期刊
BIOCHIMIE
卷 94, 期 2, 页码 318-327出版社
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.biochi.2011.07.020
关键词
Protease; Staphopain; Staphylococcal virulence; Substrates library; Substrate specificity
资金
- Polish Ministry of Science and Higher Education [K PBP 000322, N N302 130734, N N204 160036, N N301 032834]
- DFG
- European Regional Development Fund in the framework of the Polish Innovation Economy Operational Program [POIG.02.01.00-12-167/ 08]
- Malopolska Centre of Biotechnology
Human strains of Staphylococcus aureus secrete two papain-like proteases, staphopain A and B. Avian strains produce another homologous enzyme, staphopain C. Animal studies suggest that staphopains B and C contribute to bacterial virulence, in contrast to staphopain A. which seems to have a virulence unrelated function. Here we present a detailed study of substrate preferences of all three proteases. The specificity of staphopain A, B and C substrate-binding subsites was mapped using different synthetic substrate libraries, inhibitor libraries and a protein substrate combinatorial library. The analysis demonstrated that the most efficiently hydrolyzed sites, using Schechter and Berger nomenclature, comprise a P2-Gly down arrow Ala(Ser) sequence motif, where P2 distinguishes the specificity of staphopain A (Leu) from that of both staphopains B and C (Phe/Tyr). However, we show that at the same time the overall specificity of staphopains is relaxed, insofar as multiple substrates that diverge from the sequences described above are also efficiently hydrolyzed. (C) 2011 Elsevier Masson SAS. All rights reserved.
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