| Year |
Citation |
Score |
| 2014 |
Frey PA. Travels with carbon-centered radicals. 5'-deoxyadenosine and 5'-deoxyadenosine-5'-yl in radical enzymology. Accounts of Chemical Research. 47: 540-9. PMID 24308628 DOI: 10.1021/ar400194k |
0.327 |
|
| 2013 |
Frey PA, Hegeman AD. Chemical and stereochemical actions of UDP-galactose 4-epimerase. Accounts of Chemical Research. 46: 1417-26. PMID 23339688 DOI: 10.1021/Ar300246K |
0.644 |
|
| 2013 |
Chen YH, Maity AN, Frey PA, Ke SC. Mechanism-based inhibition reveals transitions between two conformational states in the action of lysine 5,6-aminomutase: a combination of electron paramagnetic resonance spectroscopy, electron nuclear double resonance spectroscopy, and density functional theory study. Journal of the American Chemical Society. 135: 788-94. PMID 23231091 DOI: 10.1021/Ja309603A |
0.374 |
|
| 2011 |
Chen YH, Maity AN, Pan YC, Frey PA, Ke SC. 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. Journal of the American Chemical Society. 133: 17152-5. PMID 21939264 DOI: 10.1021/Ja207766C |
0.388 |
|
| 2010 |
Ruzicka FJ, Frey PA. Kinetic and spectroscopic evidence of negative cooperativity in the action of lysine 2,3-aminomutase. The Journal of Physical Chemistry. B. 114: 16118-24. PMID 20608698 DOI: 10.1021/Jp103856M |
0.329 |
|
| 2010 |
Gleick PH, Adams RM, Amasino RM, Anders E, Anderson DJ, Anderson WW, Anselin LE, Arroyo MK, Asfaw B, Ayala FJ, Bax A, Bebbington AJ, Bell G, Bennett MV, Bennetzen JL, ... ... Frey PA, et al. Climate change and the integrity of science. Science (New York, N.Y.). 328: 689-90. PMID 20448167 DOI: 10.1126/Science.328.5979.689 |
0.438 |
|
| 2010 |
Frey PA. Sulfur as a mechanistic probe in enzymatic and non-enzymatic substitution at phosphorus New Journal of Chemistry. 34: 820-828. DOI: 10.1039/B9Nj00619B |
0.395 |
|
| 2009 |
Maity AN, Hsieh CP, Huang MH, Chen YH, Tang KH, Behshad E, Frey PA, Ke SC. Evidence for conformational movement and radical mechanism in the reaction of 4-thia-L-lysine with lysine 5,6-aminomutase. The Journal of Physical Chemistry. B. 113: 12161-3. PMID 19685884 DOI: 10.1021/Jp905357A |
0.593 |
|
| 2009 |
Tang KH, Mansoorabadi SO, Reed GH, Frey PA. Radical triplets and suicide inhibition in reactions of 4-thia-D- and 4-thia-L-lysine with lysine 5,6-aminomutase. Biochemistry. 48: 8151-60. PMID 19634897 DOI: 10.1021/Bi900828F |
0.597 |
|
| 2008 |
Frey PA, Hegeman AD, Ruzicka FJ. The Radical SAM Superfamily. Critical Reviews in Biochemistry and Molecular Biology. 43: 63-88. PMID 18307109 DOI: 10.1080/10409230701829169 |
0.635 |
|
| 2007 |
Wang SC, Frey PA. Binding energy in the one-electron reductive cleavage of S-adenosylmethionine in lysine 2,3-aminomutase, a radical SAM enzyme. Biochemistry. 46: 12889-95. PMID 17944492 DOI: 10.1021/Bi701745H |
0.356 |
|
| 2007 |
Schwartz PA, Lobrutto R, Reed GH, Frey PA. Probing interactions from solvent-exchangeable protons and monovalent cations with the 1,2-propanediol-1-yl radical intermediate in the reaction of dioldehydrase. Protein Science : a Publication of the Protein Society. 16: 1157-64. PMID 17525464 DOI: 10.1110/Ps.072768007 |
0.703 |
|
| 2007 |
Schwartz PA, Frey PA. Dioldehydrase: an essential role for potassium ion in the homolytic cleavage of the cobalt-carbon bond in adenosylcobalamin. Biochemistry. 46: 7293-301. PMID 17516630 DOI: 10.1021/Bi700078Z |
