Search Results - "Pratt, R.F."

Structures of Two Kinetic Intermediates Reveal Species Specificity of Penicillin-binding Proteins by McDonough, Michael A, Anderson, John W, Silvaggi, Nicholas R, Pratt, R.F, Knox, James R, Kelly, Judith A

“…Penicillin-binding proteins (PBPs), the target enzymes of β-lactam antibiotics such as penicillins and cephalosporins, catalyze the final peptidoglycan…”
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Detection of an enzyme isomechanism by means of the kinetics of covalent inhibition by Adediran, S.A., Morrison, Michael J., Pratt, R.F.

“…Turnover of substrates by many enzymes involves free enzyme forms that differ from the stable form of the enzyme in the absence of substrate. These enzyme…”
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Penicillin acylase and O-aryloxycarbonyl hydroxamates: Two acyl-enzymes, one leading to hydrolysis, the other to inactivation by Adediran, S.A., Pratt, R.F.

“…O-Aryloxycarbonyl hydroxamates have previously been shown to covalently inactivate serine/amine amidohydrolases such as class C β-lactamases and a N-terminal…”
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Intramolecular Cooperativity in the Reaction of Diacyl Phosphates with Serine ß-Lactamases by Majumdar, Sudipta, Pratt, R.F.

“…Asymmetric diaroyl phosphates (ArCOOPO 2 − OCOAr′, where Ar = Ph, Ar′ = 4-biphenyl, 2-benzothiophenyl and 2-benzofuranyl), have been prepared, evaluated as…”
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Specificity of extended O-aryloxycarbonyl hydroxamates as inhibitors of a class C β-lactamase by Malico, Alexandra A., Dave, K., Adediran, S.A., Pratt, R.F.

“…[Display omitted] Class C β-lactamases have previously been shown to be efficiently inactivated by O-aryloxycarbonyl hydroxamates…”
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Specificity and mechanism of mandelamide hydrolase catalysis by Adediran, S.A., Wang, Pan-Fen, Shilabin, Abbas G., Baron, Charles A., McLeish, Michael J., Pratt, R.F.

“…The best-studied amidase signature (AS) enzyme is probably fatty acid amide hydrolase (FAAH). Closely related to FAAH is mandelamide hydrolase (MAH), whose…”
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Inhibition of Class A and C β-Lactamases by Diaroyl Phosphates by Majumdar, Sudipta, Pratt, R. F

“…A series of diaroyl phosphates was employed to assess the general reactivity of this class of molecule against classical class A and class C β-lactamases. The…”
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β-Ketophosphonates as β-lactamase inhibitors: Intramolecular cooperativity between the hydrophobic subsites of a class D β-lactamase by Perumal, Senthil K., Adediran, S.A., Pratt, R.F.

“…A series of aryl and arylmethyl β-aryl-β-ketophosphonates have been prepared as potential β-lactamase inhibitors. These compounds, as fast, reversible,…”
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Kinetics and Mechanism of Inhibition of a Serine β-Lactamase by O-Aryloxycarbonyl Hydroxamates by Pelto, Ryan B, Pratt, R. F

“…The class C serine β-lactamase of Enterobacter cloacae P99 is irreversibly inhibited by O-aryloxycarbonyl hydroxamates. A series of these new inhibitors has…”
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Inhibition of dd-Peptidases by a Specific Trifluoroketone: Crystal Structure of a Complex with the Actinomadura R39 dd-Peptidase by Dzhekieva, Liudmila, Adediran, S. A, Herman, Raphael, Kerff, Frédéric, Duez, Colette, Charlier, Paulette, Sauvage, Eric, Pratt, R. F

“…Inhibitors of bacterial dd-peptidases represent potential antibiotics. In the search for alternatives to β-lactams, we have investigated a series of compounds…”
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Crossover inhibition as an indicator of convergent evolution of enzyme mechanisms: A β-lactamase and a N-terminal nucleophile hydrolase by Adediran, S.A., Lin, G., Pelto, R.B., Pratt, R.F.

