Publications since
1985 1.
W. S. Faraci, R. F. Pratt, “Mechanism of Inhibition
of the PCl ß-Lactamase of S.aureus by
Cephalosporins: Importance of the 3¢-Leaving
Group.” Biochemistry 24, 903-910
(1985).
2.
R. F. Pratt, W. S. Faraci, C. P. Govardhan, “A
Direct Spectrophotometric Assay for D-Alanine
Carboxypeptidases and for the Esterase Activity of
ß-Lactamases.” Analytical Biochemistry 144,
204-206 (1985).
3.
W. S. Faraci, R. F. Pratt, “Mechanism of Inhibition
of the RTEM-2 ß-Lactamase by Cephamycins: Relative
Importance of the 7a-Methoxy Group and the 3¢-Leaving
Group.” Biochemistry 25, 2934-2941
(1986).
4.
R. F. Pratt, W. S. Faraci, “Direct Observation by 1H
NMR of Cephalosporoate Intermediates in Aqueous Solution
During the Hydrazinolysis and the ß-Lactamase-Catalysed
Hydrolysis of Cephalosporins with 3¢-Leaving Groups:
Kinetics and Equilibria of the 3¢-Elimination
Reaction.” J. Amer. Chem. Soc. 108,
5328-5333 (1986).
5.
W. S. Faraci, R. F. Pratt, “Interactions of
Cephalosporins with the Streptomyces R61
DD-trans-peptidase/carboxypeptidase. Influence of the 3¢-Substituent.”
Biochem. J. 238, 309-312 (1986).
6.
W. S. Faraci, R. F. Pratt, “Nucleophilic
Reactivation of the PCl ß-Lactamase of Staphylococcus
aureus and of the DD-peptidase of Streptomyces R61
Following their Inactivation by Cephalosporins and
Cephamycins.” Biochem. J. 246, 651-658
(1987).
7.
C. P. Govardhan, R. F. Pratt, “Kinetics and
Mechanism of the Serine ß-Lactamase Catalysed Hydrolysis
of Depsipeptides.” Biochemistry 26,
3385-3395 (1987).
8.
P. H. Popieniek, R. F. Pratt, “A Fluorescent Ligand
for Binding Studies with the Glycopeptide
Antibiotics.” Analytical Biochemistry 165,
108-113 (1987).
9.
K. Knap, R. F. Pratt, “Inactivation of the Thiol
RTEM-1 ß-Lactamase by 6-ß-Bromopenicillanic Acid.
Identity of the Primary Active Site Nucleophile.” Biochem.
J. 247, 29-33 (1987).
10.
M. E. Grace, D. P. Schenkein, R. F. Pratt, “Kinetics
and Mechanism of Inactivation of the RTEM-2 ß-Lactamase
by Phenylpropynal. Identification of the Characteristic
Chromophore." J. Biol. Chem. 262,
16778-16785 (1987).
11.
P. H. Popieniek, R. F. Pratt, “Rates of Specific
Peptide Binding to the Glycopeptide Antibiotics
Vancomycin, Ristocetin and Avoparcin.” J. Amer.
Chem. Soc. 110, 1285-1286 (1988).
12.
R. F. Pratt, D. J. Cahn, “On the Mechanism of
Rearrangement of 6-Halopenicilloates to
2,3-Dihydro-1,4-thiazines.” J. Amer. Chem. Soc.
110, 5096-5104 (1988).
13.
R. F. Pratt, T. S. McConnell, S. J. Murphy,
“Accumulation of Acyl-Enzyme Intermediates during
Turnover of Penicillins by the Class A ß-Lactamase of Staphylococcus
aureus PC1.” Biochem J. 254,
919-922 (1988).
14.
B. P. Murphy, R. F. Pratt, “Evidence for an Oxyanion
Hole in Serine ß-Lactamases and DD-Peptidases.” Biochem.
J. 256, 669-672 (1988).
15.