0.719 |
|
| 2007 |
Schwartz PA, Frey PA. 5'-Peroxyadenosine and 5'-peroxyadenosylcobalamin as intermediates in the aerobic photolysis of adenosylcobalamin. Biochemistry. 46: 7284-92. PMID 17503776 DOI: 10.1021/Bi700077V |
0.715 |
|
| 2006 |
Mansoorabadi SO, Magnusson OT, Poyner RR, Frey PA, Reed GH. Analysis of the Cob(II)alamin-5'-deoxy-3',4'-anhydroadenosyl radical triplet spin system in the active site of diol dehydrase. Biochemistry. 45: 14362-70. PMID 17128975 DOI: 10.1021/Bi061586Q |
0.612 |
|
| 2006 |
Chen D, Frey PA, Lepore BW, Ringe D, Ruzicka FJ. Identification of structural and catalytic classes of highly conserved amino acid residues in lysine 2,3-aminomutase. Biochemistry. 45: 12647-53. PMID 17042481 DOI: 10.1021/Bi061329L |
0.355 |
|
| 2006 |
Frey PA, Hegeman AD, Reed GH. Free radical mechanisms in enzymology. Chemical Reviews. 106: 3302-16. PMID 16895329 DOI: 10.1021/Cr050292S |
0.645 |
|
| 2006 |
Hinckley GT, Frey PA. Cofactor dependence of reduction potentials for [4Fe-4S]2+/1+ in lysine 2,3-aminomutase. Biochemistry. 45: 3219-25. PMID 16519516 DOI: 10.1021/Bi0519497 |
0.769 |
|
| 2006 |
McCoy JG, Arabshahi A, Bitto E, Bingman CA, Ruzicka FJ, Frey PA, Phillips GN. Structure and mechanism of an ADP-glucose phosphorylase from Arabidopsis thaliana. Biochemistry. 45: 3154-62. PMID 16519510 DOI: 10.1021/Bi052232M |
0.333 |
|
| 2006 |
Hinckley GT, Frey PA. An adaptable spectroelectrochemical titrator: the midpoint reduction potential of the iron-sulfur center in lysine 2,3-aminomutase. Analytical Biochemistry. 349: 103-11. PMID 16384547 DOI: 10.1016/J.Ab.2005.11.021 |
0.762 |
|
| 2005 |
Lepore BW, Ruzicka FJ, Frey PA, Ringe D. The x-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale. Proceedings of the National Academy of Sciences of the United States of America. 102: 13819-24. PMID 16166264 DOI: 10.1073/Pnas.0505726102 |
0.353 |
|
| 2004 |
Goodman JL, Wang S, Alam S, Ruzicka FJ, Frey PA, Wedekind JE. Ornithine cyclodeaminase: structure, mechanism of action, and implications for the mu-crystallin family. Biochemistry. 43: 13883-91. PMID 15518536 DOI: 10.1021/Bi048207I |
0.371 |
|
| 2004 |
Berkovitch F, Behshad E, Tang KH, Enns EA, Frey PA, Drennan CL. A locking mechanism preventing radical damage in the absence of substrate, as revealed by the x-ray structure of lysine 5,6-aminomutase. Proceedings of the National Academy of Sciences of the United States of America. 101: 15870-5. PMID 15514022 DOI: 10.1073/Pnas.0407074101 |
0.572 |
|
| 2004 |
Huang K, Frey PA. Engineering human Fhit, a diadenosine triphosphate hydrolase, into an efficient dinucleoside polyphosphate synthase. Journal of the American Chemical Society. 126: 9548-9. PMID 15291552 DOI: 10.1021/Ja0400640 |
0.333 |
|
| 2004 |
Huang K, Arabshahi A, Wei Y, Frey PA. The mechanism of action of the fragile histidine triad, Fhit: isolation of a covalent adenylyl enzyme and chemical rescue of H96G-Fhit. Biochemistry. 43: 7637-42. PMID 15182206 DOI: 10.1021/Bi049762N |
0.4 |
|
| 2003 |
Chen D, Walsby C, Hoffman BM, Frey PA. Coordination and mechanism of reversible cleavage of S-adenosylmethionine by the [4Fe-4S] center in lysine 2,3-aminomutase. Journal of the American Chemical Society. 125: 11788-9. PMID 14505379 DOI: 10.1021/Ja036120Z |
0.306 |
|
