Published in Protein Sci on September 01, 1995
Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis. Protein Sci (1995) 1.24
Improving the Production of L-Phenylalanine by Identifying Key Enzymes Through Multi-Enzyme Reaction System in Vitro. Sci Rep (2016) 0.75
Specific synthesis of DNA in vitro via a polymerase-catalyzed chain reaction. Methods Enzymol (1987) 58.68
Measurement of protein by spectrophotometry at 205 nm. Anal Biochem (1974) 6.04
Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure. J Mol Biol (1984) 2.15
Evolutionary relationships among aminotransferases. Tyrosine aminotransferase, histidinol-phosphate aminotransferase, and aspartate aminotransferase are homologous proteins. Eur J Biochem (1989) 1.84
Pre-steady-state kinetics of Escherichia coli aspartate aminotransferase catalyzed reactions and thermodynamic aspects of its substrate specificity. Biochemistry (1990) 1.76
Nonidentity of the aspartate and the aromatic aminotransferase components of transaminase A in Escherichia coli. J Bacteriol (1972) 1.47
Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase. Nat Struct Biol (1995) 1.44
The purification and properties of the aspartate aminotransferase and aromatic-amino-acid aminotransferase from Escherichia coli. Eur J Biochem (1978) 1.41
Escherichia coli aromatic amino acid aminotransferase: characterization and comparison with aspartate aminotransferase. Biochemistry (1993) 1.33
Crystal structures of Escherichia coli aspartate aminotransferase in two conformations. Comparison of an unliganded open and two liganded closed forms. J Mol Biol (1994) 1.32
Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis. Protein Sci (1995) 1.24
X-ray crystallographic study of pyridoxal 5'-phosphate-type aspartate aminotransferases from Escherichia coli in open and closed form. J Biochem (1994) 1.21
Reversible dissociation and unfolding of aspartate aminotransferase from Escherichia coli: characterization of a monomeric intermediate. Biochemistry (1990) 1.18
Role of arginine-292 in the substrate specificity of aspartate aminotransferase as examined by site-directed mutagenesis. Biochemistry (1988) 1.17
Characterization of the apparent negative co-operativity induced in Escherichia coli aspartate aminotransferase by the replacement of Asp222 with alanine. Evidence for an extremely slow conformational change. Protein Eng (1994) 1.10
Three-dimensional structures of aspartate aminotransferase from Escherichia coli and its mutant enzyme at 2.5 A resolution. J Biochem (1990) 1.08
Brønsted analysis of aspartate aminotransferase via exogenous catalysis of reactions of an inactive mutant. Protein Sci (1992) 1.03
Mapping of the aspartate and aromatic amino acid aminotransferase genes tyrB and aspC. J Bacteriol (1977) 1.01
Crystal structures of true enzymatic reaction intermediates: aspartate and glutamate ketimines in aspartate aminotransferase. Biochemistry (1993) 1.00
Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase. Biochemistry (1991) 0.99
Aromatic amino acid aminotransferase of Escherichia coli: nucleotide sequence of the tyrB gene. Biochem Biophys Res Commun (1985) 0.98
Effects of replacement of tryptophan-140 by phenylalanine or glycine on the function of Escherichia coli aspartate aminotransferase. Biochem Biophys Res Commun (1990) 0.92
Kinetic isotope effect studies on aspartate aminotransferase: evidence for a concerted 1,3 prototropic shift mechanism for the cytoplasmic isozyme and L-aspartate and dichotomy in mechanism. Biochemistry (1989) 0.90
[Arg292----Val] or [Arg292----Leu] mutation enhances the reactivity of Escherichia coli aspartate aminotransferase with aromatic amino acids. Biochem Biophys Res Commun (1989) 0.89
Modeling the three-dimensional structures of bacterial aminotransferases. Biochemistry (1988) 0.89
Computational approach towards the three-dimensional structure of E. coli tyrosine aminotransferase. FEBS Lett (1992) 0.81
Transamination of aromatic amino acids in Escherichia coli. Methods Enzymol (1987) 0.80
Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure. J Mol Biol (1984) 2.15
