P. Frey

P. Frey, J. Campbell, R. Angelotti, 1964, Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine.

Galactose-1-phosphate uridylyltransferase: detection, isolation, and characterization of the uridylyl enzyme.

P. Frey, K. Sheu, S. L. Yang, 1982, Methods in enzymology.

Galactose-1-phosphate uridylyltransferase: isolation and properties of a uridylyl-enzyme intermediate.

P. Frey, S. L. Lee, K. Sheu, 1977, Biochemistry.

The structure of tetramethyl μ‐monothiopyrophosphate

P. Frey, M. Benning, C. J. Halkides, 1991 .

Synthesis of undecagold labeling compounds and their applications in electron microscopic analysis of multiprotein complexes.

P. Frey, T. Frey, 1999, Journal of structural biology.

Crystallization and X-ray diffraction analysis of ornithine cyclodeaminase from Pseudomonas putida.

P. Frey, J. Wedekind, F. Ruzicka, 2004, Acta crystallographica. Section D, Biological crystallography.

A novel lysine 2,3-aminomutase encoded by the yodO gene of bacillus subtilis: characterization and the observation of organic radical intermediates.

P. Frey, F. Ruzicka, D. Chen, 2000, The Biochemical journal.

Enzymology. Coenzymes and radicals.

P. Frey, 2001, Science.

2-Acetylthiamin pyrophosphate: an enzyme-bound intermediate in thiamin pyrophosphate-dependent reactions.

P. Frey, 1989, BioFactors.

Spectroscopic Evidence for the Participation of an Allylic Analogue of the 5‘-Deoxyadenosyl Radical in the Reaction of Lysine 2,3-Aminomutase

G. H. Reed, P. Frey, O. Magnusson, 1999 .

Standard free energy change for the hydrolysis of the alpha, beta-phosphoanhydride bridge in ATP.

P. Frey, A. Arabshahi, Perry A. Frey, 1995, Biochemistry.

Chiral phosphorothioates: stereochemical analysis of enzymatic substitution at phosphorus.

P. Frey, 1989, Advances in enzymology and related areas of molecular biology.

p-(Bromoacetamido)phenyl uridyl pyrophosphate: an active-site-directed irreversible inhibitor for uridine diphosphate galactose 4-epimerase.

P. Frey, Y. Wong, F. Winer, 1979, Biochemistry.

Cloning, expression, purification, cofactor requirements, and steady state kinetics of phosphoketolase-2 from Lactobacillus plantarum.

P. Frey, A. Yévenes, 2008, Bioorganic chemistry.

An organic radical in the lysine 2,3-aminomutase reaction.

G. H. Reed, P. Frey, M. Ballinger, 1992, Biochemistry.

Synthesis of UDP-4-deoxy-4-fluoroglucose and UDP-4-deoxy-4-fluorogalactose and their Interactions with Enzymes of Nucleotide Sugar Metabolism

P. Frey, M. Chapeau, 1994 .

Radical intermediates in the reaction of lysine 2,3-aminomutase

P. Frey, S. Booker, 1999 .

Combined Fmoc-Alloc strategy for a general SPPS of phosphoserine peptides; preparation of phosphorylation-dependent tau antisera.

P. Frey, C. Dalvit, C. Waridel, 1997, Bioorganic & medicinal chemistry.

Facile hydrogen-deuterium exchange at the 5'-position of an analogue of S-adenosyl-l-methionine.

P. Frey, O. Magnusson, 2002, Bioorganic chemistry.

Galactose-1-phosphate uridylyltransferase. Purification of the enzyme and stereochemical course of each step of the double-displacement mechanism.

P. Frey, A. Smallwood, A. Arabshahi, 1986, Biochemistry.

Cloning, Sequencing, Heterologous Expression, Purification, and Characterization of Adenosylcobalamin-dependentd-Lysine 5,6-Aminomutase from Clostridium sticklandii *

Christopher H. Chang, P. Frey, 2000, The Journal of Biological Chemistry.

The strongly conserved lysine 256 of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase is essential for phosphoryl transfer.

P. Frey, S. Bazaes, A. M. Jabalquinto, 1998, Biochemistry.

Crystal structures of the oxidized and reduced forms of UDP-galactose 4-epimerase isolated from Escherichia coli.

P. Frey, J. Thoden, H. Holden, 1996, Biochemistry.

Rate Enhancements Brought About by Uridine Nucleotides in the Reduction of NAD+ at the Active Site of UDP-Galactose 4-Epimerase☆☆☆

P. Frey, A. Arabshahi, Yijeng Liu, 2000 .

1H, 13C, and 31P nuclear magnetic resonance spectral assignments for tobramycin, 2''-(adenosine-5'-phosphoryl)-tobramycin and 2''-(adenosine-5'-thiophosphoryl)-tobramycin.

P. Frey, E. Mooberry, J. V. Van Pelt, 1990, Archives of biochemistry and biophysics.

Cobalamin Coenzymes in Enzymology

P. Frey, 2010 .

Free radical mechanisms in enzymology.

