A propeptide-independent protease from Tannerella sp.6_1_58FAA_CT1 displays trypsin-like specificity

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• 作者：Qitao Song ; Xiaoyue Zhang ; Na Li ; Jie Shen and Jiansong Cheng
• 刊名：Journal of Basic Microbiology
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：57
• 期：1
• 页码：50-56
• 全文大小：1681K
• ISSN：1521-4028

文摘

Despite the absence of any homologs of Tannerella forsythia KLIKK proteases in Tannerella sp.6_1_58FAA_CT1, the strain possesses a putative cysteine protease (G9S4N1) closely related to RgpB of Porphyromonas gingivalis. G9S4N1 lacks obvious propeptide that behaves as inhibitor of proteases and was proven to be a propeptide-independent protease. Unlike RgpB, which exclusively cleaves ArgXaa bonds, G9S4N1 exhibits both arginine- and citrulline-specific activities. Mutations of Asp177, a potential P1-Arg binding site, to uncharged or positively charged residues did not alter the substrate specificity of G9S4N1 significantly. Moreover, a group of arginine-specific proteases from different species including porcine trypsin, bovine thrombin, and a trypsin-like serine protease of dengue 2 virus CF40-Gly-NS3pro185 also display different specificity toward citrulline residue, suggesting that citrulline-modified protein might have different roles and destiny in biological processes involving various proteases.