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Substrate specificity of bacterial DD-peptidases (penicillin-binding proteins)

Cellular and molecular life sciences : CMLS, 2008-07, Vol.65 (14), p.2138-2155

Pratt, R. F

2008

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A Lysine-Targeted Affinity Label for Serine-β-Lactamase Also Covalently Modifies New Delhi Metallo-β-lactamase‑1 (NDM-1)

Biochemistry (Easton), 2019-06, Vol.58 (25), p.2834-2843

2019

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Elusive structural changes of New Delhi metallo-β-lactamase revealed by ultraviolet photodissociation mass spectrometry

Chemical science (Cambridge), 2020-09, Vol.11 (33), p.8999-91

2020

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Kinetic Evidence for a Second Ligand Binding Site on Streptococcus pneumoniae Penicillin-Binding Protein 2x

Biochemistry (Easton), 2018-03, Vol.57 (11), p.1758-1766

2018

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Kinetics of Action of a Two-Stage Pro-Inhibitor of Serine β‑Lactamases

Biochemistry (Easton), 2013-10, Vol.52 (40), p.7060-7070

2013

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Structural Relationship between the Active Sites of β-Lactam-Recognizing and Amidase Signature Enzymes: Convergent Evolution?

Biochemistry (Easton), 2010-11, Vol.49 (45), p.9688-9697

2010

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Interactions of “Bora-Penicilloates” with Serine β‑Lactamases and DD-Peptidases

Biochemistry (Easton), 2014-10, Vol.53 (41), p.6530-6538

2014

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Inhibition of Bacterial DD-Peptidases (Penicillin-Binding Proteins) in Membranes and in Vivo by Peptidoglycan-Mimetic Boronic Acids

Biochemistry (Easton), 2012-04, Vol.51 (13), p.2804-2811

2012

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A New Covalent Inhibitor of Class C β‑Lactamases Reveals Extended Active Site Specificity

Biochemistry (Easton), 2015-12, Vol.54 (50), p.7375-7384

2015

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Covalent Inhibition of Serine β‑Lactamases by Novel Hydroxamic Acid Derivatives

Biochemistry (Easton), 2013-05, Vol.52 (21), p.3712-3720

2013

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β-Lactamases: Why and How

Journal of medicinal chemistry, 2016-09, Vol.59 (18), p.8207-8220

Pratt, R F

2016

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Synthesis and Kinetic Analysis of Two Conformationally Restricted Peptide Substrates of Escherichia coli Penicillin-Binding Protein 5

Biochemistry (Easton), 2016-07, Vol.55 (29), p.4065-4076

2016

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Crystal Structures of Covalent Complexes of β-Lactam Antibiotics with Escherichia coli Penicillin-Binding Protein 5: Toward an Understanding of Antibiotic Specificity

Biochemistry (Easton), 2010-09, Vol.49 (37), p.8094-8104

2010

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Crystal Structure of a Complex between the Actinomadura R39 dd-Peptidase and a Peptidoglycan-mimetic Boronate Inhibitor: Interpretation of a Transition State Analogue in Terms of Catalytic Mechanism

Biochemistry (Easton), 2010-08, Vol.49 (30), p.6411-6419

2010

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Substrate Specificity of Low-Molecular Mass Bacterial dd-Peptidases

Biochemistry (Easton), 2011-11, Vol.50 (46), p.10091-10101

2011

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Unexpected Tricovalent Binding Mode of Boronic Acids within the Active Site of a Penicillin-Binding Protein

Journal of the American Chemical Society, 2011-07, Vol.133 (28), p.10839-10848

2011

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Dual Substrate Specificity of Bacillus subtilis PBP4a

Biochemistry (Easton), 2013-04, Vol.52 (15), p.2627-2637

2013

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Inhibition of Class A and C β-Lactamases by Diaroyl Phosphates

Biochemistry (Easton), 2009-09, Vol.48 (35), p.8285-8292

2009

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β-Ketophosphonates as β-lactamase inhibitors: Intramolecular cooperativity between the hydrophobic subsites of a class D β-lactamase

Bioorganic & medicinal chemistry, 2008-07, Vol.16 (14), p.6987-6994

2008

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Kinetics and Mechanism of Inhibition of a Serine β-Lactamase by O-Aryloxycarbonyl Hydroxamates