G. H. Reed, P. Frey, A. Hegeman, 2006, Chemical reviews.

Cofactor dependence of reduction potentials for [4Fe-4S]2+/1+ in lysine 2,3-aminomutase.

P. Frey, Glen T Hinckley, 2006, Biochemistry.

The role of the B12 coenzyme in the conversion of 1,2-propanediol to propionaldehyde.

P. Frey, R. Abeles, 1966, The Journal of biological chemistry.

Structural analysis of the H166G site-directed mutant of galactose-1-phosphate uridylyltransferase complexed with either UDP-glucose or UDP-galactose: detailed description of the nucleotide sugar binding site.

P. Frey, I. Rayment, J. Thoden, 1997, Biochemistry.

UDP-glucose pyrophosphorylase. Stereochemical course of the reaction of glucose 1-phosphate with uridine-5'[1-thiotriphosphate].

P. Frey, K. Sheu, 1978, The Journal of biological chemistry.

Galactose-1-phosphate uridylyltransferase: rate studies confirming a uridylyl-enzyme intermediate on the catalytic pathway.

P. Frey, L. Wong, 1974, Biochemistry.

Chemical model for the pyridoxal 5'-phosphate dependent lysine aminomutases

P. Frey, O. Han, 1990 .

Direct FeS cluster involvement in generation of a radical in lysine 2,3-aminomutase.

P A Frey, P. Frey, N. Cosper, 2000, Biochemistry.

Lysine 2,3-aminomutase and the mechanism of the interconversion of lysine and beta-lysine.

G. H. Reed, P. Frey, 2006, Advances in enzymology and related areas of molecular biology.

Importance of organic radicals in enzymic cleavage of unactivated carbon-hydrogen bonds

P. Frey, 1990 .

Studies on the mechanism of hydrogen transfer in the cobamide coenzyme-dependent dioldehydrase reaction.

P. Frey, R. Abeles, M. Essenberg, 1967, The Journal of biological chemistry.

The stereochemistry of the conversion of propanediol to propionaldehyde

P. Frey, R. Abeles, G. L. Karabatsos, 1965 .

MECHANISM OF COUPLED ELECTRON AND GROUP TRANSFER IN Escherichia coli PYRUVATE DEHYDROGENASE *

P. Frey, 1982, Annals of the New York Academy of Sciences.

Electron Spin Echo Envelope Modulation Spectroscopy Reveals How Adenosylcobalamin-Dependent Lysine 5,6-Aminomutase Positions the Radical Pair Intermediates and Modulates Their Stabilities for Efficient Catalysis

P. Frey, S. Ke, Jun-Ru Chen, 2021, ACS Catalysis.

A new concept for the mechanism of action of chymotrypsin: the role of the low-barrier hydrogen bond.

P. Frey, C. Cassidy, J. Lin, 1997, Biochemistry.

Analysis of the Cob(II)alamin-5'-deoxy-3',4'-anhydroadenosyl radical triplet spin system in the active site of diol dehydrase.

G. H. Reed, P. Frey, O. Magnusson, 2006, Biochemistry.

Importance of Organic Radicals in Enzymatic Cleavage of Unactivated C‐ H Bonds

P. Frey, 1991 .

Methane monooxygenase catalyzed oxygenation of 1,1-dimethylcyclopropane. Evidence for radical and carbocationic intermediates.

P A Frey, P. Frey, M. Donnelly, 1990, Biochemistry.

Mapping the lipoyl groups of the pyruvate dehydrogenase complex by use of gold cluster labels and scanning transmission electron microscopy.

P. Frey, J. Hainfeld, J. Wall, 1994, Biochemistry.

2-ketoacid dehydrogenase complexes of Escherichia coli: stereospecificities of the three components for (R)-lipoate.

P. Frey, Y. S. Yang, 1989, Archives of biochemistry and biophysics.

Escherichia coli pyruvate dehydrogenase complex: particle masses of the complex and component enzymes measured by scanning transmission electron microscopy.

P. Frey, J. Hainfeld, J. Wall, 1985, Biochemistry.

Bond order and charge localization in nucleoside phosphorothioates.

P. Frey, R. Sammons, 1985, Science.

Coenzymes and Radicals

P. Frey, 2001, Science.

High‐resolution X‐ray structure of UDP‐galactose 4‐epimerase complexed with UDP‐phenol

P. Frey, J. Thoden, H. Holden, 1996, Protein science : a publication of the Protein Society.

Review: Strong hydrogen bonding in molecules and enzymatic complexes

P. Frey, 2001 .

Studies on the mechanism of hydrogen transfer in the coenzyme B12 dependent dioldehydrase reaction II.

P. Frey, R. Abeles, M. Essenberg, 1971 .

Correlation of low-barrier hydrogen bonding and oxyanion binding in transition state analogue complexes of chymotrypsin.

P A Frey, P. Frey, W. Cleland, 2001, Biochemistry.

Low-Barrier Hydrogen Bonding in Aqueous and Aprotic Solutions of Dicarboxylic Acids: Spectroscopic Characterization

P. Frey, C. Cassidy, Jing Lin, 1998 .

The Low Barrier Hydrogen Bond in Enzymatic Catalysis*

P A Frey, P. Frey, J. Gerlt, 1998, The Journal of Biological Chemistry.

