beta-Lactamases are absent from Archaea (archaebacteria).
beta-Lactamases, enzymes that hydrolyze and inactive beta-lactam antibiotics, are of widespread occurrence in Bacteria and are related to the metabolism of bacterial cell wall murein. So far, no information exists on beta-lactamases in Archaea, a separate domain of prokaryotes with diverse types of unique cell wall polymers. Different mesophilic methanogenic and extremely halophilic Archaea containing methanochondroitin, pseudomurein, or S-layer protein or glycoprotein cell walls, were tested for beta-lactamase activity with the chromogenic beta-lactam nitrocefin as substrate. Also tested were representative microbial Eucarya from algae, yeasts, and protozoa. No beta-lactamase activity was detected in any of the archaeal and eukaryotic organisms. This supports the view that beta-lactamases are restricted to the domain of Bacteria.
Martin
H H
HH
Fachbereich 10-Biologie-Technische Hochschule Darmstadt, Germany.
König
H
H
D001105:Archaea / Q000201:enzymology* / Q000235:genetics / Q000648:ultrastructure; D001419:Bacteria / Q000378:metabolism; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism; D002473:Cell Wall / Q000378:metabolism; D002511:Cephalosporins / Q000378:metabolism; D003470:Culture Media; D001618:beta-Lactamases / Q000378:metabolism*
D002511:Cephalosporins; D003470:Culture Media; D001618:beta-Lactamases; C021720:nitrocefin