| 2003 |
Tang KH, Casarez AD, Wu W, Frey PA. Kinetic and biochemical analysis of the mechanism of action of lysine 5,6-aminomutase. Archives of Biochemistry and Biophysics. 418: 49-54. PMID 13679082 DOI: 10.1016/S0003-9861(03)00346-1 |
0.585 |
|
| 2003 |
Frey PA, Magnusson OT. S-Adenosylmethionine: a wolf in sheep's clothing, or a rich man's adenosylcobalamin? Chemical Reviews. 103: 2129-48. PMID 12797826 DOI: 10.1021/Cr020422M |
0.578 |
|
| 2003 |
Hinckley GT, Ruzicka FJ, Thompson MJ, Blackburn GM, Frey PA. Adenosyl coenzyme and pH dependence of the [4Fe-4S]2+/1+ transition in lysine 2,3-aminomutase. Archives of Biochemistry and Biophysics. 414: 34-9. PMID 12745252 DOI: 10.1016/S0003-9861(03)00160-7 |
0.757 |
|
| 2003 |
Chen D, Abend A, Stubbe J, Frey PA. Epimerization at carbon-5' of (5'R)-[5'-2H]adenosylcobalamin by ribonucleoside triphosphate reductase: cysteine 408-independent cleavage of the Co-C5' bond. Biochemistry. 42: 4578-84. PMID 12693955 DOI: 10.1021/Bi030018X |
0.549 |
|
| 2003 |
Beebe JA, Arabshahi A, Clifton JG, Ringe D, Petsko GA, Frey PA. Galactose mutarotase: pH dependence of enzymatic mutarotation. Biochemistry. 42: 4414-20. PMID 12693937 DOI: 10.1021/Bi020639A |
0.309 |
|
| 2002 |
Geeganage S, Frey PA. Galactose-1-phosphate uridylyltransferase: kinetics of formation and reaction of uridylyl-enzyme intermediate in wild-type and specifically mutated uridylyltransferases. Methods in Enzymology. 354: 134-48. PMID 12418221 DOI: 10.1016/S0076-6879(02)54010-6 |
0.335 |
|
| 2002 |
Tang KH, Harms A, Frey PA. Identification of a novel pyridoxal 5'-phosphate binding site in adenosylcobalamin-dependent lysine 5,6-aminomutase from Porphyromonas gingivalis. Biochemistry. 41: 8767-76. PMID 12093296 DOI: 10.1021/Bi020255K |
0.716 |
|
| 2002 |
Magnusson OT, Frey PA. Facile hydrogen-deuterium exchange at the 5'-position of an analogue of S-adenosyl-l-methionine. Bioorganic Chemistry. 30: 53-61. PMID 11955002 DOI: 10.1006/Bioo.2001.1223 |
0.613 |
|
| 2002 |
Hegeman AD, Gross JW, Frey PA. Concerted and stepwise dehydration mechanisms observed in wild-type and mutated Escherichia coli dTDP-glucose 4,6-dehydratase. Biochemistry. 41: 2797-804. PMID 11851427 DOI: 10.1021/Bi011748C |
0.629 |
|
| 2002 |
Magnusson OT, Frey PA. Interactions of diol dehydrase and 3',4'-anhydroadenosylcobalamin: suicide inactivation by electron transfer. Biochemistry. 41: 1695-702. PMID 11814365 DOI: 10.1021/Bi011947W |
0.672 |
|
| 2001 |
Frey PA. The role of radicals in enzymatic processes. Chemical Record (New York, N.Y.). 1: 277-89. PMID 11893068 DOI: 10.1002/tcr.1013 |
0.3 |
|
| 2001 |
Frey PA, Booker SJ. Radical mechanisms of S-adenosylmethionine-dependent enzymes. Advances in Protein Chemistry. 58: 1-45. PMID 11665486 DOI: 10.1016/S0065-3233(01)58001-8 |
0.628 |
|
| 2001 |
Gross JW, Hegeman AD, Gerratana B, Frey PA. Dehydration is catalyzed by glutamate-136 and aspartic acid-135 active site residues in Escherichia coli dTDP-glucose 4,6-dehydratase. Biochemistry. 40: 12497-504. PMID 11601973 DOI: 10.1021/Bi011138C |
0.636 |
|
| 2001 |
Wei Y, Lin J, Frey PA. 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. Biochemistry. 40: 11279-87. PMID 11551228 DOI: 10.1021/Bi011085Z |
0.34 |
|
| 2001 |