Characterization of a low barrier hydrogen bond in the active site of chymotrypsin

P. Frey, 2002 .

Identification of cis-ethanesemidione as the organic radical derived from glycolaldehyde in the suicide inactivation of dioldehydrase and of ethanolamine ammonia-lyase.

G. H. Reed, P. Frey, V. Bandarian, 2000, Biochemistry.

Fluoropyruvate: an unusal substrate for Escherichia coli pyruvate dehydrogenase.

P. Frey, L. Leung, 1978, Biochemical and biophysical research communications.

Acetylation stoichiometry of Escherichia coli pyruvate dehydrogenase complex.

P. Frey, S. Wong, D. Speckhard, 1977, Biochemical and biophysical research communications.

Ornithine cyclodeaminase: structure, mechanism of action, and implications for the mu-crystallin family.

P. Frey, J. Wedekind, J. L. Goodman, 2004, Biochemistry.

Re‐face stereospecificity at C4 of NAD(P) for alcohol dehydrogenase from Methanogenium organophilum and for (R)‐2‐hydroxyglutarate dehydrogenase from Acidaminococcus fermentans as determined by 1H‐NMR spectroscopy

P. Frey, R. Thauer, W. Buckel, 1996, FEBS Letters.

Nucleophile in the active site of Escherichia coli galactose-1-phosphate uridylyltransferase: degradation of the uridylyl-enzyme intermediate to N3-phosphohistidine.

P. Frey, S. L. Yang, 1979, Biochemistry.

Fundamentals of enzymology (Third Edition)

P. Frey, N. C. Price, 2001 .

Esherichia coli pyruvate dehydrogenase complex: improved purification and the flavin content.

P. Frey, D. Speckhard, 1975, Biochemical and biophysical research communications.

The Radical SAM Superfamily

Perry A. Frey, Adrian D. Hegeman, P. Frey, 2008 .

The participation of the two non-equivalent C-5' hydrogens of B 12-coenzyme in the catalytic process.

P. Frey, S. Kerwar, R. Abeles, 1967, Biochemical and biophysical research communications.

Strong Hydrogen Bonds in Aqueous and Aqueous−Acetone Solutions of Dicarboxylic Acids: Activation Energies for Exchange and Deuterium Fractionation Factors

P. Frey, Jing Lin and, 2000 .

Transient Intermediates in Enzymology, 1964–2008

P. Frey, 2015, The Journal of Biological Chemistry.

Isotope Effects in the Characterization of Low Barrier Hydrogen Bonds

P. Frey, 2005 .

Unambiguous determination of the stereochemistry of nucleotidyl transfer catalyzed by DNA polymerase I from Escherichia coli.

P. Frey, R. Brody, 1981, Biochemistry.

UDPgalactose 4-epimerase catalyzed oxygen dependent reduction of a free radical substrate analogue by two electron reducing agents.

P. Frey, S. Wong, 1976, Journal of the American Chemical Society.

The substrate reactivity of mu-monothiopyrophosphate with pyrophosphate-dependent phosphofructokinase: evidence for a dissociative transition state in enzymatic phosphoryl group transfer.

P. Frey, E. Lightcap, C. J. Halkides, 1991, Biochemistry.

S-Adenosylmethionine: a wolf in sheep's clothing, or a rich man's adenosylcobalamin?

P. Frey, O. Magnusson, Olafur Th Magnusson, 2003, Chemical reviews.

Radical mechanisms of enzymatic catalysis.

P A Frey, P. Frey, Perry A. Frey, 2001, Annual review of biochemistry.

Radical mechanisms in adenosylmethionine- and adenosylcobalamin-dependent enzymatic reactions.

G. H. Reed, P. Frey, 2000, Archives of biochemistry and biophysics.

Probing interactions from solvent‐exchangeable protons and monovalent cations with the 1,2‐propanediol‐1‐yl radical intermediate in the reaction of dioldehydrase

G. H. Reed, P. Frey, Phillip A. Schwartz, 2007, Protein science : a publication of the Protein Society.

Radicals in enzymatic reactions.

P. Frey, 1997, Current opinion in chemical biology.

Fluorescence and nucleotide binding properties of Escherichia coli uridine diphosphate galactose 4-epimerase: support for a model for nonstereospedific action.

P. Frey, S. Wong, 1977, Biochemistry.

Synthesis and Characterization of 3‘,4‘-Anhydroadenosylcobalamin: A Coenzyme B12 Analogue with Unusual Properties

P. Frey, Olafur Th. Magnusson and, 2000 .

Stereochemical course of nucleotidyl transfer catalyzed by bacteriophage T7 induced DNA polymerase.

P. Frey, W. Stec, P. Modrich, 1982, Biochemistry.

Dioldehydrase: an essential role for potassium ion in the homolytic cleavage of the cobalt-carbon bond in adenosylcobalamin.

