Structural and biochemical characterization of the environmental MBLs MYO-1, ECV-1 and SHD-1 | Zendy

Christopher Frøhlich | Zendy; Vidar Sørum | Zendy; Sandra Huber | Zendy; Ørjan Samuelsen | Zendy; Fanny Berglund | Zendy; Erik Kristiansson | Zendy; Stathis D. Kotsakis | Zendy; Nachiket P. Marathe | Zendy; D. G. Joakim Larsson | Zendy; HannaKirsti S. Leiros | Zendy

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Structural and biochemical characterization of the environmental MBLs MYO-1, ECV-1 and SHD-1

Author(s) -

Christopher Frøhlich,

Vidar Sørum,

Sandra Huber,

Ørjan Samuelsen,

Fanny Berglund,

Erik Kristiansson,

Stathis D. Kotsakis,

Nachiket P. Marathe,

D. G. Joakim Larsson,

HannaKirsti S. Leiros

Publication year - 2020

Publication title -

journal of antimicrobial chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.124

H-Index - 194

eISSN - 1460-2091

pISSN - 0305-7453

DOI - 10.1093/jac/dkaa175

Subject(s) - thermostability , aztreonam , enzyme kinetics , enzyme , cephalosporin , homology modeling , biology , escherichia coli , microbiology and biotechnology , biochemistry , chemistry , antibiotics , computational biology , antibiotic resistance , active site , gene , imipenem

MBLs form a large and heterogeneous group of bacterial enzymes conferring resistance to β-lactam antibiotics, including carbapenems. A large environmental reservoir of MBLs has been identified, which can act as a source for transfer into human pathogens. Therefore, structural investigation of environmental and clinically rare MBLs can give new insights into structure-activity relationships to explore the role of catalytic and second shell residues, which are under selective pressure.

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