L. J. Mazzella, R. F. Pratt, “Effect of the 3¢-Leaving
Group on Turnover of Cephem Antibiotics by a Class C
ß-Lactamase.” Biochem. J. 259,
255-260 (1989).
16.
B. P. Murphy, R. F. Pratt, “A Thiono-ß-Lactam
Substrate for the ß-Lactamase II of Bacillus.
Evidence for Direct Interaction Between the Essential
Metal Ion and the Substrate.” Biochem. J. 258,
765-768 (1989).
17.
R. F. Pratt, “ß-Lactamase Inhibitors,” in Design
of Enzyme Inhibitors as Drugs, M. Sandler and H. J.
Smith, eds., Oxford University Press (1989).
18.
S. Pazhanisamy, C. P. Govardhan, R. F. Pratt, “The
ß-Lactamase-Catalysed Aminolysis of Depsipeptides: Amine
Specificity and Steady-State Kinetics.” Biochemistry
28, 6863-6870 (1989).
19.
S. Pazhanisamy, R. F. Pratt, “The
ß-Lactamase-Catalysed Aminolysis of Depsipeptides: Proof
of the Non-Existence of a Specific D-Phenylalanine-Enzyme
Complex by Double Label Isotope-Trapping.” Biochemistry
28, 6870-6875 (1989).
20.
S. Pazhanisamy, R. F. Pratt, “The
ß-Lactamase-Catalysed Aminolysis of Depsipeptide:
Peptide Inhibition and a New Kinetic Mechanism.” Biochemistry
28, 6875-6882 (1989).
21.
K. Knap, R. F. Pratt, “Chemical Modification of the
RTEM-1 Thiol ß-Lactamase by Thiol-Selective Reagents:
Evidence for Activation of the Primary Nucleophile of the
ß-Lactamase Active Site by Adjacent Functional
Groups.” Proteins: Structure Function and
Genetics 6, 316-323 (1989).
22.
R. F. Pratt, “Inhibition of a Class C ß-Lactamase
by a Specific Phosphonate Monoester.” Science 246,
917-919 (1989).
23.
J. R. Knox, R. F. Pratt, “Different Modes of
Vancomycin and D-Alanyl-D-Alanine Peptidase Binding to
Cell Wall Peptide and a Possible Role for the Vancomycin
Resistance Protein.” Antimicrob. Agents
Chemother. 34, 1342-1347 (1990).
24.
K. Knap, R. F. Pratt, “Inactivation of the RTEM-1
Thiol ß-Lactamase by Iodoacetate: The Nature of Active
Site Functional Groups and Comparisons with the Native
Enzyme.” Biochem. J. 273, 85-91
(1991).
25.
P. H. Popieniek, R. F. Pratt, “Kinetics and
Mechanism of Binding of Specific Peptides to Vancomycin
and Other Glycopeptide Antibiotics.” J. Amer.
Chem. Soc. 113, 2264-2270 (1991).
26.
B . P. Murphy, R. F. Pratt,
"N-(Phenylacetyl)glycyl-D-Aziridine-2-Carboxylate,
an Acyclic Amide Substrate of ß-Lactamases: The
Importance of Shape of the Active Site in ß-Lactamase
Evolution." Biochemistry 30, 36403649
(1991).
27.
L. J. Mazzella, S. Pazhanisamy, R. F. Pratt,
“Evidence from a Mutant ß-Lactamase for the
Mechanism of ß-Lactamase-Catalysed Depsipeptide
Aminolysis.” Biochem J. 274, 855-859
(1991).
28.
J. Rahil, R. F. Pratt, “Phosphonate Monoester
Inhibitors of Class A ß-Lactamases.” Biochem J.
275, 793-795 (1991).
29.
J. Rahil, R. F. Pratt, “Intramolecular Participation
of the Amide Group in Acid and Base-Catalysed Phosphonate
Monoester Hydrolysis.” J. Chem. Soc. Perkin Trans
2, 947 (1991).
30.
