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The mechanism of NDM-1-catalyzed carbapenem hydrolysis is distinct from that of penicillin or cephal...

The mechanism of NDM-1-catalyzed carbapenem hydrolysis is distinct from that of penicillin or cephal...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_3d6920df3c794045acc9dd9cd1b32ccc

The mechanism of NDM-1-catalyzed carbapenem hydrolysis is distinct from that of penicillin or cephalosporin hydrolysis

About this item

Full title

The mechanism of NDM-1-catalyzed carbapenem hydrolysis is distinct from that of penicillin or cephalosporin hydrolysis

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2017-12, Vol.8 (1), p.2242-2242, Article 2242

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

New Delhi metallo-β-lactamases (NDMs), the recent additions to metallo-β-lactamases (MBLs), pose a serious public health threat due to its highly efficient hydrolysis of β-lactam antibiotics and rapid worldwide dissemination. The MBL-hydrolyzing mechanism for carbapenems is less studied than that of penicillins and cephalosporins. Here, we report c...

Alternative Titles

Full title

The mechanism of NDM-1-catalyzed carbapenem hydrolysis is distinct from that of penicillin or cephalosporin hydrolysis

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_3d6920df3c794045acc9dd9cd1b32ccc

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_3d6920df3c794045acc9dd9cd1b32ccc

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-017-02339-w

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