Abstract
HMRZ-86 was designed as a new chromogenic cephalosporin to detect extended-spectrum β-lactamases (ESBLs) and similar evolved β-lactamases, such as metallo-β-lactamases, derepressed AmpC, and extended oxacillinase. We report here our investigation of the kinetic parameters of several types of β-lactamases to show the enzymatic characteristics of HMRZ-86. The Michaelis constant (K m values of HMRZ-86 for ESBLs were twice to three and half times as high as those of nitrocefin, and the maximum velocity (Vmax) was one-fifth that of nitrocefin. The K m and Vmax of HMRZ-86 for AmpC were both smaller than those of nitrocefin. The kinetic parameters of HMRZ-86 for metallo β-lactamase (MBL) were very variable, depending on the type of buffer solution used and the concentration of zinc ions. For MBL, the K m values of HMRZ-86 were higher than those of nitrocefin, but the Vmax values were almost the same as those of nitrocefin. Although the chemical structure of HMRZ-86 is similar to that of nitrocefin, we think the enzymatic reactivities of the two entities for β-lactamases are very different.
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Hanaki, H., Koide, Y., Yamazaki, H. et al. Substrate specificity of HMRZ-86 for β-lactamases, including extended-spectrum β-lactamases (ESBLs). J Infect Chemother 13, 390–395 (2007). https://doi.org/10.1007/s10156-007-0563-2
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DOI: https://doi.org/10.1007/s10156-007-0563-2