P. Frey, Phillip A. Schwartz, 2007, Biochemistry.

A locking mechanism preventing radical damage in the absence of substrate, as revealed by the x-ray structure of lysine 5,6-aminomutase.

Catherine L Drennan, Eva A Enns, P. Frey, 2004, Proceedings of the National Academy of Sciences of the United States of America.

[14] Stereochemistry of selected phosphotransferases and nucleotidyltransferases

P. Frey, J. Richard, R. Sammons, 1982 .

Stereochemistry of enzymatic reactions of phosphates

P. Frey, 1982 .

Chapter 5 Stereochemistry of enzymatic substitution at phosphorus

P. Frey, 1982 .

Stereochemical course of thiophosphoryl transfer catalyzed by cytosolic phosphoenolpyruvate carboxykinase.

P. Frey, H. Lardy, J. Konopka, 1986, Biochemistry.

The stereochemical course of thiophosphoryl group transfer catalyzed by adenosine kinase.

P. Frey, J. Richard, D. Ives, 1980, Biochemical and biophysical research communications.

Gentamicin nucleotidyltransferase. Stereochemical inversion at phosphorus in enzymatic 2'-deoxyadenylyl transfer to tobramycin.

P. Frey, R. Iyengar, J. V. Van Pelt, 1986, The Journal of biological chemistry.

Studies on the mechanism of action of cobamide coenzymes. Chemical properties of the enzyme-coenzyme complex.

P. Frey, R. Abeles, H. A. Lee, 1966, The Journal of biological chemistry.

Stereochemical courses of nucleotidyltransferase and phosphotransferase action. Uridine diphosphate glucose pyrophosphorylase, galactose-1-phosphate uridylyltransferase, adenylate kinase, and nucleoside diphosphate kinase.

K F Sheu, J P Richard, P A Frey, 1979, Biochemistry.

4 Nucleotidyltransferases and Phosphotransferases: Stereochemistry and Covalent Intermediates

P. Frey, 1992 .

Enzymatic and 32P nuclear magnetic resonance study of adenylate kinase-catalyzed stereospecific phosphorylation of adenosine 5'-phosphorothioate.

P. Frey, K. Rex Sheu, 1977, The Journal of biological chemistry.

Effect of ion pairing on bond order and charge localization in alkyl phosphorothioates

P. Frey, J. Baraniak, 1988 .

Stereochemical course of phosphoanhydride synthesis

P. Frey, J. Richard, 1983 .

The stereochemical course of thiophosphoryl group transfer catalyzed by T4 polynucleotide kinase.

P. Frey, S. Benkovic, F. R. Bryant, 1981, The Journal of biological chemistry.

Nucleoside phosphotransferase from barley. Characterization and evidence for ping pong kinetics involving phosphoryl enzyme.

P. Frey, D. Prasher, D. Ives, 1982, The Journal of biological chemistry.

Phosphorus-oxygen bond order in adenosine 5'-O-phosphorothioate dianion

P. Frey, F. Eckstein, R. Iyengar, 1984 .

Synthesis of nucleoside [18O]pyrophosphorothioates with chiral [18O]phosphorothioate groups of known configuration. Stereochemical orientations of enzymic phosphorylations of chiral [18O]phosphorothioates

P. Frey, J. Richard, H. Ho, 1978 .

Studies on the mechanism of action of uridine diphosphate galactose 4-epimerase. II. Substrate-dependent reduction by sodium borohydride.

P. Frey, T. G. Wee, 1973, The Journal of biological chemistry.

Studies on the Mechanism of Action of Uridine Diphosphate-galactose-4-epimerase I. AN AMBIGUITY IN THE CHEMICAL TRAPPING OF A PROPOSED KETO-INTERMEDIATE BY NaB3H4

P. Frey, Janet E. Davis, T. G. Wee, 1972 .

5'-Peroxyadenosine and 5'-peroxyadenosylcobalamin as intermediates in the aerobic photolysis of adenosylcobalamin.

P. Frey, Phillip A. Schwartz, 2007, Biochemistry.

Epimerization at carbon-5' of (5'R)-[5'-2H]adenosylcobalamin by ribonucleoside triphosphate reductase: cysteine 408-independent cleavage of the Co-C5' bond.

P. Frey, J. Stubbe, Dawei Chen, 2003, Biochemistry.

Interactions of diol dehydrase and 3',4'-anhydroadenosylcobalamin: suicide inactivation by electron transfer.

P. Frey, O. Magnusson, 2002, Biochemistry.

Electron transfer in the substrate-dependent suicide inactivation of lysine 5,6-aminomutase.

P. Frey, C. Chang, K. Tang, 2001, Biochemistry.

A Novel Mechanistic Role for Pyridoxal-5′-Phosphate

P. Frey, R. Petrovich, K. Song, 1991 .

Kinetic characterization of transient free radical intermediates in reaction of lysine 2,3-aminomutase by EPR lineshape analysis.

G. H. Reed, Christopher H. Chang, P. Frey, 2002, Methods in enzymology.

Synthesis of Rp and Sp [alpha-18O]ADP from Sp and Rp beta-cyanoethyl-adenosine 5'[1-thiodiphosphate].