R. F. Pratt, R. Krishnaraj, H. Xu, “Effect of
Side-Chain Thionation on Turnover of ß-Lactam Substrates
by ß-Lactamases: Further Evidence on the Question of
Side-Chain Hydrogen-Bonding in Catalysis.”
Biochem. J. 286, 857-862 (1992).
31.
J. Rahil, R. F. Pratt, "Mechanism of Inhibition of
the Class C ß-Lactamase of Enterobacter cloacae
P99 by a Phosphonate Monoester." Biochemistry
31, 5869-5878 (1992).
32.
R. F. Pratt, “ß-Lactamase Inhibition” in The
Chemistry of ß-Lactams, M. I. Page, ed., Chapman and
Hall, 1992.
33.
R. F. Pratt, “On the Definition and Classification
of Mechanism-Based Enzyme Inhibitors.” Bioorg.
Med. Chem. Lett. 2, 1323-1326 (1992).
34.
J. Rahil, R. F. Pratt, “Kinetics and Mechanism of
ß-Lactamase Inhibition by Phosphonamidates: The Quest
for a Proton.” Biochemistry 32,
1076310772 (1993).
35.
C. C. H. Chen, J. Rahil, R. F. Pratt, O. Herzberg,
“Structure of a Phosphonate-Inhibited ß-Lactamase:
An Analog of the Tetrahedral Transition
State/Intermediate of ß-Lactam Hydrolysis.” J.
Mol. Biol. 234, 165178 (1993).
36.
J. Rahil, R. F. Pratt, “Structure-Activity
Relationships in the Inhibition of Serine ß-Lactamases
by Phosphonic Acid Derivatives.” Biochem. J. 296,
389-393 (1993).
37.
J. Rahil, R. F. Pratt, “Characterization of
Covalently-Bound Enzyme Inhibitors as Transition State
Analogs by Protein Stability Measurements: Phosphonate
Monoester Inhibitors of a ß-Lactamase.” Biochemistry
33, 116-125 (1994).
38.
E. Lobkovsky, E. M. Billings, P. C. Moews, J. Rahil, R.
F. Pratt, J. R. Knox, “Crystallographic
Structure of a Phosphonate Derivative of the Enterobacter
cloacae P99 Cephalosporinase: Mechanistic
Interpretation of a ß-Lactamase Transition State.” Biochemistry
33, 6762-6772 (1994).
39.
D. Cabaret, J. Liu, M. Wakselman, R. F. Pratt, Y. Xu,
“Functionalized Depsipeptides, Substrates and
Inhibitors of ß-Lactamases and DD-Peptidases.” Bioorg.
Med. Chem. 2, 757-771 (1994).
40.
Y. Xu, G. Soto, H. Adachi, M. P. G. van der Linden, W.
Keck, R. F. Pratt, “The Relative Specificities of a
Series of ß-Lactam-Recognizing Enzymes Toward the
Side-Chains of Penicillins and Acyclic
Thioldepsipeptides.” Biochem. J. 302,
851-856 (1994).
41.
Y. Xu, R. F. Pratt, “ß-Lactam-Recognizing Enzymes
Exhibit Different Structural Specificity in Acyclic Amide
and Ester Substrates: A Starting Point in ß-Lactamase
Evolution?” Bioorg. Med. Chem. Letts. 4,
2291-2296 (1994).
42.
S. Vijayakumar, G. Ravishanker, R. F. Pratt, D. L.
Beveridge, “Molecular Dynamics Simulation of a Class
A ß-Lactamase: Structural and Mechanistic
Implications.” J. Amer. Chem. Soc. 117,
1722-1730 (1995).
43.
M. Dryjanski, R. F. Pratt, “Steady State Kinetics of
the Binding of ß-Lactams and Penicilloates to the Second
Binding Site of the Enterobacter cloacae P99
ß-Lactamase.” Biochemistry 34,
3561-3568 (1995).
44.
