000 02068 a2200541 4500
005 20250514163600.0
264 0 _c20040408
008 200404s 0 0 eng d
022 _a0006-2960
024 7 _a10.1021/bi0350607
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aStefanova, Miglena E
245 0 0 _aNeisseria gonorrhoeae penicillin-binding protein 3 exhibits exceptionally high carboxypeptidase and beta-lactam binding activities.
_h[electronic resource]
260 _bBiochemistry
_cDec 2003
300 _a14614-25 p.
_bdigital
500 _aPublication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
650 0 4 _aAcylation
650 0 4 _aAnti-Bacterial Agents
_xchemistry
650 0 4 _aBacterial Proteins
_xantagonists & inhibitors
650 0 4 _aCarrier Proteins
_xantagonists & inhibitors
650 0 4 _aCell Division
_xgenetics
650 0 4 _aCell Survival
_xgenetics
650 0 4 _aCloning, Molecular
650 0 4 _aDrug Resistance, Microbial
650 0 4 _aEndopeptidases
_xchemistry
650 0 4 _aEnzyme Stability
650 0 4 _aEscherichia coli Proteins
650 0 4 _aGene Expression Regulation, Bacterial
650 0 4 _aHexosyltransferases
_xantagonists & inhibitors
650 0 4 _aHydrogen-Ion Concentration
650 0 4 _aMicroscopy, Electron, Scanning
650 0 4 _aMolecular Sequence Data
650 0 4 _aMuramoylpentapeptide Carboxypeptidase
_xantagonists & inhibitors
650 0 4 _aNeisseria gonorrhoeae
_xenzymology
650 0 4 _aPenicillin-Binding Proteins
650 0 4 _aPeptidoglycan Glycosyltransferase
650 0 4 _aPeptidyl Transferases
_xantagonists & inhibitors
650 0 4 _aProtein Binding
650 0 4 _aSubstrate Specificity
650 0 4 _abeta-Lactams
_xchemistry
700 1 _aTomberg, Joshua
700 1 _aOlesky, Melanie
700 1 _aHöltje, Joachim-Volker
700 1 _aGutheil, William G
700 1 _aNicholas, Robert A
773 0 _tBiochemistry
_gvol. 42
_gno. 49
_gp. 14614-25
856 4 0 _uhttps://doi.org/10.1021/bi0350607
_zAvailable from publisher's website
999 _c14395617
_d14395617