Gerratana B, Cleland WW, Frey PA. Mechanistic roles of Thr134, Tyr160, and Lys 164 in the reaction catalyzed by dTDP-glucose 4,6-dehydratase. Biochemistry. 40: 9187-95. PMID 11478886 DOI: 10.1021/Bi0108249 |
0.385 |
|
| 2001 |
Magnusson OT, Reed GH, Frey PA. Characterization of an allylic analogue of the 5'-deoxyadenosyl radical: an intermediate in the reaction of lysine 2,3-aminomutase. Biochemistry. 40: 7773-82. PMID 11425303 DOI: 10.1021/Bi0104569 |
0.658 |
|
| 2001 |
Frey PA. Radical mechanisms of enzymatic catalysis. Annual Review of Biochemistry. 70: 121-48. PMID 11395404 DOI: 10.1146/annurev.biochem.70.1.121 |
0.321 |
|
| 2001 |
Berger E, Arabshahi A, Wei Y, Schilling JF, Frey PA. Acid-base catalysis by UDP-galactose 4-epimerase: correlations of kinetically measured acid dissociation constants with thermodynamic values for tyrosine 149. Biochemistry. 40: 6699-705. PMID 11380265 DOI: 10.1021/Bi0104571 |
0.303 |
|
| 2001 |
Hegeman AD, Gross JW, Frey PA. Probing catalysis by Escherichia coli dTDP-glucose-4,6-dehydratase: identification and preliminary characterization of functional amino acid residues at the active site. Biochemistry. 40: 6598-610. PMID 11380254 DOI: 10.1021/Bi010441A |
0.608 |
|
| 2001 |
Neidhart D, Wei Y, Cassidy C, Lin J, Cleland WW, Frey PA. Correlation of low-barrier hydrogen bonding and oxyanion binding in transition state analogue complexes of chymotrypsin. Biochemistry. 40: 2439-47. PMID 11327865 DOI: 10.1021/Bi002535A |
0.357 |
|
| 2001 |
Tang KH, Chang CH, Frey PA. Electron transfer in the substrate-dependent suicide inactivation of lysine 5,6-aminomutase. Biochemistry. 40: 5190-9. PMID 11318641 DOI: 10.1021/Bi010157J |
0.648 |
|
| 2001 |
Chen D, Frey PA. Identification of lysine 346 as a functionally important residue for pyridoxal 5'-phosphate binding and catalysis in lysine 2, 3-aminomutase from Bacillus subtilis. Biochemistry. 40: 596-602. PMID 11148055 DOI: 10.1021/Bi002265W |
0.398 |
|
| 2000 |
Cosper NJ, Booker SJ, Ruzicka F, Frey PA, Scott RA. Direct FeS cluster involvement in generation of a radical in lysine 2,3-aminomutase. Biochemistry. 39: 15668-73. PMID 11123891 DOI: 10.1021/Bi0022184 |
0.629 |
|
| 2000 |
Gross JW, Hegeman AD, Vestling MM, Frey PA. Characterization of enzymatic processes by rapid mix-quench mass spectrometry: the case of dTDP-glucose 4,6-dehydratase. Biochemistry. 39: 13633-40. PMID 11076501 DOI: 10.1021/Bi001963D |
0.74 |
|
| 2000 |
Hedstrom L, Frey PA. Robert H. Abeles (1926-2000). Nature. 407: 854. PMID 11057653 DOI: 10.1038/35038202 |
0.455 |
|
| 2000 |
Wu W, Booker S, Lieder KW, Bandarian V, Reed GH, Frey PA. Lysine 2,3-aminomutase and trans-4,5-dehydrolysine: characterization of an allylic analogue of a substrate-based radical in the catalytic mechanism. Biochemistry. 39: 9561-70. PMID 10924153 DOI: 10.1021/Bi000658P |
0.635 |
|
| 2000 |
Geeganage S, Ling VW, Frey PA. Roles of two conserved amino acid residues in the active site of galactose-1-phosphate uridylyltransferase: an essential serine and a nonessential cysteine. Biochemistry. 39: 5397-404. PMID 10820011 DOI: 10.1021/Bi992594S |
0.426 |
|
| 2000 |
Magnusson OT, Frey PA. Synthesis and characterization of 3',4'-anhydroadenosylcobalamin: A coenzyme B12 analogue with unusual properties Journal of the American Chemical Society. 122: 8807-8813. DOI: 10.1021/Ja0013780 |
0.648 |
|
| 2000 |