M. Dryjanski, R. F. Pratt, “Inactivation of the Enterobacter
cloacae P99 ß-Lactamase by a Fluorescent
Phosphonate: Direct Detection of Ligand Binding at the
Second Site.” Biochemistry 34,
3569-3575 (1995).
45.
S. A. Deraniyagala, S. A. Adediran, R. F. Pratt,
“ß-Secondary and Solvent Deuterium Kinetic Isotope
Effects and the Mechanisms of Base and Acid-Catalysed
Hydrolysis of Penicillanic Acid.” J. Org. Chem.
60, 1619-1625 (1995).
46.
Y. Xu, G. Soto, K. R. Hirsch, R. F. Pratt, “Kinetics
and Mechanism of the Hydrolysis of Depsipeptides
Catalyzed by the ß-Lactamase of Enterobacter cloacae
P99.” Biochemistry 35, 3595-3603
(1996).
47.
S. A. Adediran, S. A. Deraniyagala, Y. Xu, R. F. Pratt,
“ß-Secondary and Solvent Deuterium Kinetic Isotope
Effects on ß-Lactamase Catalysis.” Biochemistry
35, 3604-3613 (1996).
48.
R. F. Pratt, M. Dryjanski, E. S. Wun, V. M. Marathias,
"8-Hydroxypenillic Acid from 6-Amino-penicillanic
Acid: A New Reaction Catalyzed by a Class C
ß-Lactamase." J. Amer. Chem. Soc. 118,
8207-8212 (1996).
49.
K. Curley, R. F. Pratt, "Effectiveness of
Tetrahedral Adducts as Transition-State Analogs and
Inhibitors of the Class C ß-Lactamase of Enterobacter
cloacae P99." J. Amer. Chem. Soc. 119,
1529-1538 (1997).
50.
K. Curley, R. F. Pratt, "Structure of
an a-Keto-ß-amido Acid, 3-(Phenylacetamido)pyruvic Acid
and its Methyl Ester in the Solid State and in Organic
and Aqueous Solvents." J. Org. Chem. 62,
4479-4483 (1997).
51.
N. Li, J. Rahil, M. E. Wright, R. F. Pratt,
"Structure-Activity Studies of the Inhibition of
Serine ß-Lactamases by Phosphonate Monoesters. Bioorg.
Med. Chem. 5, 1783-1788 (1997).
52.
R. F. Pratt, N. J. Hammar, "Salicyloyl Cyclic
Phosphate, A 'Penicillin-Like' Inhibitor of ß-Lactamases."
J. Amer. Chem. Soc. 120, 3004-3006 (1998).
53.
L. Maveyraud, R. F. Pratt, J.-P. Samama, "Crystal
Structure of an Acylation Transition-State Analog of the
TEM-1 ß-Lactamase. Mechanistic Implications for
the Class A ß-Lactamases." Biochemistry 37,
2622-2628 (1998).
54.
R. F. Pratt, N. Li, "Inhibition of Serine
ß-Lactamases by Acyl Phosph(on)ates: A New Source of
Inert Acyl [and Phosph(on)yl]-Enzymes." J. Amer.
Chem. Soc. 120, 4264-4268 (1998).
55.
K. Graves-Woodward, R. F. Pratt, "Reaction of
Soluble Penicillin-Binding Protein 2a of
Methicillin-Resistant Staphylococcus aureus with
ß-Lactams and Acyclic Substrates: Kinetics in
Homogeneous Solution." Biochem. J. 332,
755-761 (1998).
56.
S. A. Adediran, R. F. Pratt, "ß-Secondary and
Solvent Deuterium Kinetic Isotope Effects on Catalysis by
the Streptomyces R61 DD-Peptidase: Comparisons
with a Structurally Similar Class C ß-Lactamase." Biochemistry
38, 1469-1477 (1999).
57.
D. Cabaret, S. A. Adediran, M. J. Garcia-Gonzalez, R. F.
Pratt, M. Wakselman, "Synthesis and Reactivity with
ß-Lactamases of 'Penicillin-like' Cyclic
Depsipeptides." J. Org. Chem. 64,
713-720 (1999).
