Dual activity of PNGM-1 pinpoints the evolutionary origin of subclass B3 metallo-beta-lactamases: a molecular and evolutionary study SCIE SCOPUS

DC Field Value Language
dc.contributor.author Lee, Jung Hun -
dc.contributor.author Takahashi, Masayuki -
dc.contributor.author Jeon, Jeong Ho -
dc.contributor.author Kang, Lin-Woo -
dc.contributor.author Seki, Mineaki -
dc.contributor.author Park, Kwang Seung -
dc.contributor.author Hong, Myoung-Ki -
dc.contributor.author Park, Yoon Sik -
dc.contributor.author Kim, Tae Yeong -
dc.contributor.author Karim, Asad Mustafa -
dc.contributor.author Lee, Jung-Hyun -
dc.contributor.author Nashimoto, Masayuki -
dc.contributor.author Lee, Sang Hee -
dc.date.accessioned 2020-12-10T08:00:52Z -
dc.date.available 2020-12-10T08:00:52Z -
dc.date.created 2020-05-27 -
dc.date.issued 2019-01 -
dc.identifier.issn 2222-1751 -
dc.identifier.uri https://sciwatch.kiost.ac.kr/handle/2020.kiost/38875 -
dc.description.abstract Resistance to beta-lactams is one of the most serious problems associated with Gram-negative infections. beta-Lactamases are able to hydrolyze beta-lactams such as cephalosporins and/or carbapenems. Evolutionary origin of metallo-beta-lactamases (MBLs), conferring critical antibiotic resistance threats, remains unknown. We discovered PNGM-1, the novel subclass B3 MBL, in deep-sea sediments that predate the antibiotic era. Here, our phylogenetic analysis suggests that PNGM-1 yields insights into the evolutionary origin of subclass B3 MBLs. We reveal the structural similarities between tRNase Zs and PNGM-1, and demonstrate that PNGM-1 has both MBL and tRNase Z activities, suggesting that PNGM-1 is thought to have evolved from a tRNase Z. We also show kinetic and structural comparisons between PNGM-1 and other proteins including subclass B3 MBLs and tRNase Zs. These comparisons revealed that the B3 MBL activity of PNGM-1 is a promiscuous activity and subclass B3 MBLs are thought to have evolved through PNGM-1 activity. -
dc.description.uri 1 -
dc.language English -
dc.publisher Nature Publishing Group -
dc.title Dual activity of PNGM-1 pinpoints the evolutionary origin of subclass B3 metallo-beta-lactamases: a molecular and evolutionary study -
dc.type Article -
dc.citation.endPage 1700 -
dc.citation.startPage 1688 -
dc.citation.title Emerging Microbes and Infections -
dc.citation.volume 8 -
dc.citation.number 1 -
dc.contributor.alternativeName 이정현 -
dc.identifier.bibliographicCitation Emerging Microbes and Infections, v.8, no.1, pp.1688 - 1700 -
dc.identifier.doi 10.1080/22221751.2019.1692638 -
dc.identifier.scopusid 2-s2.0-85075399344 -
dc.identifier.wosid 000498718400001 -
dc.type.docType Article -
dc.description.journalClass 1 -
dc.description.isOpenAccess N -
dc.subject.keywordPlus STANDARD NUMBERING SCHEME -
dc.subject.keywordPlus ANTIBIOTIC-RESISTANCE -
dc.subject.keywordPlus CRYSTAL-STRUCTURE -
dc.subject.keywordPlus RNA -
dc.subject.keywordPlus MECHANISM -
dc.subject.keywordAuthor Antimicrobial resistance -
dc.subject.keywordAuthor subclass B3 metallo-beta-lactamase -
dc.subject.keywordAuthor tRNase Z -
dc.subject.keywordAuthor dual activity -
dc.subject.keywordAuthor structure and evolutionary origin -
dc.relation.journalWebOfScienceCategory Immunology -
dc.relation.journalWebOfScienceCategory Microbiology -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -
dc.relation.journalResearchArea Immunology -
dc.relation.journalResearchArea Microbiology -
Appears in Collections:
Marine Resources Research Division > Marine Biotechnology Research Center > 1. Journal Articles
Files in This Item:
There are no files associated with this item.


Items in ScienceWatch@KIOST are protected by copyright, with all rights reserved, unless otherwise indicated.