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

Stefanova, Miglena E

Neisseria gonorrhoeae penicillin-binding protein 3 exhibits exceptionally high carboxypeptidase and beta-lactam binding activities. [electronic resource] - Biochemistry Dec 2003 - 14614-25 p. digital

Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.

0006-2960

10.1021/bi0350607 doi


Acylation
Anti-Bacterial Agents--chemistry
Bacterial Proteins--antagonists & inhibitors
Carrier Proteins--antagonists & inhibitors
Cell Division--genetics
Cell Survival--genetics
Cloning, Molecular
Drug Resistance, Microbial
Endopeptidases--chemistry
Enzyme Stability
Escherichia coli Proteins
Gene Expression Regulation, Bacterial
Hexosyltransferases--antagonists & inhibitors
Hydrogen-Ion Concentration
Microscopy, Electron, Scanning
Molecular Sequence Data
Muramoylpentapeptide Carboxypeptidase--antagonists & inhibitors
Neisseria gonorrhoeae--enzymology
Penicillin-Binding Proteins
Peptidoglycan Glycosyltransferase
Peptidyl Transferases--antagonists & inhibitors
Protein Binding
Substrate Specificity
beta-Lactams--chemistry