Published in CRC Crit Rev Biochem on November 01, 1976
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Directed selective pressure on a beta-lactamase to analyse molecular changes involved in development of enzyme function. Nature (1977) 2.93
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The pH-dependence of the binding of competitive inhibitors to pepsin. Biochem J (1969) 2.44
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Chemical studies on the inactivation of Escherichia coli RTEM beta-lactamase by clavulanic acid. Biochemistry (1978) 2.12
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Evolutionary optimization of the catalytic effectiveness of an enzyme. Biochemistry (1989) 1.93
Searching sequence space by definably random mutagenesis: improving the catalytic potency of an enzyme. Proc Natl Acad Sci U S A (1990) 1.92
Stabilization of a reaction intermediate as a catalytic device: definition of the functional role of the flexible loop in triosephosphate isomerase. Biochemistry (1990) 1.81
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Penicillanic acid sulfone: an unexpected isotope effect in the interaction of 6 alpha- and 6 beta-monodeuterio and of 6,6-dideuterio derivatives with RTEM beta-lactamase from Escherichia coli. Biochemistry (1981) 1.70
The antibody binding site. Labelling of a specific antibody against the photo-precursor of an aryl nitrene. Biochem J (1972) 1.68
Penicillanic acid sulfone: interaction with RTEM beta-lactamase from Escherichia coli at different pH values. Biochemistry (1981) 1.62
Secretion of beta-lactamase into the periplasm of Escherichia coli: evidence for a distinct release step associated with a conformational change. Proc Natl Acad Sci U S A (1986) 1.58
Free-energy profile of the reaction catalyzed by triosephosphate isomerase. Biochemistry (1976) 1.56
The interaction of the phosphonate analogue of 3-phospho-D-glycerate with phosphoglycerate kinase. Biochem J (1974) 1.55
Specificity and kinetics of triose phosphate isomerase from chicken muscle. Biochem J (1972) 1.51
An aspartic acid residue at the active site of pepsin. The isolation and sequence of the heptapeptide. Biochem J (1969) 1.50
The pH-dependence of pepsin-catalysed reactions. Biochem J (1969) 1.48
Inhibition of the RTEM beta-lactamase from Escherichia coli. Interaction of the enzyme with derivatives of olivanic acid. Biochemistry (1982) 1.45
Reduction of aryl azides by thiols: implications for the use of photoaffinity reagents. Biochem Biophys Res Commun (1978) 1.44
Active site of triosephosphate isomerase: in vitro mutagenesis and characterization of an altered enzyme. Proc Natl Acad Sci U S A (1985) 1.44
Phosphonate biosynthesis: isolation of the enzyme responsible for the formation of a carbon-phosphorus bond. Nature (1988) 1.42
Inhibition of the RTEM beta-lactamase from Escherichia coli. Interaction of enzyme with derivatives of olivanic acid. Biochemistry (1981) 1.40
Segmental motion in catalysis: investigation of a hydrogen bond critical for loop closure in the reaction of triosephosphate isomerase. Biochemistry (1992) 1.36
Photogenerated reagents for membrane labeling. 1. Phenylnitrene formed within the lipid bilayer. Biochemistry (1978) 1.36
Active-site labelling of triose phosphate isomerase. The reaction of bromohydroxyacetone phosphate with a unique glutamic acid residue and the migration of the label to tyrosine. Biochem J (1972) 1.35
A reliable method for random mutagenesis: the generation of mutant libraries using spiked oligodeoxyribonucleotide primers. Gene (1989) 1.35
Segmental movement: definition of the structural requirements for loop closure in catalysis by triosephosphate isomerase. Biochemistry (1992) 1.34
Inactivation of RTEM beta-lactamase from Escherichia coli by clavulanic acid and 9-deoxyclavulanic acid. Biochemistry (1981) 1.33