Ancestral lysozymes reconstructed, neutrality tested, and thermostability linked to hydrocarbon packing. Nature (1990) 2.14
Direct Brønsted analysis of the restoration of activity to a mutant enzyme by exogenous amines. Science (1989) 1.70
Site-directed mutagenesis of the catalytic residues Asp-52 and Glu-35 of chicken egg white lysozyme. Proc Natl Acad Sci U S A (1989) 1.54
Fractional diffusion-limited component of reactions catalyzed by acetylcholinesterase. Biochemistry (1986) 1.54
Investigation of diffusion-limited rates of chymotrypsin reactions by viscosity variation. Biochemistry (1982) 1.53
Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase. Nat Struct Biol (1995) 1.44
Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene. J Mol Biol (1999) 1.27
The mechanism of the activation of papain. Biochem Biophys Res Commun (1969) 1.27
Diffusion-limited component of reactions catalyzed by Bacillus cereus beta-lactamase I. Biochemistry (1984) 1.25
Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis. Protein Sci (1995) 1.24
Energetic analysis of an antigen/antibody interface: alanine scanning mutagenesis and double mutant cycles on the HyHEL-10/lysozyme interaction. Protein Sci (1999) 1.19
Role of arginine-292 in the substrate specificity of aspartate aminotransferase as examined by site-directed mutagenesis. Biochemistry (1988) 1.17
Decreasing the basicity of the active site base, Lys-258, of Escherichia coli aspartate aminotransferase by replacement with gamma-thialysine. Biochemistry (1995) 1.17
The tyrosine-225 to phenylalanine mutation of Escherichia coli aspartate aminotransferase results in an alkaline transition in the spectrophotometric and kinetic pKa values and reduced values of both kcat and Km. Biochemistry (1991) 1.16
Expression of apple 1-aminocyclopropane-1-carboxylate synthase in Escherichia coli: kinetic characterization of wild-type and active-site mutant forms. Proc Natl Acad Sci U S A (1994) 1.11
Characterization of the apparent negative co-operativity induced in Escherichia coli aspartate aminotransferase by the replacement of Asp222 with alanine. Evidence for an extremely slow conformational change. Protein Eng (1994) 1.10
A rapid method for determination of endoproteinase substrate specificity: specificity of the 3C proteinase from hepatitis A virus. Proc Natl Acad Sci U S A (1991) 1.07
Reengineering the catalytic lysine of aspartate aminotransferase by chemical elaboration of a genetically introduced cysteine. Biochemistry (1991) 1.06
Tyrosine 70 fine-tunes the catalytic efficiency of aspartate aminotransferase. Biochemistry (1991) 1.05
Oxygen-18 leaving group kinetic isotope effects on the hydrolysis of nitrophenyl glycosides. 2. Lysozyme and beta-glucosidase: acid and alkaline hydrolysis. Biochemistry (1981) 1.04
High-resolution mapping of the HyHEL-10 epitope of chicken lysozyme by site-directed mutagenesis. Proc Natl Acad Sci U S A (1993) 1.04
Brønsted analysis of aspartate aminotransferase via exogenous catalysis of reactions of an inactive mutant. Protein Sci (1992) 1.03
Kinetic epitope mapping of the chicken lysozyme.HyHEL-10 Fab complex: delineation of docking trajectories. Protein Sci (1998) 1.03
The kinetics of the papain-catalyzed hydrolysis of esters of carbobenzoxyglycine. Evidence for an acyl-enzyme intermediate. Biochemistry (1966) 1.01
Design and structural analysis of an engineered thermostable chicken lysozyme. Protein Sci (1995) 1.00
Thermal stability determinants of chicken egg-white lysozyme core mutants: hydrophobicity, packing volume, and conserved buried water molecules. Protein Sci (1995) 1.00
Oxygen-18 leaving group kinetic isotope effects on the hydrolysis of nitrophenyl glycosides. 1. beta-galactosidease-catalyzed hydrolysis. Biochemistry (1981) 0.99
Lysine 258 in aspartate aminotransferase: enforcer of the Circe effect for amino acid substrates and general-base catalyst for the 1,3-prototropic shift. Biochemistry (1993) 0.98
pH dependence and solvent deuterium oxide kinetic isotope effects on Bacillus cereus beta-lactamase I catalyzed reactions. Biochemistry (1984) 0.95
A general method for the quantitative analysis of functional chimeras: applications from site-directed mutagenesis and macromolecular association. Protein Sci (2001) 0.95
