{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wang Y"],"funding":["MOST | National Key Research and Development Program of China","National Science Foundation of China","Major Scientific and Technological Innovation Project (MSTIP) of Shandong Province","Scientific Research Think Tank of Biological Manufacturing Industry in Qingdao","Taishan Scholars Program of Shandong Province"],"pagination":["e0167721"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9004396"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["88(7)"],"pubmed_abstract":["<i>Vibrio</i> collagenases of the M9A subfamily are closely related to <i>Vibrio</i> pathogenesis for their role in collagen degradation during host invasion. Although some <i>Vibrio</i> collagenases have been characterized, the collagen degradation mechanism of <i>Vibrio</i> collagenase is still largely unknown. Here, an M9A collagenase, VP397, from marine Vibrio pomeroyi strain 12613 was characterized, and its fragmentation pattern on insoluble type I collagen fibers was studied. VP397 is a typical <i>Vibrio</i> collagenase composed of a catalytic module featuring a peptidase M9N domain and a peptidase M9 domain and two accessory bacterial prepeptidase C-terminal domains (PPC domains). It can hydrolyze various collagenous substrates, including fish collagen, mammalian collagens of types "],"journal":["Applied and environmental microbiology"],"pubmed_title":["Mechanistic Insight into the Fragmentation of Type I Collagen Fibers into Peptides and Amino Acids by a <i>Vibrio</i> Collagenase."],"pmcid":["PMC9004396"],"funding_grant_id":["31670038","U1706207","QDSWZK202002","2019JZZY010817","2018YFC0310704","tspd20181203","U2006205"],"pubmed_authors":["Zhang YZ","Zhang XY","Su HN","Wang P","Liu SC","Li CY","Zhang X","Wang Y","Chen XL","Cao HY","Liu SM"],"additional_accession":[]},"is_claimable":false,"name":"Mechanistic Insight into the Fragmentation of Type I Collagen Fibers into Peptides and Amino Acids by a <i>Vibrio</i> Collagenase.","description":"<i>Vibrio</i> collagenases of the M9A subfamily are closely related to <i>Vibrio</i> pathogenesis for their role in collagen degradation during host invasion. Although some <i>Vibrio</i> collagenases have been characterized, the collagen degradation mechanism of <i>Vibrio</i> collagenase is still largely unknown. Here, an M9A collagenase, VP397, from marine Vibrio pomeroyi strain 12613 was characterized, and its fragmentation pattern on insoluble type I collagen fibers was studied. VP397 is a typical <i>Vibrio</i> collagenase composed of a catalytic module featuring a peptidase M9N domain and a peptidase M9 domain and two accessory bacterial prepeptidase C-terminal domains (PPC domains). It can hydrolyze various collagenous substrates, including fish collagen, mammalian collagens of types ","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Apr","modification":"2026-06-12T09:47:47.643Z","creation":"2024-11-06T07:22:46.224Z"},"accession":"S-EPMC9004396","cross_references":{"pubmed":["35285716"],"doi":["10.1128/aem.01677-21"]}}