58.
S. A. Adediran, D. Cabaret, R. F. Pratt, M. Wakselman,
"A 'Cephalosporin-like' Cyclic Depsipeptide:
Synthesis and Reaction with ß-Lactam-Recognizing
Enzymes." Bioorg. Med. Chem. Letts. 9,
341-346 (1999).
59.
N. J. Bernstein, R. F. Pratt, "On the Importance of
a Methyl Group in ß-Lactamase Evolution: Free Energy
Profiles and Molecular Modeling." Biochemistry
38, 10499-10510 (1999).
60.
K. Graves-Woodward, R. F. Pratt, "Interactions
of Soluble Penicillin-Binding Protein 2a of
Methicillin-Resistant Staphylococcus aureus with
Moenomycin." Biochemistry 32,
10533-10542 (1999).
61.
J. H. Bell, K. Curley, R. F. Pratt, "Inhibition of
Serine Amidohydrolases by Complexes of Vanadate with
Hydroxamic Acids." Biochem. Biophys. Res. Commun.
274, 732-735 (2000).
62.
J. W. Anderson, R. F. Pratt, "Dipeptide Binding to
the Extended Active Site of the Streptomyces R61
D-Alanyl-D-Alanine-Peptidase: The Path to a Specific
Substrate." Biochemistry 39,
12200-12209 (2000).
63.
K. Curley, R. F. Pratt, "The Oxyanion Hole in Serine
ß-Lactamase Catalysis: Interactions of Thiono Substrates
with the Active Site." Bioorg. Chem. 28,
338-356 (2000).
64.
D. Cabaret, M. Garcia Gonzalez, M. Wakselman, S. A.
Adediran, R. F. Pratt, "Synthesis, Hydrolysis, and
Evaluation of 3-Acylamino-3,4-dihydro-2-oxo-2H-1,3-benzoxazinecarboxylic
Acids and Linear Azadepsipeptides as Potential
Substrates/Inhibitors of ß-Lactam-Recognizing
Enzymes." Eur. J. Org. Chem. 1,
141-149 (2001).
65.
K. Kaur, R. F. Pratt, "Mechanism of Reaction of Acyl
Phosph(on)ates with the ß-Lactamase of Enterobacter
cloacae P99." Biochemistry 40,
4610--4621 (2001).
66.
S. A. Adediran, D. Cabaret, B. Drouillat, R. F. Pratt, M.
Wakselman, "The Synthesis and Evaluation of
Benzofuranones as b-Lactamase Substrates." Bioorg.
Med. Chem. 9, 1175-1183 (2001).
67.
A. Bebrone, C. Moali, F. Mahy, S. Rival, J. D. Doquier,
G. M. Rossolini, J. Fastrez, R. F. Pratt, J.-M. Frère,
M. Galleni, "CENTA as a Chromogenic Substrate for
Studying ß-Lactamases." Antimicrob. Ag.
Chemotherap. 45, 1868-1871 (2001).
68.
S. Kumar, A. L. Pearson, R. F. Pratt, "Design,
Synthesis and Evaluation of a-Ketoheterocycles as class C
b-Lactamase Inhibitors," Bioorg. Med. Chem. 9,
2035-2044 (2001).
69.
M. J. Morrison, N. Li, R. F. Pratt, "Inverse Acyl
Phosph(on)ates: Substrates or Inhibitors of
ß-Lactam-Recognizing Enzymes?" Bioorg. Chem.
29, 271-281 (2001).
70.
K. Kaur, M. J. K. Lan, R. F. Pratt, "Mechanism of
Inhibition of the Class C ß-Lactamase of Enterobacter
cloacae P99 by Cyclic Acyl Phosph(on)ates: Rescue by
Return." J. Amer. Chem Soc. 123,
10436-10443 (2001).
71.
R.F. Pratt, "Functional Evolution of the b-Lactamase Active Site." J.
