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Bacterial Enzymes Interacting with β-Lactam Antibiotics

  • N. H. Georgopapadakou
  • R. B. Sykes
Part of the Handbook of Experimental Pharmacology book series (HEP, volume 67 / 2)

Abstract

Development of β-lactam antibiotics over the past 40 years represents an unparalleled effort in the history of antimicrobial chemotherapy. The continual emergence of new compounds, natural, semisynthetic, and synthetic, is a tribute to the research programs being carried out around the world. Alongside the intensive search for new and improved β-lactam antibiotics has been the study of enzymes that interact with these molecules.

Keywords

Antimicrob Agent Clavulanic Acid Bacterial Enzyme Substrate Profile Transpeptidase Activity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Abbreviations

6-APA

6-Aminopenicillanic acid

pCMB

p-chloromercuribenzoate

Diac-l-Lys-d-Ala-d-Ala

α,ε-diacetyl-l-lysyl-d-alanyl-d-alanine

Diac-l-Lys-d-Ala-d-Lac

α,ε-diacetal-l-lysyl-d-alanyl-d-lactate

DFP

diisopropylfluorophosphate

DTNB

5,5′-dithiobis (2-nit- \( \overline r \) obenzoic acid)

pI

isoelectric point

MSF

methanesulfonyl fluoride

MIC

minimum inhibitory concentration

NEM

N-ethylmaleimide

PBP

penicillin-binding protein

PSE

penicillin-sensitive enzyme

SDS

sodium dodecylsulfate

UDP-MurNac-l-Ala-d-Glumeso-Dap-d-Ala-d-Ala

UDP-N-acetylmuramyl-l-alanyl-γ-d-glutamyl-meso-2,6-diaminopimelyl-d-alanyl-d-alanine

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Copyright information

© Springer-Verlag Berlin Heidelberg 1983

Authors and Affiliations

  • N. H. Georgopapadakou
  • R. B. Sykes

There are no affiliations available

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