Increase of the deacylation rate of PBP2x from Streptococcus pneumoniae by single point mutations mimicking the class A beta-lactamases. (Q53976636)

23 May 2018

title

Increase of the deacylation rate of PBP2x from Streptococcus pneumoniae by single point mutations mimicking the class A beta-lactamases. (English)

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23 May 2018

main subject

Streptococcus pneumoniae

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André Zapun

2

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author name string

Laurent Chesnel

1

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23 May 2018

Nicolas Mouz

3

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23 May 2018

Otto Dideberg

4

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23 May 2018

Thierry Vernet

5

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23 May 2018

language of work or name

English

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publication date

1 March 2002

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23 May 2018

published in

FEBS Journal

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23 May 2018

volume

269

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23 May 2018

issue

6

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23 May 2018

page(s)

1678-1683

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23 May 2018

Serine beta-lactamases and penicillin-binding proteins

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1 reference

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Kinetics of beta-lactam interactions with penicillin-susceptible and -resistant penicillin-binding protein 2x proteins from Streptococcus pneumoniae. Involvement of acylation and deacylation in beta-lactam resistance

21 January 2018

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Inhibition of the expression of penicillin resistance in Streptococcus pneumoniae by inactivation of cell wall muropeptide branching genes.

21 January 2018

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Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8 A resolution

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Molecular structure of the acyl-enzyme intermediate in beta-lactam hydrolysis at 1.7 A resolution

21 January 2018

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X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme

21 January 2018

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Role of the omega-loop in the activity, substrate specificity, and structure of class A beta-lactamase

21 January 2018

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21 January 2018

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Mutations in the active site of penicillin-binding protein PBP2x from Streptococcus pneumoniae. Role in the specificity for beta-lactam antibiotics.

21 January 2018

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21 January 2018

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Biochemical characterization of penicillin-resistant and -sensitive penicillin-binding protein 2x transpeptidase activities of Streptococcus pneumoniae and mechanistic implications in bacterial resistance to beta-lactam antibiotics

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Active-site-serine D-alanyl-D-alanine-cleaving-peptidase-catalysed acyl-transfer reactions. Procedures for studying the penicillin-binding proteins of bacterial plasma membranes

21 January 2018

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21 January 2018

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Site-directed mutagenesis of glutamate 166 in two beta-lactamases. Kinetic and molecular modeling studies

21 January 2018

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Deacylation kinetics analysis of Streptococcus pneumoniae penicillin-binding protein 2x mutants resistant to beta-lactam antibiotics using electrospray ionization- mass spectrometry

21 January 2018

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10.1046/J.1432-1327.2002.02815.X

21 January 2018

Identifiers

DOI

1 reference

23 May 2018

PubMed ID

11895438

1 reference

23 May 2018