{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lu WJ"],"funding":["National Taiwan Ocean University"],"pagination":["e0032621"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8370199"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["65(9)"],"pubmed_abstract":["Vibrio vulnificus is a pathogen that accounts for one of the highest mortality rates and is responsible for most reported seafood-related illnesses and deaths worldwide. Owing to the threats of pathogens with β-lactamase activity, it is important to identify and characterize β-lactamases with clinical significance. In this study, the protein sequence of the metallo-β-lactamase (MBL) fold metallohydrolase from V. vulnificus (designated Vmh) was analyzed, and its oligomeric state, β-lactamase activity, and metal binding ability were determined. BLASTp analysis indicated that the V. vulnificus Vmh protein showed no significant sequence identity with any experimentally identified Ambler class B MBLs or enzymes containing the MBL protein fold; it was also predicted to have a signal peptide of 1"],"journal":["Antimicrobial agents and chemotherapy"],"pubmed_title":["A Novel Cooperative Metallo-β-Lactamase Fold Metallohydrolase from Pathogen Vibrio vulnificus Exhibits β-Lactam Antibiotic-Degrading Activities."],"pmcid":["PMC8370199"],"funding_grant_id":["NTOU-RD-AA-2019-1-02011-2, NTOU-RD-AA-2021-1-02018"],"pubmed_authors":["Lin HV","Hsu PH","Lu WJ"],"additional_accession":[]},"is_claimable":false,"name":"A Novel Cooperative Metallo-β-Lactamase Fold Metallohydrolase from Pathogen Vibrio vulnificus Exhibits β-Lactam Antibiotic-Degrading Activities.","description":"Vibrio vulnificus is a pathogen that accounts for one of the highest mortality rates and is responsible for most reported seafood-related illnesses and deaths worldwide. Owing to the threats of pathogens with β-lactamase activity, it is important to identify and characterize β-lactamases with clinical significance. In this study, the protein sequence of the metallo-β-lactamase (MBL) fold metallohydrolase from V. vulnificus (designated Vmh) was analyzed, and its oligomeric state, β-lactamase activity, and metal binding ability were determined. BLASTp analysis indicated that the V. vulnificus Vmh protein showed no significant sequence identity with any experimentally identified Ambler class B MBLs or enzymes containing the MBL protein fold; it was also predicted to have a signal peptide of 1","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Aug","modification":"2026-06-12T09:53:19.991Z","creation":"2025-02-19T03:24:06.88Z"},"accession":"S-EPMC8370199","cross_references":{"pubmed":["34228542"],"doi":["10.1128/aac.00326-21","10.1128/AAC.00326-21"]}}