Chetankumar Tailor; Philip M Sherman
Journal:  PLoS One       Date:  2009-03-18       Impact factor: 3.240

7.  Enzymatic properties, evidence for in vivo expression, and intracellular localization of shewasin D, the pepsin homolog from Shewanella denitrificans.

Authors:  Ana Rita Leal; Rui Cruz; Daniel Bur; Pitter F Huesgen; Rosário Faro; Bruno Manadas; Alexander Wlodawer; Carlos Faro; Isaura Simões
Journal:  Sci Rep       Date:  2016-03-31       Impact factor: 4.379

Review 8.  The interactome: predicting the protein-protein interactions in cells.

Authors:  Dariusz Plewczyński; Krzysztof Ginalski
Journal:  Cell Mol Biol Lett       Date:  2008-10-06       Impact factor: 5.787

  8 in total

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