Efficiency and evolution of enzyme catalysis. Angew Chem Int Ed Engl (1977) 1.32
Neutral imidazole is the electrophile in the reaction catalyzed by triosephosphate isomerase: structural origins and catalytic implications. Biochemistry (1991) 1.31
Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95. Biochemistry (1991) 1.28
Crystallographic detection of a second ligand binding site in influenza virus hemagglutinin. Proc Natl Acad Sci U S A (1992) 1.27
Secondary tritium isotope effects as probes of the enzymic and nonenzymic conversion of chorismate to prephenate. Biochemistry (1983) 1.27
Direct observation of substrate distortion by triosephosphate isomerase using Fourier transform infrared spectroscopy. Biochemistry (1980) 1.25
A simple and efficient method for chemical mutagenesis of DNA. Nucleic Acids Res (1985) 1.22
Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycolohydroxamate complex at 1.8-A resolution. Biochemistry (1994) 1.21
Reaction energetics of a mutant triosephosphate isomerase in which the active-site glutamate has been changed to aspartate. Biochemistry (1986) 1.21
Mechanism of the reaction catalyzed by glutamate racemase. Biochemistry (1993) 1.20
Triosephosphate isomerase requires a positively charged active site: the role of lysine-12. Biochemistry (1994) 1.19
Uniquely labelled active site sequence in chicken muscle triose phosphate isomerase. Nature (1970) 1.19
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Isotope effects and the identification of catalytic residues in the reaction catalyzed by glutamate racemase. Biochemistry (1993) 1.17
Penicillanic acid sulfone: nature of irreversible inactivation of RTEM beta-lactamase from Escherichia coli. Biochemistry (1984) 1.16
Purification, cloning, and cofactor independence of glutamate racemase from Lactobacillus. Biochemistry (1993) 1.16
Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism. Biochemistry (1988) 1.16
Ligand recognition by influenza virus. The binding of bivalent sialosides. J Biol Chem (1991) 1.15
Illicit secretion of a cytoplasmic protein into the periplasm of Escherichia coli requires a signal peptide plus a portion of the cognate secreted protein. Demarcation of the critical region of the mature protein. J Biol Chem (1989) 1.15
The consequences of stepwise deletions from the signal-processing site of beta-lactamase. J Biol Chem (1987) 1.13
Phosphoglycerate mutases: stereochemical course of the phosphoryl group transfers catalyzed by the cofactor-dependent enzyme from rabbit muscle and the cofactor-independent enzyme from wheat germ. Biochemistry (1980) 1.13
A convenient titrant for alpha-chymotrypsin and trypsin. Biochim Biophys Acta (1968) 1.12
Purification of leucyl transfer ribonucleic acid synthetase from Escherichia coli. J Biol Chem (1970) 1.11
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The alpha-chymotryptic ydrolysis of glycine esters. Biochem J (1966) 1.09
Dehydroquinate synthase from Escherichia coli: purification, cloning, and construction of overproducers of the enzyme. Biochemistry (1984) 1.08
A conservative amino acid substitution, arginine for lysine, abolishes export of a hybrid protein in Escherichia coli. Implications for the mechanism of protein secretion. J Biol Chem (1989) 1.07
Stereochemical course of the reactions catalyzed by the bacterial phosphoenolpyruvate:glucose phosphotransferase system. Biochemistry (1982) 1.07
Monofunctional chorismate mutase from Bacillus subtilis: kinetic and 13C NMR studies on the interactions of the enzyme with its ligands. Biochemistry (1990) 1.05
Energetics of triosephosphate isomerase: deuterium isotope effects in the enzyme-catalyzed reaction. Biochemistry (1976) 1.05
The inhibition of pepsin-catalysed reactions by products and product analogues. Kinetic evidence for ordered release of products. Biochem J (1969) 1.04
