Characterization of HMRZ-86: a novel chromogenic cephalosporin for the detection of extended-spectrum -lactamases | Zendy

Hideaki Hanaki | Zendy

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Characterization of HMRZ-86: a novel chromogenic cephalosporin for the detection of extended-spectrum -lactamases

Author(s) -

Hideaki Hanaki

Publication year - 2004

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/dkh166

Subject(s) - cephalosporin , chromogenic , ring (chemistry) , lactam , chemistry , double bond , hydrolysis , stereochemistry , antibiotics , chromatography , biochemistry , organic chemistry

Sir, HMRZ-86 is a new chromogenic cephalosporin. A carboxypropyl- oxyimino group bonded to the side chain at position 7 in the compound (Figure 1) protects the β-lactam ring from a range of β-lactamases, but not from extended-spectrum β-lactamases (ESBLs) or metallo-β-lactamases.1 Hydrolysis of the β-lactam ring by these enzymes changes the wavelength absorbed by the conjugated double bond located at position 3, shifting the colour of the com- pound from yellow to red, in much the same way as occurs with nitrocefin.2 In this study, we determined the usefulness of the com-

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