Magnusson OT, Frey PA. Synthesis and characterization of 3′,4′-anhydroadenosylcobalamin: A coenzyme B12 analogue with unusual properties Journal of the American Chemical Society. 122: X. |
0.558 |
|
| 1999 |
Geeganage S, Frey PA. Significance of metal ions in galactose-1-phosphate uridylyltransferase: an essential structural zinc and a nonessential structural iron. Biochemistry. 38: 13398-406. PMID 10529216 DOI: 10.1021/Bi9910631 |
0.347 |
|
| 1999 |
Abend A, Garrison PN, Barnes LD, Frey PA. Stereochemical retention of the configuration in the action of Fhit on phosphorus-chiral substrates. Biochemistry. 38: 3668-76. PMID 10090754 DOI: 10.1021/Bi981895J |
0.395 |
|
| 1999 |
Magnusson OT, Reed GH, Frey PA. Spectroscopic evidence for the participation of an allylic analogue of the 5'-deoxyadenosyl radical in the reaction of lysine 2,3-aminomutase [22] Journal of the American Chemical Society. 121: 9764-9765. DOI: 10.1021/Ja9925507 |
0.632 |
|
| 1998 |
Beebe JA, Frey PA. Galactose mutarotase: purification, characterization, and investigations of two important histidine residues. Biochemistry. 37: 14989-97. PMID 9778377 DOI: 10.1021/Bi9816047 |
0.366 |
|
| 1998 |
Geeganage S, Frey PA. 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. Biochemistry. 37: 14500-7. PMID 9772178 DOI: 10.1021/Bi9815546 |
0.393 |
|
| 1998 |
Cleland WW, Frey PA, Gerlt JA. The low barrier hydrogen bond in enzymatic catalysis. The Journal of Biological Chemistry. 273: 25529-32. PMID 9748211 DOI: 10.1074/Jbc.273.40.25529 |
0.451 |
|
| 1998 |
Lin J, Cassidy CS, Frey PA. 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. Biochemistry. 37: 11940-8. PMID 9718318 DOI: 10.1021/Bi980278S |
0.329 |
|
| 1998 |
Ruzicka FJ, Geeganage S, Frey PA. Kinetic mechanism of UDP-hexose synthase, a point variant of hexose-1-phosphate uridylyltransferase from Escherichia coli. Biochemistry. 37: 11385-92. PMID 9698386 DOI: 10.1021/Bi980877Z |
0.403 |
|
| 1998 |
Lieder KW, Booker S, Ruzicka FJ, Beinert H, Reed GH, Frey PA. S-Adenosylmethionine-dependent reduction of lysine 2,3-aminomutase and observation of the catalytically functional iron-sulfur centers by electron paramagnetic resonance. Biochemistry. 37: 2578-85. PMID 9485408 DOI: 10.1021/Bi972417W |
0.651 |
|
| 1997 |
Liu Y, Thoden JB, Kim J, Berger E, Gulick AM, Ruzicka FJ, Holden HM, Frey PA. Mechanistic roles of tyrosine 149 and serine 124 in UDP-galactose 4-epimerase from Escherichia coli. Biochemistry. 36: 10675-84. PMID 9271498 DOI: 10.1021/Bi970430A |
0.363 |
|
| 1997 |
Gerlt JA, Kreevoy MM, Cleland W, Frey PA. Understanding enzymic catalysis: the importance of short, strong hydrogen bonds. Chemistry & Biology. 4: 259-67. PMID 9195866 DOI: 10.1016/S1074-5521(97)90069-7 |
0.505 |
|
| 1997 |
Thoden JB, Hegeman AD, Wesenberg G, Chapeau MC, Frey PA, Holden HM. Structural analysis of UDP-sugar binding to UDP-galactose 4-epimerase from Escherichia coli. Biochemistry. 36: 6294-304. PMID 9174344 DOI: 10.1021/Bi970025J |
0.652 |
|
| 1997 |
Cassidy CS, Lin J, Frey PA. A new concept for the mechanism of action of chymotrypsin: the role of the low-barrier hydrogen bond. Biochemistry. 36: 4576-84. PMID 9109667 DOI: 10.1021/Bi962013O |
0.371 |
|
| 1997 |
Thoden JB, Ruzicka FJ, Frey PA, Rayment I, Holden HM. 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. Biochemistry. 36: 1212-22. PMID 9063869 DOI: 10.1021/Bi9626517 |