A continuous coupled spectrophotometric assay for tyrosine aminotransferase activity with aromatic and other nonpolar amino acids. Anal Biochem (1997) 0.93
Kinetic and spectroscopic investigations of wild-type and mutant forms of apple 1-aminocyclopropane-1-carboxylate synthase. Biochemistry (1997) 0.92
Ligand-dependent conformational plasticity of the periplasmic histidine-binding protein HisJ. Involvement in transport specificity. J Biol Chem (1996) 0.91
Is aspartate 52 essential for catalysis by chicken egg white lysozyme? The role of natural substrate-assisted hydrolysis. Biochemistry (1996) 0.91
The human cDNA for a homologue of the plant enzyme 1-aminocyclopropane-1-carboxylate synthase encodes a protein lacking that activity. Gene (2001) 0.90
Kinetic isotope effect studies on aspartate aminotransferase: evidence for a concerted 1,3 prototropic shift mechanism for the cytoplasmic isozyme and L-aspartate and dichotomy in mechanism. Biochemistry (1989) 0.90
Sequential protection-modification method for selective sulfhydryl group derivatization in proteins having more than one cysteine. Protein Eng (1990) 0.90
A rapid, sensitive fluorometric assay for avidin and biotin. Methods Enzymol (1979) 0.89
Use of site-directed mutagenesis and alternative substrates to assign the prototropic groups important to catalysis by Escherichia coli aspartate aminotransferase. Biochemistry (1995) 0.89
Quantitative evaluation of the chicken lysozyme epitope in the HyHEL-10 Fab complex: free energies and kinetics. Protein Sci (1998) 0.88
Cysteine-191 in aspartate aminotransferases appears to be conserved due to the lack of a neutral mutation pathway to the functional equivalent, alanine-191. Proteins (1996) 0.88
A novel, definitive test for substrate channeling illustrated with the aspartate aminotransferase/malate dehydrogenase system. Biochemistry (1999) 0.88
Kinetics and equilibria for the reactions of coenzymes with wild type and the Y70F mutant of Escherichia coli aspartate aminotransferase. Biochemistry (1991) 0.87
The reaction catalyzed by Escherichia coli aspartate aminotransferase has multiple partially rate-determining steps, while that catalyzed by the Y225F mutant is dominated by ketimine hydrolysis. Biochemistry (1996) 0.86
Structure of the complex between pyridoxal 5'-phosphate and the tyrosine 225 to phenylalanine mutant of Escherichia coli aspartate aminotransferase determined by isotope-edited classical Raman difference spectroscopy. Biochemistry (1993) 0.85
The activation of papain and the inhibition of the active enzyme by carbonyl reagents. J Biol Chem (1969) 0.84
Glutamate 47 in 1-aminocyclopropane-1-carboxylate synthase is a major specificity determinant. Biochemistry (2001) 0.84
Site-directed mutagenesis of aspartate aminotransferase from E. coli. Biochem Biophys Res Commun (1985) 0.84
The K258R mutant of aspartate aminotransferase stabilizes the quinonoid intermediate. J Biol Chem (1991) 0.83
Demonstration of a change in the rate-determining step in papain- and ficin-catalyzed acyl-transfer reactions. Biochemistry (1971) 0.83
Enzymatic displacement of oxygen and sulfur from purines. J Am Chem Soc (1968) 0.83
Isolation of a Staphylococcus aureus beta-lactamase-dicloxacillin complex and kinetic studies on the reactivation of the enzyme. Arch Biochem Biophys (1989) 0.83
Reconstruction and testing of ancestral proteins. Methods Enzymol (1993) 0.83
Tyrosine 70 increases the coenzyme affinity of aspartate aminotransferase. A site-directed mutagenesis study. J Biol Chem (1987) 0.82
A novel engineered subtilisin BPN' lacking a low-barrier hydrogen bond in the catalytic triad. Biochemistry (2001) 0.82
Mechanism of enzyme action. Annu Rev Biochem (1973) 0.82
Contribution to catalysis and stability of the five cysteines in Escherichia coli aspartate aminotransferase. Preparation and properties of a cysteine-free enzyme. Biochemistry (1992) 0.81
Papain-catalyzed reactions of esters with alcohols. The nature of the rate-determining step. Biochemistry (1967) 0.81
A sensitive fluorometric assay for avidin and biotin. Anal Biochem (1977) 0.80