P. Frey, R. Sammons, 1982, The Journal of biological chemistry.

Understanding enzymic catalysis: the importance of short, strong hydrogen bonds.

P. Frey, J. Gerlt, W. Cleland, 1997, Chemistry & biology.

Low-barrier hydrogen bonding in molecular complexes analogous to histidine and aspartate in the catalytic triad of serine proteases.

P. Frey, S. A. Whitt, C. Cassidy, 1995, Biochemistry.

Galactose-1-phosphate uridylyltransferase: identification of histidine-164 and histidine-166 as critical residues by site-directed mutagenesis.

P. Frey, W. Reznikoff, T. L. Field, 1989, Biochemistry.

Surprises and revelations in biochemistry: 1950–2000

P. Frey, 2002 .

Stereochemical retention of the configuration in the action of Fhit on phosphorus-chiral substrates.

L. D. Barnes, P. Frey, P. Garrison, 1999, Biochemistry.

Three-dimensional structure of galactose-1-phosphate uridylyltransferase from Escherichia coli at 1.8 A resolution.

P. Frey, J. Wedekind, I. Rayment, 1995, Biochemistry.

pH‐Dependence in the Hydrolytic Action of the Human Fragile Histidine Triad

P. Frey, A. Arabshahi, K. Huang, 2005 .

Transient kinetics of formation and reaction of the uridylyl-enzyme form of galactose-1-P uridylyltransferase and its Q168R-variant: insight into the molecular basis of galactosemia.

P. Frey, S. Geeganage, 1998, Biochemistry.

The structure of nucleotidylated histidine-166 of galactose-1-phosphate uridylyltransferase provides insight into phosphoryl group transfer.

P A Frey, P. Frey, J. Wedekind, 1996, Biochemistry.

Galactose 1-phosphate uridylyltransferase. Isolation of a uridylyl-enzyme intermediate.

P. Frey, L. Wong, 1974, The Journal of biological chemistry.

Sulfur as a mechanistic probe in enzymatic and non-enzymatic substitution at phosphorus

P. Frey, 2010 .

Galactose-1-phosphate uridylyltransferase: kinetics of formation and reaction of uridylyl-enzyme intermediate in wild-type and specifically mutated uridylyltransferases.

P. Frey, S. Geeganage, 2002, Methods in enzymology.

Pyruvate dehydrogenase complex of Escherichia coli: radial mass analysis of subcomplexes by scanning transmission electron microscopy.

P. Frey, J. Hainfeld, J. Wall, 1986, Biophysical journal.

Pyruvate dehydrogenase complex of Escherichia coli. Thiamin pyrophosphate and NADH-dependent hydrolysis of acetyl-CoA.

P. Frey, C. Cajacob, G. Gavino, 1985, The Journal of biological chemistry.

Chemical Intermediates in Catalysis by Thiamine Diphosphate

P. Frey, 2003 .

Synthesis and properties of 2-acetylthiamin pyrophosphate: an enzymatic reaction intermediate.

P. Frey, C. J. Halkides, K. Gruys, 1987, Biochemistry.

Inactivation of the pyruvate dehydrogenase complex of Escherichia coli by fluoropyruvate.

P. Frey, D. Flournoy, 1989, Biochemistry.

Quaternary structure of pyruvate dehydrogenase complex from Escherichia coli.

P. Frey, J. Hainfeld, J. Wall, 1985, The Journal of biological chemistry.

Escherichia coli pyruvate dehydrogenase complex. Thiamin pyrophosphate-dependent inactivation by 3-bromopyruvate.

P. Frey, Perry, David, 1984, The Journal of biological chemistry.

2-Acetylthiamin pyrophosphate (acetyl-TPP) pH-rate profile for hydrolysis of acetyl-TPP and isolation of acetyl-TPP as a transient species in pyruvate dehydrogenase catalyzed reactions.

P. Frey, K. Gruys, A. Datta, 1989, Biochemistry.

Pyruvate dehydrogenase and 3-fluoropyruvate: chemical competence of 2-acetylthiamin pyrophosphate as an acetyl group donor to dihydrolipoamide.

P. Frey, D. Flournoy, 1986, Biochemistry.

Escherichia coli alpha-ketoglutarate dehydrogenase complex.

P. Frey, C. A. Steginsky, 1984, The Journal of biological chemistry.

Snapshots of three intermediates at the active site of pyruvate oxidase

P. Frey, 2006, Nature chemical biology.

Uridine diphosphate galactose 4-epimerase: nucleotide and 8-anilino-1-naphthalenesulfonate binding properties of the substrate binding site.

P. Frey, S. Wong, 1978, Biochemistry.

Synthesis of undecagold cluster molecules as biochemical labeling reagents. 1. Monoacyl and mono[N-(succinimidooxy)succinyl] undecagold clusters.

P. Frey, J. Reardon, 1984, Biochemistry.

HYDROGEN BONDING IN COMPLEXES OF CARBOXYLIC ACIDS WITH 1-ALKYLIMIDAZOLES :STERIC AND ISOTOPIC EFFECTS ON LOW BARRIER HYDROGEN BONDING

P. Frey, W. Cleland, C. Cassidy, 1999 .

Synthesis of undecagold cluster molecules as biochemical labeling reagents. 2. Bromoacetyl and maleimido undecagold clusters.