0.37 |
|
| 1996 |
Wedekind JE, Frey PA, Rayment I. The structure of nucleotidylated histidine-166 of galactose-1-phosphate uridylyltransferase provides insight into phosphoryl group transfer. Biochemistry. 35: 11560-9. PMID 8794735 DOI: 10.1021/Bi9612677 |
0.418 |
|
| 1996 |
Chang CH, Ballinger MD, Reed GH, Frey PA. Lysine 2,3-aminomutase: rapid mix-freeze-quench electron paramagnetic resonance studies establishing the kinetic competence of a substrate-based radical intermediate. Biochemistry. 35: 11081-4. PMID 8780510 DOI: 10.1021/Bi960850K |
0.424 |
|
| 1996 |
Liu Y, Vanhooke JL, Frey PA. UDP-galactose 4-epimerase: NAD+ content and a charge-transfer band associated with the substrate-induced conformational transition. Biochemistry. 35: 7615-20. PMID 8652544 DOI: 10.1021/Bi960102V |
0.352 |
|
| 1996 |
Thoden JB, Frey PA, Holden HM. Crystal structures of the oxidized and reduced forms of UDP-galactose 4-epimerase isolated from Escherichia coli. Biochemistry. 35: 2557-66. PMID 8611559 DOI: 10.1021/Bi952715Y |
0.362 |
|
| 1996 |
Thoden JB, Frey PA, Holden HM. Molecular structure of the NADH/UDP-glucose abortive complex of UDP-galactose 4-epimerase from Escherichia coli: implications for the catalytic mechanism. Biochemistry. 35: 5137-44. PMID 8611497 DOI: 10.1021/Bi9601114 |
0.37 |
|
| 1995 |
Tobin JB, Whitt SA, Cassidy CS, Frey PA. Low-barrier hydrogen bonding in molecular complexes analogous to histidine and aspartate in the catalytic triad of serine proteases. Biochemistry. 34: 6919-24. PMID 7766600 DOI: 10.1021/Bi00021A002 |
0.323 |
|
| 1995 |
Krautwurst H, Encinas MV, Marcus F, Latshaw SP, Kemp RG, Frey PA, Cardemil E. Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase: revised amino acid sequence, site-directed mutagenesis, and microenvironment characteristics of cysteines 365 and 458. Biochemistry. 34: 6382-8. PMID 7756267 DOI: 10.1021/Bi00019A017 |
0.317 |
|
| 1995 |
Ruzicka FJ, Wedekind JE, Kim J, Rayment I, Frey PA. Galactose-1-phosphate uridylyltransferase from Escherichia coli, a zinc and iron metalloenzyme. Biochemistry. 34: 5610-7. PMID 7727423 DOI: 10.1021/Bi00016A036 |
0.335 |
|
| 1995 |
Wedekind JE, Frey PA, Rayment I. Three-dimensional structure of galactose-1-phosphate uridylyltransferase from Escherichia coli at 1.8 A resolution. Biochemistry. 34: 11049-61. PMID 7669762 DOI: 10.1021/Bi00035A010 |
0.359 |
|
| 1995 |
Wu W, Lieder KW, Reed GH, Frey PA. Observation of a second substrate radical intermediate in the reaction of lysine 2,3-aminomutase: a radical centered on the beta-carbon of the alternative substrate, 4-thia-L-lysine. Biochemistry. 34: 10532-7. PMID 7654708 DOI: 10.1021/Bi00033A027 |
0.377 |
|
| 1995 |
Ballinger MD, Frey PA, Reed GH, LoBrutto R. Pulsed electron paramagnetic resonance studies of the lysine 2,3-aminomutase substrate radical: evidence for participation of pyridoxal 5'-phosphate in a radical rearrangement. Biochemistry. 34: 10086-93. PMID 7632680 DOI: 10.1021/Bi00031A033 |
0.357 |
|
| 1994 |
Tamada Y, Swanson BA, Arabshahi A, Frey PA. Preparation and characterization of a bifunctional fusion enzyme composed of UDP-galactose 4-epimerase and galactose-1-P uridylyltransferase. Bioconjugate Chemistry. 5: 660-5. PMID 7873670 DOI: 10.1021/Bc00030A023 |
0.337 |
|
| 1993 |