Chem. Soc. Perkin Trans. II, 851 (2002).
72.
J.H. Bell, R.F. Pratt, "Mechanism of inhibition of
the b-Lactamse of Enterobacter
cloacae P99 by 1:1 Complexes of Vanadate with
Hydroxamic Acids." Biochemistry 41,
4329-4338 (2002).
73.
J.H. Bell, R.F. Pratt, "Formation and Structure of
1:1 Complexes Between Aryl Hydroxamic Acids and Vanadate
at neutral pH." Inorg. Chem. 41,
2747-2753 (2002).
74.
M.A. McDonough, J.W. Anderson, N.R. Silvaggi, R.F. Pratt,
J.R. Knox, J.A. Kelly, "Structures of Two Kinetic
Intermediates Reveal Species Specificity of
Penicillin-binding Proteins." J. Mol Biol. 322,
111-122 (2002).
75.
N.R. Silvaggi, J.W. Anderson, S.R. Brinsmade, R.F. Pratt,
J.A. Kelly, "The Crystal Structure of
Phosphonate-Inhibited D-Ala-D-Ala peptidase Reveals an
Analogue of a Tetrahedral Transition State." Biochemistry
42, 1199-1208 (2003).
76.
K. Kaur, S.A. Adediran, M.J.K. Lan, R.F. Pratt,
"Inhibition of b-Lactamases
by Monocyclic Acyl Phosph(on)ates." Biochemistry
42, 1529-1536 (2003).
77.
D. Cabaret, S.A. Adediran, R.F. Pratt, M. Wakselman,
"New Substrates for b-Lactam-Recognizing
Enzymes: Aryl Malonamates." Biochemistry 42,
6719-6725 (2003).
78.
J.W. Anderson, S.A. Adediran, P. Charlier, M.
Nguyen-Disteche, J-M. Frere, R.A. Nicholas, R.F. Pratt,
"On the Substrate Specificity of Bacterial
DD-Peptidases: Evidence from two Series of
Peptidoglycan-mimetic Peptides." Biochem. J.
373, 949-955 (2003).
79.
M. Nukaga, S. Kumar, K. Nukaga, R.F. Pratt, J.R. Knox,
"Hydrolysis of Third-generation Cephalosporins by
Class C b-Lactamases:
Structures of a Transition State Analog of Cefotaxime in
Wild-type and Extended Spectrum Enzymes." J.
Biol. Chem. 279, 9344-9352 (2004).
80.
S. Kumar, S.A. Adediran, M. Nukaga, R.F. Pratt,
"Kinetics of Turnover of Cefotaxime by the Enterobacter
cloacae P99 and GCl b-Lactamases:
Two Free Enzyme Forms of the P99 b-Lactamase
Detected by a Combination of Pre- and Post-Steady State
Kinetics." Biochemistry 43,
2664-2672 (2004).
81.
Y.M. Ahn, R.F. Pratt, "Kinetic and Structural
Consequences of the Leaving Group in Substrates of a
Class C b-Lactamase." Biorg.
Med. Chem. 12, 1537-1542 (2004).
82.
N.R. Silvaggi, K. Kaur, S.A. Adediran, R. F. Pratt, J.A.
Kelly, "Toward Better Antibiotics: Crystallographic
Studies of a Novel Class of DD-Peptidase/b-Lactamase Inhibitors." Biochemistry
43, 7046-7053 (2004).
83.
H.R. Josephine, I. Kumar, R. F. Pratt, "The Perfect
Penicillin? Inhibition of a Bacterial DD-Peptidase by
Peptidoglycan-Mimetic b-Lactams."
J. Amer. Chem. Soc. 126,
8122-8123 (2004).
84.
R. Nagarajan, R.F. Pratt, "Thermodynamic Evaluation
of a Covalently Bonded Transition State Analogue
Inhibitor: Inhibition of b-Lactamases
by Phosphonates." Biochemistry 43,
9664-9673 (2004).