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Journal Article | Research Support, Non-U.S. Gov't | Research Support, U.S. Gov't, P.H.S.

Substitution of cysteine 192 in a highly conserved Streptococcus pyogenes extracellular cysteine protease (interleukin 1beta convertase) alters proteolytic activity and ablates zymogen processing.

J M Musser, K Stockbauer, V Kapur, G W Rudgers
J M Musser
Department of Pathology, Baylor College of Medicine, Houston, Texas 77030, USA.
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K Stockbauer
Department of Pathology, Baylor College of Medicine, Houston, Texas 77030, USA.
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V Kapur
Department of Pathology, Baylor College of Medicine, Houston, Texas 77030, USA.
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G W Rudgers
Department of Pathology, Baylor College of Medicine, Houston, Texas 77030, USA.
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ABSTRACT

Virtually all strains of the human pathogenic bacterium Streptococcus pyogenes express a highly conserved extracellular cysteine protease. The protein is made as an inactive zymogen of 40,000 Da and undergoes autocatalytic truncation to result in a 28,000-Da active protease. Numerous independent lines of investigation suggest that this enzyme participates in one or more phases of host-parasite interaction, such as inflammation and soft tissue invasion. Replacement of the single cysteine residue (C-192) with serine (C192S mutation) resulted in loss of detectable proteolytic activity against bovine casein, human fibronectin, and the low-molecular-weight synthetic substrate 7-amino-4-trifluoromethyl coumarin. The C192S mutant molecule does not undergo autocatalytic processing of zymogen to mature form. Taken together, these data support the hypothesis that C-192 participates in active-site formation and enzyme catalysis.

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Substitution of cysteine 192 in a highly conserved Streptococcus pyogenes extracellular cysteine protease (interleukin 1beta convertase) alters proteolytic activity and ablates zymogen processing.
J M Musser, K Stockbauer, V Kapur, G W Rudgers
Infection and Immunity Jun 1996, 64 (6) 1913-1917; DOI:

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Substitution of cysteine 192 in a highly conserved Streptococcus pyogenes extracellular cysteine protease (interleukin 1beta convertase) alters proteolytic activity and ablates zymogen processing.
J M Musser, K Stockbauer, V Kapur, G W Rudgers
Infection and Immunity Jun 1996, 64 (6) 1913-1917; DOI:
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