Frey PA. Lysine 2,3-aminomutase: Is adenosylmethionine a poor man's adenosylcobalamin? Faseb Journal. 7: 662-670. PMID 8500691 |
0.317 |
|
| 1993 |
Buchbinder JL, Baraniak J, Frey PA, Reed GH. Stereochemistry of metal ion coordination to the terminal thiophosphoryl group of adenosine 5'-O-(3-thiotriphosphate) at the active site of pyruvate kinase. Biochemistry. 32: 14111-6. PMID 8260493 DOI: 10.1021/Bi00214A006 |
0.343 |
|
| 1993 |
Swanson BA, Frey PA. Identification of lysine 153 as a functionally important residue in UDP-galactose 4-epimerase from Escherichia coli. Biochemistry. 32: 13231-6. PMID 8241178 DOI: 10.1021/Bi00211A035 |
0.377 |
|
| 1993 |
Burke JR, Frey PA. The importance of binding energy in catalysis of hydride transfer by UDP-galactose 4-epimerase: a 13C and 15N NMR and kinetic study. Biochemistry. 32: 13220-30. PMID 8241177 DOI: 10.1021/Bi00211A034 |
0.368 |
|
| 1992 |
Ballinger MD, Frey PA, Reed GH. Structure of a substrate radical intermediate in the reaction of lysine 2,3-aminomutase Biochemistry. 31: 10782-10789. PMID 1329955 DOI: 10.1021/Bi00159A020 |
0.39 |
|
| 1992 |
Petrovich RM, Ruzicka FJ, Reed GH, Frey PA. Characterization of iron-sulfur clusters in lysine 2,3-aminomutase by electron paramagnetic resonance spectroscopy Biochemistry. 31: 10774-10781. PMID 1329954 DOI: 10.1021/Bi00159A019 |
0.388 |
|
| 1992 |
Ballinger MD, Reed GH, Frey PA. An organic radical in the lysine 2,3-aminomutase reaction Biochemistry®. 31: 949-953. PMID 1310425 DOI: 10.1021/Bi00119A001 |
0.432 |
|
| 1991 |
Halkides CJ, Lightcap ES, Frey PA. The substrate reactivity of μ-monothiopyrophosphate with pyrophosphate-dependent phosphofructokinase: Evidence for a dissociative transition state in enzymatic phosphoryl group transfer Biochemistry. 30: 10313-10322. PMID 1657145 DOI: 10.1021/Bi00106A032 |
0.415 |
|
| 1991 |
Lightcap ES, Frey PA. Evidence for monomeric metaphosphate as an intermediate in the hydrolysis of μ-monothiopyrophosphate Journal of the American Chemical Society. 113: 9415-9416. DOI: 10.1021/Ja00024A084 |
0.312 |
|
| 1990 |
Ruzicka F, Huang DS, Donnelly MI, Frey PA. Methane monooxygenase catalyzed oxygenation of 1,1-dimethylcyclopropane. Evidence for radical and carbocationic intermediates. Biochemistry. 29: 1696-700. PMID 2331458 DOI: 10.1021/Bi00459A005 |
0.357 |
|
| 1990 |
Kim J, Ruzicka F, Frey PA. Remodeling hexose-1 -phosphate uridylyltransferase: Mechanism-inspired mutation into a new enzyme, UDP-hexose synthase Biochemistry. 29: 10590-10593. PMID 2271670 DOI: 10.1021/Bi00499A003 |
0.391 |
|
| 1990 |
Flentke GR, Frey PA. Reaction of uridine diphosphate galactose 4-epimerase with a suicide inactivator Biochemistry. 29: 2430-2436. PMID 2186813 DOI: 10.1021/Bi00461A029 |
0.416 |
|
| 1990 |
Han O, Frey PA. Chemical model for the pyridoxal 5'-phosphate dependent lysine aminomutases Journal of the American Chemical Society. 112: 8982-8983. DOI: 10.1021/Ja00180A054 |
0.323 |
|
| 1989 |
Frey PA. 2-Acetylthiamin pyrophosphate: An enzyme-bound intermediate in thiamin pyrophosphate-dependent reactions Biofactors. 2: 1-9. PMID 2679649 |
0.301 |
|
| 1989 |
Konopka JM, Halkides CJ, Vanhooke JL, Gorenstein DG, Frey PA. UDP-galactose 4-epimerase. Phosphorus-31 nuclear magnetic resonance analysis of NAD+ and NADH bound at the active site Biochemistry. 28: 2645-2654. PMID 2659075 DOI: 10.1021/Bi00432A043 |