Specificity and stereospecificity of alpha-chymotrypsin. Biochem J (1967) 1.04
Monofunctional chorismate mutase from Bacillus subtilis: FTIR studies and the mechanism of action of the enzyme. Biochemistry (1994) 1.03
On the mechanism of action of pepsin. Philos Trans R Soc Lond B Biol Sci (1970) 1.03
Phosphoglycerate kinase and triosephosphate isomerase from the hyperthermophilic bacterium Thermotoga maritima form a covalent bifunctional enzyme complex. EMBO J (1995) 1.02
Triosephosphate isomerase: energetics of the reaction catalyzed by the yeast enzyme expressed in Escherichia coli. Biochemistry (1988) 1.02
How can a catalytic lesion be offset? The energetics of two pseudorevertant triosephosphate isomerases. Biochemistry (1990) 1.01
Specificity in deacylation of acyl-alpha-chymotrypsins. Biochem Biophys Res Commun (1966) 1.00
Direct evidence for the exploitation of an alpha-helix in the catalytic mechanism of triosephosphate isomerase. Biochemistry (1993) 1.00
Enzyme specificity: alpha-chymotrypsin. J Theor Biol (1965) 1.00
Malate synthase: proof of a stepwise Claisen condensation using the double-isotope fractionation test. Biochemistry (1988) 0.99
Adenosine 5'-O-([gamma-18O]gamma-thio)triphosphate chiral at the gamma-phosphorus: stereochemical consequences of reactions catalyzed by pyruvate kinase, glycerol kinase, and hexokinase. Proc Natl Acad Sci U S A (1978) 0.98
Dehydroquinate synthase: the role of divalent metal cations and of nicotinamide adenine dinucleotide in catalysis. Biochemistry (1989) 0.97
Complementation of fragments of triosephosphate isomerase defined by exon boundaries. Biochemistry (1995) 0.97
The number of catalytically essential carboxyl groups in pepsin. Modification of the enzyme by trimethyloxonium fluoroborate. Eur J Biochem (1972) 0.96
Signal sequence mutants of beta-lactamase. J Biol Chem (1985) 0.95
Polarization of substrate carbonyl groups by yeast aldolase: investigation by Fourier transform infrared spectroscopy. Biochemistry (1983) 0.95
Energetics of proline racemase: tracer perturbation experiments using [14C]proline that measure the interconversion rate of the two forms of free enzyme. Biochemistry (1986) 0.95
Triosephosphate isomerase: isotope studies on the mechanistic pathway. Cold Spring Harb Symp Quant Biol (1972) 0.95
Pyruvate kinase: is the mechanism of phospho transfer associative or dissociative? Biochemistry (1982) 0.95
Enzyme relaxation in the reaction catalyzed by triosephosphate isomerase: detection and kinetic characterization of two unliganded forms of the enzyme. Biochemistry (1987) 0.94
On the intermediacy of carboxyphosphate in biotin-dependent carboxylations. Biochemistry (1988) 0.94
The rate-determining step in pepsin-catalysed reactions, and evidence against an acyl-enzyme intermediate. Biochem J (1969) 0.94
Internal thermodynamics of enzymes determined by equilibrium quench: values of Kint for enolase and creatine kinase. Biochemistry (1989) 0.94
Ribulose-1,5-bisphosphate carboxylase: primary deuterium kinetic isotope effect using [3-2H]ribulose 1,5-bisphosphate. Biochemistry (1982) 0.93
Ribulose-1,5-bisphosphate carboxylase: enzyme-catalyzed appearance of solvent tritium at carbon 3 of ribulose 1,5-bisphosphate reisolated after partial reaction. Biochemistry (1982) 0.93
The pathway of pepsin-catalysed transpeptidation. Evidence for the reactive species being the anion of the acceptor molecule. Biochem J (1971) 0.92
Stepwise improvements in catalytic effectiveness: independence and interdependence in combinations of point mutations of a sluggish triosephosphate isomerase. Biochemistry (1991) 0.92
Photogenerated reagents for membrane labeling. 2. Phenylcarbene and adamantylidene formed within the lipid bilayer. Biochemistry (1978) 0.92