P. Frey, H. Yang, J. Reardon, 1984, Biochemistry.

Conformations of synthetic beta peptides in solid state and in aqueous solution: relation to toxicity in PC12 cells.

P. Frey, M. Staufenbiel, H. Gremlich, 1996, Biochimica et biophysica acta.

Synthesis of chiral [18O]phosphorothioate analogs of adenine nucleotides

P. Frey, J. Richard, 1982 .

Phosphorus-sulfur bond order in phosphorothioate anions

P. Frey, P. Paneth, W. Reimschüssel, 1986 .

Prospects for Improvements in Biocatalysts for Large Scale Applications

P. Frey, Bans Liao, 1988 .

Radical stabilization is crucial in the mechanism of action of lysine 5,6-aminomutase: role of tyrosine-263α as revealed by electron paramagnetic resonance spectroscopy.

P. Frey, Yuhui Pan, S. Ke, 2011, Journal of the American Chemical Society.

Evidence for conformational movement and radical mechanism in the reaction of 4-thia-L-lysine with lysine 5,6-aminomutase.

P. Frey, K. Tang, E. Behshad, 2009, The journal of physical chemistry. B.

Kinetic and biochemical analysis of the mechanism of action of lysine 5,6-aminomutase.

P. Frey, K. Tang, Weiming Wu, 2003, Archives of biochemistry and biophysics.

Evidence implicating cyclo-diphosphates as intermediates in reactions of nucleoside phosphorothioates with cyanogen bromide

P. Frey, R. Sammons, H.-T. Ho, 1982 .

Mutation Arg336 to Lys in Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase originates an enzyme with increased oxaloacetate decarboxylase activity

P. Frey, F. González-Nilo, A. Yévenes, 2001, FEBS letters.

Enzymatic and chemical reactivities of sym-monothiopyrophosphate

P. Frey, E. Lightcap, C. J. Halkides, 1991 .

A reporter group at the active site of acetoacetate decarboxylase. I. Ionization constant of the nitrophenol.

P. Frey, F. Westheimer, F. Kokesh, 1971, Journal of the American Chemical Society.

Epimerization in the synthesis of thiophosphoanhydrides

P. Frey, R. Iyengar, 1988 .

Mevalonate-5-diphosphate decarboxylase: stereochemical course of ATP-dependent phosphorylation of mevalonate 5-diphosphate.

P. Frey, R. Iyengar, E. Cardemil, 1986, Biochemistry.

Identification of a novel pyridoxal 5'-phosphate binding site in adenosylcobalamin-dependent lysine 5,6-aminomutase from Porphyromonas gingivalis.

P. Frey, A. Harms, K. Tang, 2002, Biochemistry.

Structure and mechanism of an ADP-glucose phosphorylase from Arabidopsis thaliana.

P. Frey, G. Phillips, C. Bingman, 2006, Biochemistry.

The molecular structure of UDP‐galactose 4‐epimerase from Escherichia coli determined at 2.5 Å resolution

P A Frey, H M Holden, P. Frey, 1992, Proteins.

Standard Free Energy for the Hydrolysis of Adenylylated T4 DNA Ligase and the Apparent pK a of Lysine 159*

P. Frey, A. Arabshahi, 1999, The Journal of Biological Chemistry.

Solvent effects on the solvolysis of ADPβS

P. Frey, Yuh-Shyong Yang, 1990 .

Serine Protease Catalysis: A Computational Study of Tetrahedral Intermediates and Inhibitory Adducts.

P. Frey, Phong D. Ngo, S. Mansoorabadi, 2016, The journal of physical chemistry. B.

Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase: revised amino acid sequence, site-directed mutagenesis, and microenvironment characteristics of cysteines 365 and 458.

P. Frey, R. G. Kemp, S. Latshaw, 1995, Biochemistry.

A confluence of radical chemistry: S-Adenosylmethionine and Adenosylcob(III)alamin

P. Frey, 2018 .

The Role of S‐Adenosylmethionine as a Poor Man's Adenosylcobalamin in the Reaction of Lysine 2,3‐Aminomutase

G. H. Reed, Christopher H. Chang, P. Frey, 2007 .

5.09 – Radical Reactions Featuring Lysine 2,3-Aminomutase

P. Frey, 1999 .

Radical mechanisms of S-adenosylmethionine-dependent enzymes.

P. Frey, S. Booker, 2001, Advances in protein chemistry.

Stereochemistry of metal ion coordination to the terminal thiophosphoryl group of adenosine 5'-O-(3-thiotriphosphate) at the active site of pyruvate kinase.

G. H. Reed, P. Frey, J. Buchbinder, 1993, Biochemistry.

The stereochemical configuration of Mn(II) . ADP at the active site of creatine kinase elucidated by electron paramagnetic resonance with Rp [alpha-17O]ADP and Sp [alpha-17O]ADP.

