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R F Pratt
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Articles

Reaction of soluble penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus with β-lactams and acyclic substrates: kinetics in homogeneous solution

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Karen GRAVES-WOODWARD, R. F. PRATT
Journal: Biochemical Journal
Biochem J (1998) 332 (3): 755–761.
https://doi.org/10.1042/bj3320755
Published: 15 June 1998
View articletitled, Reaction of soluble penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus with β-lactams and acyclic substrates: kinetics in homogeneous solution
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Articles

Relative specificities of a series of β -lactam-recognizing enzymes towards the side-chains of penicillins and of acyclic thioldepsipeptides

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Y Xu, G Soto, H Adachi, M P van der Linden, W Keck, R F Pratt
Journal: Biochemical Journal
Biochem J (1994) 302 (3): 851–856.
https://doi.org/10.1042/bj3020851
Published: 15 September 1994
View articletitled, Relative specificities of a series of β -lactam-recognizing enzymes towards the side-chains of penicillins and of acyclic thioldepsipeptides
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Articles

Structure-activity relationships in the inhibition of serine β-lactamases by phosphonic acid derivatives

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J Rahil, R F Pratt
Journal: Biochemical Journal
Biochem J (1993) 296 (2): 389–393.
https://doi.org/10.1042/bj2960389
Published: 01 December 1993
View articletitled, Structure-activity relationships in the inhibition of serine β-lactamases by phosphonic acid derivatives
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Articles

Effect of side-chain amide thionation on turnover of β -lactam substrates by β -lactamases. Further evidence on the question of side-chain hydrogen-bonding in catalysis

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R F Pratt, R Krishnaraj, H Xu
Journal: Biochemical Journal
Biochem J (1992) 286 (3): 857–862.
https://doi.org/10.1042/bj2860857
Published: 15 September 1992
View articletitled, Effect of side-chain amide thionation on turnover of β -lactam substrates by β -lactamases. Further evidence on the question of side-chain hydrogen-bonding in catalysis
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Articles

Phosphonate monoester inhibitors of class A β -lactamases

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J Rahil, R F Pratt
Journal: Biochemical Journal
Biochem J (1991) 275 (3): 793–795.
https://doi.org/10.1042/bj2750793
Published: 01 May 1991
View articletitled, Phosphonate monoester inhibitors of class A β -lactamases
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Articles

Evidence from a mutant β -lactamase for the mechanism of β -lactamase-catalysed depsipeptide aminolysis

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L J Mazzella, S Pazhanisamy, R F Pratt
Journal: Biochemical Journal
Biochem J (1991) 274 (3): 855–859.
https://doi.org/10.1042/bj2740855
Published: 15 March 1991
View articletitled, Evidence from a mutant β -lactamase for the mechanism of β -lactamase-catalysed depsipeptide aminolysis
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Articles

Inactivation of the RTEM-1 cysteine β -lactamase by iodoacetate. The nature of active-site functional groups and comparisons with the native enzyme

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A K Knap, R F Pratt
Journal: Biochemical Journal
Biochem J (1991) 273 (1): 85–91.
https://doi.org/10.1042/bj2730085
Published: 01 January 1991
View articletitled, Inactivation of the RTEM-1 cysteine β -lactamase by iodoacetate. The nature of active-site functional groups and comparisons with the native enzyme
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Articles

Effect of the 3′-leaving group on turnover of cephem antibiotics by a class C β -lactamase

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L J Mazzella, R F Pratt
Journal: Biochemical Journal
Biochem J (1989) 259 (1): 255–260.
https://doi.org/10.1042/bj2590255
Published: 01 April 1989
View articletitled, Effect of the 3′-leaving group on turnover of cephem antibiotics by a class C β -lactamase
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Articles

A thiono- β -lactam substrate for the β -lactamase II of Bacillus cereus . Evidence for direct interaction between the essential metal ion and substrate

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B P Murphy, R F Pratt
Journal: Biochemical Journal
Biochem J (1989) 258 (3): 765–768.
https://doi.org/10.1042/bj2580765
Published: 15 March 1989
View articletitled, A thiono- β -lactam substrate for the β -lactamase II of Bacillus cereus . Evidence for direct interaction between the essential metal ion and substrate
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Articles

Evidence for an oxyanion hole in serine β-lactamases and dd-peptidases

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B P Murphy, R F Pratt
Journal: Biochemical Journal
Biochem J (1988) 256 (2): 669–672.
https://doi.org/10.1042/bj2560669
Published: 01 December 1988
View articletitled, Evidence for an oxyanion hole in serine β-lactamases and dd-peptidases
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Articles

Accumulation of acyl-enzyme intermediates during turnover of penicillins by the class A β -lactamase of Staphylococcus aureus PC1

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R F Pratt, T S McConnell, S J Murphy
Journal: Biochemical Journal
Biochem J (1988) 254 (3): 919–922.
https://doi.org/10.1042/bj2540919
Published: 15 September 1988
View articletitled, Accumulation of acyl-enzyme intermediates during turnover of penicillins by the class A β -lactamase of Staphylococcus aureus PC1
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Articles

Inactivation of the thiol RTEM-1 β -lactamase by 6- β -bromopenicillanic acid. Identity of the primary active-site nucleophile

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A K Knap, R F Pratt
Journal: Biochemical Journal
Biochem J (1987) 247 (1): 29–33.
https://doi.org/10.1042/bj2470029
Published: 01 October 1987
View articletitled, Inactivation of the thiol RTEM-1 β -lactamase by 6- β -bromopenicillanic acid. Identity of the primary active-site nucleophile
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Articles

Nucleophilic re-activation of the PC1 β-lactamase of Staphylococcus aureus and of the dd-peptidase of Streptomyces R61 after their inactivation by cephalosporins and cephamycins

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W S Faraci, R F Pratt
Journal: Biochemical Journal
Biochem J (1987) 246 (3): 651–658.
https://doi.org/10.1042/bj2460651
Published: 15 September 1987
View articletitled, Nucleophilic re-activation of the PC1 β-lactamase of Staphylococcus aureus and of the dd-peptidase of Streptomyces R61 after their inactivation by cephalosporins and cephamycins
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Articles

Interactions of cephalosporins with the Streptomyces R61 dd-transpeptidase/carboxypeptidase. Influence of the 3′-substituent

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W S Faraci, R F Pratt
Journal: Biochemical Journal
Biochem J (1986) 238 (1): 309–312.
https://doi.org/10.1042/bj2380309
Published: 15 August 1986
View articletitled, Interactions of cephalosporins with the Streptomyces R61 dd-transpeptidase/carboxypeptidase. Influence of the 3′-substituent
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