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J. Biol. Chem., Vol. 278, Issue 19, 17336-17343, May 9, 2003

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Maturation Processing and Characterization of Streptopain^*

Chiu-Yueh Chen, Shih-Chi Luo, Chih-Feng Kuo^§, Yee-Shin Lin^§, Jiunn-Jong Wu^¶, Ming T. Lin, Ching-Chuan Liu, Wen-Yih Jeng, and Woei-Jer Chuang^**

From the Departments of  Biochemistry, ^§ Microbiology and Immunology, ^¶ Medical Technology, and  Pediatrics, National Cheng Kung University College of Medicine, 1 University Road, Tainan 701, Taiwan

Streptopain is a cysteine protease expressed by Streptococcus pyogenes. To study the maturation mechanism of streptopain, wild-type and Q186N, C192S, H340R, N356D and W357A mutant proteins were expressed in Escherichia coli and purified to homogeneity. Proteolytic analyses showed that the maturation of prostreptococcal pyrogenic exotoxin B zymogen (pro-SPE B) involves eight intermediates with a combination of cis- and trans-processing. Based on the sequences of these intermediates, the substrate specificity of streptopain favors a hydrophobic residue at the P2 site. The relative autocatalytic rates of these mutants exhibited the order Q186N > W357A > N356D, C192S, H340R. Interestingly, the N356D mutant containing protease activity could not be converted into the 28-kDa form by autoprocessing. This observation suggested that Asn³⁵⁶ might involve the cis-processing of the propeptide. In addition, the maturation rates of pro-SPE B with trypsin and plasmin were 10- and 60-fold slower than that with active mature streptopain. These findings indicate that active mature streptopain likely plays the most important role in the maturation of pro-SPE B under physiological conditions.

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