Search Results - "Kirsch, J F"

Energetic analysis of an antigen/antibody interface: Alanine scanning mutagenesis and double mutant cycles on the HyHEL-10/lysozyme interaction by PONS, JAUME, RAJPAL, ARVIND, KIRSCH, JACK F.

“…Alanine scanning mutagenesis of the HyHEL-10 paratope of the HyHEL-10/HEWL complex demonstrates that the energetically important side chains (hot spots) of…”
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PYRIDOXAL PHOSPHATE ENZYMES: Mechanistic, Structural, and Evolutionary Considerations by Eliot, Andrew C, Kirsch, Jack F

“…Pyridoxal phosphate (PLP)-dependent enzymes are unrivaled in the diversity of reactions that they catalyze. New structural data have paved the way for targeted…”
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Site-Directed Mutagenesis of the Catalytic Residues Asp-52 and Glu-35 of Chicken Egg White Lysozyme by Malcolm, Bruce A., Rosenberg, Steven, Corey, Michael J., Allen, Judith S., De Baetselier, Annie, Kirsch, Jack F.

“…The roles of the catalytic active-site residues aspartic acid-52 and glutamic acid-35 of chicken lysozyme (EC 3.2.1.17) have been investigated by separate in…”
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A Novel Engineered Subtilisin BPN‘ Lacking a Low-Barrier Hydrogen Bond in the Catalytic Triad by Stratton, Jennifer R, Pelton, Jeffrey G, Kirsch, Jack F

“…The low-barrier hydrogen bond (LBHB) between the Asp and His residues of the catalytic triad in a serine protease was perturbed via the D32C mutation in…”
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Glutamate 47 in 1-Aminocyclopropane-1-carboxylate Synthase Is a Major Specificity Determinant by McCarthy, Darla L, Capitani, Guido, Feng, Liang, Gruetter, Markus G, Kirsch, Jack F

“…Glutamate 47 is conserved in 1-aminocyclopropane-1-carboxylate (ACC) synthases and is positioned near the sulfonium pole of (S,S)-S-adenosyl-l-methionine (SAM)…”
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Redesign of the substrate specificity of escherichia coli aspartate aminotransferase to that of escherichia coli tyrosine aminotransferase by homology modeling and site‐directed mutagenesis by Onuffer, James J., Kirsch, Jack F.

“…Although several high‐resolution X‐ray crystallographic structures have been determined for Escherichia coli aspartate aminotransferase (eAATase), efforts to…”
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Design and structural analysis of an engineered thermostable chicken lysozyme by Shih, Phoebe, Kirsch, Jack F.

“…A hyperstable (hs) variant of chicken egg‐white lysozyme with enhanced thermal (ΔTm ≈︁ +10.5 °C) and chemical (ΔCm for guanidine hydrochloride denaturation =…”
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Direct Brønsted Analysis of the Restoration of Activity to a Mutant Enzyme by Exogenous Amines by Toney, Michael D., Kirsch, Jack F.

“…A true Brønsted analysis of proton transfer in an enzyme mechanism is made possible by the chemical rescue of an inactive mutant of aspartate aminotransferase,…”
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Thermal stability determinants of chicken egg‐white lysozyme core mutants: Hydrophobicity, packing volume, and conserved buried water molecules by Shih, Phoebe, Kirsch, Jack F., Holland, Debra R.

“…A series of 24 mutants was made in the buried core of chicken lysozyme at positions 40, 55, and 91. The midpoint temperature of thermal denaturation transition…”
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Lysine 258 in aspartate aminotransferase: Enforcer of the Circe effect for amino acid substrates and the general-base catalyst for the 1,3-prototropic shift by Toney, Michael D, Kirsch, Jack F

“…The replacement of Lys258 by alanine (K258A) in aspartate aminotransferase reduces the rate constant for the central, 1,3-prototropic shift by…”
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Aminotransferase Activity and Bioinformatic Analysis of 1-Aminocyclopropane-1-carboxylate Synthase by Feng, Liang, Geck, Mary K, Eliot, Andrew C, Kirsch, Jack F

“…The mechanistic fate of pyridoxal phosphate (PLP)-dependent enzymes diverges after the quinonoid intermediate. 1-Aminocyclopropane-1-carboxylate (ACC)…”
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Quantitative evaluation of the chicken lysozyme epitope in the HyHEL‐10 fab complex: Free energies and kinetics by Rajpal, Arvind, Taylor, Marc G., Kirsch, Jack F.

“…The hen (chicken) egg‐white lysozyme (HEWL) epitope for the monoclonal antibody HyHEL‐I0 Fab (Fab‐I0) was investigated by alanine scan mutagenesis. The…”
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Expression of apple 1-aminocyclopropane-1-carboxylate synthase in Escherichia coli: kinetic characterization of wild-type and active-site mutant forms by White, M.F. (University of California, Berkeley, CA.), Vasquez, J, Yang, S.F, Kirsch, J.F

“…The pyridoxal phosphate-dependent enzyme 1-aminocyclopropane-1-carboxylate synthase (ACC synthase; S-adenosyl-L-methionine methylthioadenosine-lyase, EC…”
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High-Resolution Mapping of the HyHEL-10 Epitope of Chicken Lysozyme by Site-Directed Mutagenesis by Lauren N. W. Kam-Morgan, Smith-Gill, Sandra J., Taylor, Marc G., Zhang, Lei, Wilson, Allan C., Kirsch, Jack F.

“…The complex formed between hen egg white lysozyme (HEL) and the monoclonal antibody HyHEL-10 Fab fragment has an interface composed of van der Waals…”
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Reengineering the catalytic lysine of aspartate aminotransferase by chemical elaboration of a genetically introduced cysteine by Planas, Antoni, Kirsch, Jack F

“…The active-site essential catalytic residue of aspartate aminotransferase, Lys 258, has been converted to Cys (K258C) by site-directed mutagenesis. This mutant…”
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Brønsted analysis of aspartate aminotransferase via exogenous catalysis of reactions of an inactive mutant by Toney, M D, Kirsch, J F

“…Primary amines functionally replace lysine 258 by catalyzing both the 1,3-prototropic shift and external aldimine hydrolysis reactions with the inactive…”
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The K258R mutant of aspartate aminotransferase stabilizes the quinonoid intermediate by TONEY, M. D, KIRSCH, J. F

“…Lys-258 of aspartate aminotransferase forms a Schiff base with pyridoxal phosphate and is responsible for catalysis of the 1,3-prototropic shift central to the…”
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Tyrosine 70 increases the coenzyme affinity of aspartate aminotransferase. A site-directed mutagenesis study by Toney, M D, Kirsch, J F

“…The crucial step in enzymatic transamination is the tautomerization of aldimine/ketimine intermediates, formed between the pyridoxyl coenzyme and the…”
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Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure by Kirsch, J F, Eichele, G, Ford, G C, Vincent, M G, Jansonius, J N, Gehring, H, Christen, P

“…Aspartate aminotransferase is a pyridoxal phosphate-dependent enzyme that catalyses the transamination reaction: L-aspartate + 2-oxoglutarate---oxaloacetate +…”
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Role of arginine-292 in the substrate specificity of aspartate aminotransferase as examined by site-directed mutagenesis by Cronin, Ciaran N., Kirsch, Jack F.

“…X-ray crystallographic data have implicated Arg-292 as the residue responsible for the preferred side-chain substrate specificity of aspartate…”
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