Biochemistry (Easton), 2008-11, Vol.47 (46), p.12037-12046

2008

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Inhibition of dd-Peptidases by a Specific Trifluoroketone: Crystal Structure of a Complex with the Actinomadura R39 dd-Peptidase

Biochemistry (Easton), 2013-03, Vol.52 (12), p.2128-2138

2013

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β‑Lactamases: Why and How: Miniperspective

Journal of medicinal chemistry, 2016-09, Vol.59 (18), p.8207-8220

Pratt, R. F

2016

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Neutral β‑Lactams Inactivate High Molecular Mass Penicillin-Binding Proteins of Class B1, Including PBP2a of MRSA

ACS medicinal chemistry letters, 2014-02, Vol.5 (2), p.154-157

2014

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Crystal Structures of Complexes of Bacterial dd-Peptidases with Peptidoglycan-Mimetic Ligands: The Substrate Specificity Puzzle

Journal of molecular biology, 2008-08, Vol.381 (2), p.383-393

2008

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Serendipitous Discovery of α-Hydroxyalkyl Esters as β-Lactamase Substrates

Biochemistry (Easton), 2010-12, Vol.49 (49), p.10496-10506

2010

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1 – 25 von 1.761

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Substrate specificity of bacterial DD-peptidases (penicillin-binding proteins)

A Lysine-Targeted Affinity Label for Serine-β-Lactamase Also Covalently Modifies New Delhi Metallo-β-lactamase‑1 (NDM-1)

Elusive structural changes of New Delhi metallo-β-lactamase revealed by ultraviolet photodissociation mass spectrometry

Kinetic Evidence for a Second Ligand Binding Site on Streptococcus pneumoniae Penicillin-Binding Protein 2x

Kinetics of Action of a Two-Stage Pro-Inhibitor of Serine β‑Lactamases

Structural Relationship between the Active Sites of β-Lactam-Recognizing and Amidase Signature Enzymes: Convergent Evolution?

Interactions of “Bora-Penicilloates” with Serine β‑Lactamases and DD-Peptidases

Inhibition of Bacterial DD-Peptidases (Penicillin-Binding Proteins) in Membranes and in Vivo by Peptidoglycan-Mimetic Boronic Acids

A New Covalent Inhibitor of Class C β‑Lactamases Reveals Extended Active Site Specificity

Covalent Inhibition of Serine β‑Lactamases by Novel Hydroxamic Acid Derivatives

β-Lactamases: Why and How

Synthesis and Kinetic Analysis of Two Conformationally Restricted Peptide Substrates of Escherichia coli Penicillin-Binding Protein 5

Crystal Structures of Covalent Complexes of β-Lactam Antibiotics with Escherichia coli Penicillin-Binding Protein 5: Toward an Understanding of Antibiotic Specificity

Crystal Structure of a Complex between the Actinomadura R39 dd-Peptidase and a Peptidoglycan-mimetic Boronate Inhibitor: Interpretation of a Transition State Analogue in Terms of Catalytic Mechanism

Substrate Specificity of Low-Molecular Mass Bacterial dd-Peptidases

Unexpected Tricovalent Binding Mode of Boronic Acids within the Active Site of a Penicillin-Binding Protein

Dual Substrate Specificity of Bacillus subtilis PBP4a

Inhibition of Class A and C β-Lactamases by Diaroyl Phosphates

β-Ketophosphonates as β-lactamase inhibitors: Intramolecular cooperativity between the hydrophobic subsites of a class D β-lactamase

Kinetics and Mechanism of Inhibition of a Serine β-Lactamase by O-Aryloxycarbonyl Hydroxamates

Inhibition of dd-Peptidases by a Specific Trifluoroketone: Crystal Structure of a Complex with the Actinomadura R39 dd-Peptidase

β‑Lactamases: Why and How: Miniperspective

Neutral β‑Lactams Inactivate High Molecular Mass Penicillin-Binding Proteins of Class B1, Including PBP2a of MRSA

Crystal Structures of Complexes of Bacterial dd-Peptidases with Peptidoglycan-Mimetic Ligands: The Substrate Specificity Puzzle

Serendipitous Discovery of α-Hydroxyalkyl Esters as β-Lactamase Substrates

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