“…► A cross-check of two inhibitors shows both inhibit a β-lactamase and a proteasome. ► Similar inhibition mechanisms and similar products. ► Active site…”
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Crystal Structures of Covalent Complexes of [beta]-Lactam Antibiotics with Escherichia coli Penicillin-Binding Protein 5: Toward an Understanding of Antibiotic Specificity by Nicola, George, Tomberg, Joshua, Pratt, R.F., Nicholas, Robert A., Davies, Christopher

“…Penicillin-binding proteins (PBPs) are the molecular targets for the widely used {beta}-lactam class of antibiotics, but how these compounds act at the…”
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Crystal Structures of Complexes of Bacterial dd-Peptidases with Peptidoglycan-Mimetic Ligands: The Substrate Specificity Puzzle by Sauvage, Eric, Powell, Ailsa J., Heilemann, Jason, Josephine, Helen R., Charlier, Paulette, Davies, Christopher, Pratt, R.F.

“…The X-ray crystal structures of covalent complexes of the Actinomadura R39 dd-peptidase and Escherichia coli penicillin-binding protein (PBP) 5 with β-lactams…”
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Approaches to the simultaneous inactivation of metallo-and serine-β-lactamases by REDDY GANTA, Sudhakar, PERUMAL, Senthil, REDDY PAGADALA, Sundar Ram, SAMUELSEN, Ørjan, SPENCER, James, PRATT, R. F, BUYNAK, John D

“…A series of cephalosporin-derived reverse hydroxamates and oximes were prepared and evaluated as inhibitors of representative metallo- and…”
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Crystal Structure of the Bacillus subtilis Penicillin-binding Protein 4a, and its Complex with a Peptidoglycan Mimetic Peptide by Sauvage, Eric, Duez, Colette, Herman, Raphaël, Kerff, Frédéric, Petrella, Stephanie, Anderson, John W., Adediran, S.A., Pratt, R.F., Frère, Jean-Marie, Charlier, Paulette

“…The genome of Bacillus subtilis encodes 16 penicillin-binding proteins (PBPs) involved in the synthesis and/or remodelling of the peptidoglycan during the…”
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Inhibition of Chymotrypsin by a Complex of Ortho-Vanadate and Benzohydroxamic Acid:  Structure of the Inert Complex and Its Mechanistic Interpretation by Moulin, Aaron, Bell, Jason H, Pratt, R. F, Ringe, Dagmar

“…Serine proteases, like serine β-lactamases, are rapidly and covalently inhibited by suitably designed phosph(on)ates. The active sites of these enzymes must,…”
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Crystal structures of complexes between the R61 DD-peptidase and peptidoglycan-mimetic beta-lactams: a non-covalent complex with a "perfect penicillin" by Silvaggi, Nicholas R, Josephine, Helen R, Kuzin, Alexandre P, Nagarajan, Rajesh, Pratt, R F, Kelly, Judith A

“…The bacterial D-alanyl-D-alanine transpeptidases (DD-peptidases) are the killing targets of beta-lactams, the most important clinical defense against bacterial…”
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Reactions of Peptidoglycan-Mimetic β-Lactams with Penicillin-Binding Proteins in Vivo and in Membranes by Kumar, Ish, Josephine, Helen R, Pratt, R. F

“…The membrane-bound bacterial d-alanyl-d-alanine peptidases or penicillin-binding proteins (PBPs) catalyze the final transpeptidation reaction of bacterial cell…”
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Substituted aryl malonamates as new serine β-lactamase substrates: Structure–activity studies by Adediran, S.A., Cabaret, D., Lohier, J.-F., Wakselman, M., Pratt, R.F.

“…A series of substituted aryl malonamates have been prepared. These compounds are analogues of aryl phenaceturates where the amido side chain has been replaced…”
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Deacylation Transition States of a Bacterial DD-Peptidase by Adediran, S. A, Kumar, I, Pratt, R. F

“…β-Lactam antibiotics restrict bacterial growth by inhibiting DD-peptidases. These enzymes catalyze the final transpeptidation step in bacterial cell wall…”
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