scholarly journals Unique Substrate Specificity of SplE Serine Protease from Staphylococcus aureus

Structure ◽  
2018 ◽  
Vol 26 (4) ◽  
pp. 572-579.e4 ◽  
Author(s):  
Natalia Stach ◽  
Magdalena Kalinska ◽  
Michal Zdzalik ◽  
Radoslaw Kitel ◽  
Abdulkarim Karim ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Substrate Specificity ◽  
Serine Protease

Profiling serine protease substrate specificity with solution phase fluorogenic peptide microarrays

PROTEOMICS ◽  
2005 ◽  
Vol 5 (5) ◽  
pp. 1292-1298 ◽  
Author(s):  
Dhaval N. Gosalia ◽  
Cleo M. Salisbury ◽  
Dustin J. Maly ◽  
Jonathan A. Ellman ◽  
Scott L. Diamond
Keyword(s):  
Substrate Specificity ◽  
Serine Protease ◽  
Solution Phase ◽  
Peptide Microarrays ◽  
Protease Substrate ◽  
Fluorogenic Peptide

Substrate specificity of Staphylococcus aureus cysteine proteases – Staphopains A, B and C

Biochimie ◽  
2012 ◽  
Vol 94 (2) ◽  
pp. 318-327 ◽  
Author(s):  
Magdalena Kalińska ◽  
Tomasz Kantyka ◽  
Doron C. Greenbaum ◽  
Katrine S. Larsen ◽  
Benedykt Władyka ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Substrate Specificity ◽  
Cysteine Proteases

scholarly journals Involvement of the Arg566 residue of Aeromonas sobria serine protease in substrate specificity

PLoS ONE ◽  
2017 ◽  
Vol 12 (10) ◽  
pp. e0186392 ◽  
Author(s):  
Hidetomo Kobayashi ◽  
Tadamune Otsubo ◽  
Fumiteru Teraoka ◽  
Kiyoshi Ikeda ◽  
Soshi Seike ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Serine Protease ◽  
Aeromonas Sobria

scholarly journals Evolution of the C30 Carotenoid Synthase CrtM for Function in a C40 Pathway

2002 ◽  
Vol 184 (23) ◽  
pp. 6690-6699 ◽  
Author(s):  
Daisuke Umeno ◽  
Alexander V. Tobias ◽  
Frances H. Arnold
Keyword(s):  
Escherichia Coli ◽  
Staphylococcus Aureus ◽  
Substrate Specificity ◽  
Significant Variation ◽  
The Other ◽  
Biosynthetic Pathways ◽  
Product Range

ABSTRACT The C30 carotene synthase CrtM from Staphylococcus aureus and the C40 carotene synthase CrtB from Erwinia uredovora were swapped into their respective foreign C40 and C30 biosynthetic pathways (heterologously expressed in Escherichia coli) and evaluated for function. Each displayed negligible ability to synthesize the natural carotenoid product of the other. After one round of mutagenesis and screening, we isolated 116 variants of CrtM able to synthesize C40 carotenoids. In contrast, we failed to find a single variant of CrtB with detectable C30 activity. Subsequent analysis revealed that the best CrtM mutants performed comparably to CrtB in an in vivo C40 pathway. These mutants showed significant variation in performance in their original C30 pathway, indicating the emergence of enzymes with broadened substrate specificity as well as those with shifted specificity. We discovered that Phe 26 alone determines the specificity of CrtM. The plasticity of CrtM with respect to its substrate and product range highlights the potential for creating further new carotenoid backbone structures.

scholarly journals Staphylococcus aureus Induces Increased Serine Protease Activity in Keratinocytes

2017 ◽  
Vol 137 (2) ◽  
pp. 377-384 ◽  
Author(s):  
Michael R. Williams ◽  
Teruaki Nakatsuji ◽  
James A. Sanford ◽  
Alison F. Vrbanac ◽  
Richard L. Gallo
Keyword(s):  
Staphylococcus Aureus ◽  
Serine Protease ◽  
Protease Activity ◽  
Serine Protease Activity

scholarly journals Staphylococcal Exfoliative Toxins Cleave α- and β-Melanocyte-Stimulating Hormones

2000 ◽  
Vol 68 (4) ◽  
pp. 2366-2368 ◽  
Author(s):  
James V. Rago ◽  
Gregory M. Vath ◽  
Timothy J. Tripp ◽  
Gregory A. Bohach ◽  
Douglas H. Ohlendorf ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Glutamic Acid ◽  
Crystal Structures ◽  
Serine Protease ◽  
Protease Activity ◽  
Staphylococcal Scalded Skin Syndrome ◽  
Melanocyte Stimulating Hormone ◽  
Causative Agents ◽  
Serine Protease Family ◽  
Stimulating Hormone

ABSTRACT The staphylococcal exfoliative toxins (ETs) A and B (ETA and ETB) are 27-kDa exotoxins produced by certain strains ofStaphylococcus aureus and are the causative agents of staphylococcal scalded-skin syndrome. The crystal structures of the ETs strongly indicate that the proteins are members of the serine protease family of enzymes, although protease activity until now has not yet been conclusively demonstrated. Here, we show that the peptide β-melanocyte-stimulating hormone (β-MSH) is cleaved by ETA and that both ETA and ETB are capable of cleaving α-MSH. Both toxins exhibit cleavage at specific glutamic acid residues in MSH peptides. Moreover, biologically inactive mutants of ETA were incapable of cleaving β-MSH.

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