Neisseria gonorroeae penicillin-binding protein 3 exhibits exceptionally high carboxypeptidase and beta-lactam binding activities

Authors :: Stefanova, Miglena E.
Tomberg, Joshua
Olesky, Melanie
Holtje, Joachim-Volker
Gutheil, William G.; Nicholas, Robert A.
Source :: Biochemistry. Dec 16, 2003, Vol. 42 Issue 49, 14614-14625
Publication Year :: 2003
Abstract: Neisseria gonorroeae expressed a soluble form of penicillin-binding protein 3 (PBP 3) which was purified from Escherichia coli and characterized for its interaction with beta-lactam antibiotics, its catalytic properties with peptide and peptidoglycan substrates, and its role in cell viability and morphology.

Subjects :: Peptidoglycans -- Research
Escherichia coli -- Properties
Escherichia coli -- Research
Protein binding -- Research
Penicillin -- Research
Neisseria gonorrhoeae -- Research
Biological sciences
Chemistry

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