G. H. Reed, P. Frey, T. Leyh, 1982, The Journal of biological chemistry.

Stereochemical course of thiophosphoryl group transfer catalyzed by mitochondrial phosphoenolpyruvate carboxykinase.

K F Sheu, H T Ho, L D Nolan, 1984, Biochemistry.

Stereochemical course of thiophosphoryl group transfer catalyzed by adenylate kinase

P. Frey, J. Richard, 1978 .

S-adenosylmethionine: a 'poor man's coenzyme B12' in the reaction of lysine 2,3-aminomutase.

G. H. Reed, P. Frey, M. Ballinger, 1998, Biochemical Society transactions.

Lysine 2,3-aminomutase: rapid mix-freeze-quench electron paramagnetic resonance studies establishing the kinetic competence of a substrate-based radical intermediate.

G. H. Reed, P. Frey, C. Chang, 1996, Biochemistry.

Identification of lysine 153 as a functionally important residue in UDP-galactose 4-epimerase from Escherichia coli.

P. Frey, B. Swanson, 1993, Biochemistry.

Low-barrier hydrogen bonds.

P A Frey, P. Frey, 1995, Science.

Fractionation factors and activation energies for exchange of the low barrier hydrogen bonding proton in peptidyl trifluoromethyl ketone complexes of chymotrypsin.

P. Frey, W. M. Westler, J. Markley, 1998, Proceedings of the National Academy of Sciences of the United States of America.

The deuterium isotope effect on the NMR signal of the low-barrier hydrogen bond in a transition-state analog complex of chymotrypsin.

P. Frey, C. Cassidy, J. Lin, 2000, Biochemical and biophysical research communications.

Steric Enhancement of Imidazole Basicity incis-Urocanic Acid Derivatives: Models for the Action of Chymotrypsin

P. Frey, M. Cloninger, 1998 .

Are There Strong Hydrogen Bonds in Aqueous Solutions

P. Frey, W. Cleland, 1998 .

Characterization and activation of naturally occurring abortive complexes of UDP-galactose 4-epimerase from Escherichia coli.

P. Frey, J. Vanhooke, 1994, Journal of Biological Chemistry.

Stereochemical course of a phosphokinase using a chiral [18O]phosphorothioate. Comparison with the transfer of a chiral [16O,17O,18O]phosphoryl group.

P. Frey, J. Knowles, D. Schomburg, 1980, Biochemistry.

Chiral [18O]phosphorothioates. The stereochemical course of thiophosphoryl group transfer catalyzed by nucleoside phosphotransferase.

P. Frey, D. Prasher, J. Richard, 1979, The Journal of biological chemistry.

Escherichia coli pyruvate dehydrogenase complex. Site coupling in electron and acetyl group transfer pathways.

P. Frey, S. Wong, G. Gavino, 1978, The Journal of biological chemistry.

Discrete monomeric metaphosphate anion as an intermediate in the hydrolysis of .mu.-monothiopyrophosphate

P. Frey, E. Lightcap, 1992 .

The mechanism of the hydrolysis of .mu.-monothiopyrophosphate

P. Frey, C. J. Halkides, 1991 .

Evidence for monomeric metaphosphate as an intermediate in the hydrolysis of .mu.-monothiopyrophosphate

P. Frey, E. Lightcap, 1991 .

Correlations of the basicity of His 57 with transition state analogue binding, substrate reactivity, and the strength of the low-barrier hydrogen bond in chymotrypsin.

P. Frey, C. Cassidy, J. Lin, 1998, Biochemistry.

Low-Barrier Hydrogen Bonds

P. Frey, 2013 .

Low Barrier Hydrogen Bonds

P. Frey, 2004 .

The mechanism of action of the fragile histidine triad, Fhit: isolation of a covalent adenylyl enzyme and chemical rescue of H96G-Fhit.

P. Frey, A. Arabshahi, Kaisheng Huang, 2004, Biochemistry.

The nucleotide sequence of the gal T gene of Escherichia coli.

P. Frey, W. Reznikoff, S. Adhya, 1987, Nucleic acids research.

Synthesis and Rearrangements of Alkyl Phosphorothioates

P. Frey, T. Meade, R. Iyengar, 1985 .

A new method for synthesizing phosphoanhydrides: synthesis of adenosine 5'-(2-thiodiphosphate) and adenosine 5'-(2-thiotriphosphate)

P. Frey, H. Ho, 1984 .

13C NMR analysis of electrostatic interactions between NAD+ and active site residues of UDP-galactose 4-epimerase: implications for the activation induced by uridine nucleotides.

P. Frey, J. Lin, Y. Wei, 2001, Biochemistry.

Acid-base catalysis by UDP-galactose 4-epimerase: correlations of kinetically measured acid dissociation constants with thermodynamic values for tyrosine 149.

P. Frey, E. Berger, A. Arabshahi, 2001, Biochemistry.

Correlation of Electronic Effects in N-Alkylnicotinamides with NMR Chemical Shifts and Hydride Transfer Reactivity.