L-Vinylglycine is an alternative substrate as well as a mechanism-based inhibitor of 1-aminocyclopropane-1-carboxylate synthase. Biochemistry (2000) 0.80
Effects of substituents on the rates of deacylation of substituted benzoyl papains. Role of a carboxylate residue in the catalytic mechanism. Biochemistry (1978) 0.80
Examining the structural and chemical flexibility of the active site base, Lys-258, of Escherichia coli aspartate aminotransferase by replacement with unnatural amino acids. Biochemistry (1995) 0.80
The presteady-state kinetics of the papain-catalyzed hydrolysis of isomeric nitrophenyl esters of carbobenzoxyglycine. Biochemistry (1968) 0.79
Site-directed mutagenesis in analysis of protein-protein interactions. Methods Enzymol (1993) 0.79
The stereospecific labilization of the C-4' pro-S hydrogen of pyridoxamine 5'-phosphate is abolished in (Lys258----Ala) aspartate aminotransferase. J Biol Chem (1987) 0.79
Letter: Kinetic isotope effects for the chymotrypsin catalyzed hydrolysis of ethoxyl-18 O labeled specific ester substrates. J Am Chem Soc (1975) 0.79
Kinetics and mechanism of inhibition of Escherichia coli alkaline phosphatase by permanganate ion. Biochemistry (1980) 0.78
Aminotransferase activity and bioinformatic analysis of 1-aminocyclopropane-1-carboxylate synthase. Biochemistry (2000) 0.78
Pyridoxamine-pyruvate transaminase. 1. Determination of the active site stoichiometry and the pH dependence of the dissociation constant for 5'-deoxypyridoxal. Biochemistry (1977) 0.78
Kinetics and thermodynamics of the reactions of acyl-papains. Effects of pH, temperature, solvents, ionic strength, and added nucleophiles. Biochemistry (1971) 0.78
Role of the minor energetic determinants of chicken egg white lysozyme (HEWL) to the stability of the HEWL.antibody scFv-10 complex. Proteins (2000) 0.78
Accumulation of the quinonoid intermediate in the reaction catalyzed by aspartate aminotransferase with cysteine sulfinic acid. Arch Biochem Biophys (1995) 0.77
Pyridoxamine-pyruvate transaminase. 2. Temperature-jump and stopped-flow kinetic investigation of the rates and mechanism of the reaction of 5'-deoxypyridoxal with the enzyme. Biochemistry (1977) 0.77
Three-dimensional structure of mitochondrial aspartate aminotransferase and some functional derivatives: implications for its mode of action. Biochem Soc Trans (1984) 0.77
Crystallographic studies on the mechanism of action of mitochondrial aspartate aminotransferase. Prog Clin Biol Res (1984) 0.77
Crystallization and preliminary X-ray analysis of recombinant 1-aminocyclopropane-1-carboxylate synthase from apple. A key enzyme in the biosynthesis of the plant hormone ethylene. J Mol Biol (1994) 0.77
Synergistic contributions of asparagine 46 and aspartate 52 to the catalytic mechanism of chicken egg white lysozyme. Biochemistry (1996) 0.77
A novel yeast expression/secretion system for the recombinant plant thiol endoprotease propapain. Protein Eng (1996) 0.76
Noncoded amino acid replacement probes of the aspartate aminotransferase mechanism. Biochemistry (1997) 0.76
[Experiences with the hip arthrodesis using the AO-technic]. Arch Orthop Unfallchir (1971) 0.75
Estimation of free energy barriers in the cytoplasmic and mitochondrial aspartate aminotransferase reactions probed by hydrogen-exchange kinetics of C alpha-labeled amino acids with solvent. Biochemistry (1989) 0.75
Aspartate aminotransferase catalyzed oxygen exchange with solvent from oxygen-18-enriched alpha-ketoglutarate: evidence for slow exchange of enzyme-bound water. Biochemistry (1989) 0.75
Acylation of chymotrypsin by active esters of nonspecific substrates. Evidence for a transient acylimidazole intermediate. Biochemistry (1972) 0.75
Anomalous pH dependence of the reactions of carbenicillin and sulbenicillin with Bacillus cereus beta-lactamase I. Influence of the alpha-substituent charge on the kinetic parameters. Biochemistry (1984) 0.75
Multiple system atrophy presenting with language impairment. Neurology (2006) 0.75
Preliminary X-ray data for aspartate aminotransferase from Escherichia coli. J Mol Biol (1986) 0.75