A propeptide‐independent protease from Tannerella sp.6_1_58FAA_CT1 displays trypsin‐like specificity. (7th October 2016)

• Record Type: Journal Article
• Authors: Song, Qitao; Zhang, Xiaoyue; Li, Na; Shen, Jie; Cheng, Jiansong
• Is Part Of: Journal of basic microbiology. Volume 57:issue 1(2017:Jan.)
• Page Start: 50
• Page End: 56
• Publication Date: 2016-10-07
• Subjects: Protease -- Trypsin‐like -- Propeptide -- Citrulline -- Tannerella; Microbiology -- Periodicals; 579
• DOI: 10.1002/jobm.201600486
• Languages: English
• ISSNs: 0233-111X

Abstract

Abstract : 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 ArgXaa 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.