P. Frey, J. Burke, 1996, Journal of Organic Chemistry.

Reaction of uridine diphosphate galactose 4-epimerase with a suicide inactivator.

P. Frey, G. R. Flentke, 1990, Biochemistry.

Uridine diphosphate galactose 4-epimerase. pH dependence of the reduction of NAD+ by a substrate analog.

P. Frey, A. Arabshahi, G. R. Flentke, 1988, The Journal of biological chemistry.

UMP-dependent reduction of UDP-galactose 4-epimerase-NAD+ complex by sodium cyanoborohydride

P. Frey, Janet E. Davis, L. D. Nolan, 1974 .

Uridine Diphosphate Galactose 4-Epimerase

P. Frey, A. Arabshahi, G. R. Flentke, 2001 .

Uridine diphosphate galactose 4-epimerase. Alkylation of enzyme-bound diphosphopyridine nucleotide by p-(bromoacetamido)phenyl uridyl pyrophosphate, an active-site-directed irreversible inhibitor.

P. Frey, Y. Wong, 1979, Biochemistry.

Escherichia coli uridine diphosphate galactose 4-epimerase: circular dichroism of the protein and protein bound dihydronicotinamide adenine dinucleotide.

P. Frey, S. Wong, J. Cassim, 1978, Biochemistry.

Correlation of Electronic Effects in N‐Alkylnicotinamides with NMR Chemical Shifts and Hydride Transfer Reactivity.

P. Frey, J. Burke, 1996 .

Uridine diphosphate galactose-4-epimerase. Uridine monophosphate-dependent reduction by alpha- and beta-D-glucose.

P. Frey, U. G. Kang, L. D. Nolan, 1975, The Journal of biological chemistry.

Synthesis of undecagold cluster molecules as biochemical labeling reagents. 3. Dimeric cluster with a single reactive amino group.

P. Frey, H. Yang, 1984, Biochemistry.

Probing catalysis by Escherichia coli dTDP-glucose-4,6-dehydratase: identification and preliminary characterization of functional amino acid residues at the active site.

P. Frey, A. Hegeman, J. Gross, 2001, Biochemistry.

Characterization of enzymatic processes by rapid mix-quench mass spectrometry: the case of dTDP-glucose 4,6-dehydratase.

P. Frey, A. Hegeman, J. Gross, 2000, Biochemistry.

Effects of oxygen-17 and oxygen-18 on phosphorus-31 NMR: further investigation and applications

P. Frey, M. Tsai, K. Bruzik, 1983 .

Significance of metal ions in galactose-1-phosphate uridylyltransferase: an essential structural zinc and a nonessential structural iron.

P. Frey, S. Geeganage, 1999, Biochemistry.

PHOSPHORUS-OXYGEN BOND ORDER IN ADENOSINE 5′-O-PHOSPHOROTHIOATE DIANION

P. Frey, F. Eckstein, R. Iyengar, 1985 .

Galactose mutarotase: pH dependence of enzymatic mutarotation.

G. Petsko, P. Frey, J. Clifton, 2003, Biochemistry.

Galactose mutarotase: purification, characterization, and investigations of two important histidine residues.

P. Frey, J. Beebe, 1998, Biochemistry.

Adenosyl coenzyme and pH dependence of the [4Fe-4S]2+/1+ transition in lysine 2,3-aminomutase.

P. Frey, G. Blackburn, F. Ruzicka, 2003, Archives of Biochemistry and Biophysics.

On low-barrier hydrogen bonds and enzyme catalysis.

P A Kollman, P. Kollman, P. Frey, 1995, Science.

Kinetic mechanism of UDP-hexose synthase, a point variant of hexose-1-phosphate uridylyltransferase from Escherichia coli.

P. Frey, F. Ruzicka, S. Geeganage, 1998, Biochemistry.

Radical triplets and suicide inhibition in reactions of 4-thia-D- and 4-thia-L-lysine with lysine 5,6-aminomutase.

G. H. Reed, P. Frey, K. Tang, 2009, Biochemistry.

Roles of two conserved amino acid residues in the active site of galactose-1-phosphate uridylyltransferase: an essential serine and a nonessential cysteine.

P. Frey, S. Geeganage, V. W. Ling, 2000, Biochemistry.

Radical stabilization is crucial in the mechanism of action of lysine 5,6-aminomutase: role of tyrosine-263α as revealed by electron paramagnetic resonance spectroscopy.

P. Frey, Yuhui Pan, S. Ke, 2011, Journal of the American Chemical Society.

Kinetic and spectroscopic evidence of negative cooperativity in the action of lysine 2,3-aminomutase.

P. Frey, F. Ruzicka, 2010, The journal of physical chemistry. B.

How an enzyme tames reactive intermediates: positioning of the active-site components of lysine 2,3-aminomutase during enzymatic turnover as determined by ENDOR spectroscopy.

P. Frey, B. Hoffman, C. Walsby, 2006, Journal of the American Chemical Society.

Galactose-1-phosphate uridylyltransferase: rate studies confirming a uridylyl-enzyme intermediate on the catalytic pathway.

P. Frey, L. Wong, 1974, Biochemistry.