0.562 |
|
| 1989 |
Gruys KJ, Datta A, Frey PA. 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 Biochemistry. 28: 9071-9080. PMID 2605241 DOI: 10.1021/Bi00449A018 |
0.325 |
|
| 1989 |
Field TL, Reznikoff WS, Frey PA. Galactose-1-phosphate uridylyltransferase: identification of histidine-164 and histidine-166 as critical residues by site-directed mutagenesis. Biochemistry. 28: 2094-9. PMID 2541773 DOI: 10.1021/Bi00431A019 |
0.349 |
|
| 1989 |
Cole R, Frey P, Stubbe J, Sigman D. Abstracts, division of biological chemistry, 199th national meeting of the American chemical society, April 22-27, 1990 Biochemistry. 28: 2181-2204. DOI: 10.1021/Bi00430A600 |
0.434 |
|
| 1988 |
Gruys KJ, Halkides CJ, Frey PA. Synthesis and properties of 2-acetylthiamin pyrophosphate: an enzymatic reaction intermediate. Biochemistry. 26: 7575-85. PMID 2827756 DOI: 10.1021/Bi00398A007 |
0.344 |
|
| 1986 |
Konopka JM, Lardy HA, Frey PA. Stereochemical course of thiophosphoryl transfer catalyzed by cytosolic phosphoenolpyruvate carboxykinase. Biochemistry. 25: 5571-5. PMID 3778874 DOI: 10.1021/Bi00367A034 |
0.388 |
|
| 1986 |
Iyengar R, Cardemil E, Frey PA. Mevalonate-5-diphosphate decarboxylase: stereochemical course of ATP-dependent phosphorylation of mevalonate 5-diphosphate. Biochemistry. 25: 4693-8. PMID 3768305 DOI: 10.1021/Bi00364A036 |
0.345 |
|
| 1986 |
Flournoy DS, Frey PA. Pyruvate dehydrogenase and 3-fluoropyruvate: chemical competence of 2-acetylthiamin pyrophosphate as an acetyl group donor to dihydrolipoamide. Biochemistry. 25: 6036-43. PMID 3098283 DOI: 10.1021/Bi00368A030 |
0.351 |
|
| 1985 |
Meade TJ, Iyengar R, Frey PA. Synthesis and rearrangements of alkyl phosphorothioates Journal of Organic Chemistry. 50: 936-940. DOI: 10.1002/Chin.198535239 |
0.507 |
|
| 1984 |
Yang H, Frey PA. Synthesis of undecagold cluster molecules as biochemical labeling reagents. 3. Dimeric cluster with a single reactive amino group. Biochemistry. 23: 3863-8. PMID 6487583 DOI: 10.1021/Bi00312A011 |
0.318 |
|
| 1984 |
Sheu KF, Ho HT, Nolan LD, Markovitz P, Richard JP, Utter MF, Frey PA. Stereochemical course of thiophosphoryl group transfer catalyzed by mitochondrial phosphoenolpyruvate carboxykinase. Biochemistry. 23: 1779-83. PMID 6372862 DOI: 10.1021/Bi00303A030 |
0.546 |
|
| 1984 |
RICHARD JP, FREY PA. ChemInform Abstract: STEREOCHEMICAL COURSE OF PHOSPHOANHYDRIDE SYNTHESIS Chemischer Informationsdienst. 15. DOI: 10.1002/chin.198406224 |
0.416 |
|
| 1983 |
Frey PA, Richard JP, Ho HT, Brody RS, Sammons RD, Sheu KF. Stereochemistry of selected phosphotransferases and nucleotidyltransferases. Methods in Enzymology. 87: 213-35. PMID 6294450 DOI: 10.1016/S0076-6879(82)87016-X |
0.535 |
|
| 1983 |
Frey PA, Wong LJ, Sheu KF, Yang SL. Galactose-1-phosphate uridylyltransferase: detection, isolation, and characterization of the uridylyl enzyme. Methods in Enzymology. 87: 20-36. PMID 6294449 DOI: 10.1016/S0076-6879(82)87004-3 |
0.375 |
|
| 1983 |
Richard JP, Frey PA. Stereochemical course of phosphoanhydride synthesis Journal of the American Chemical Society. 105: 6605-6609. DOI: 10.1002/Chin.198406224 |
0.47 |
|
| 1982 |
Frey PA. Mechanism of coupled electron and group transfer in Escherichia coli pyruvate dehydrogenase. Annals of the New York Academy of Sciences. 378: 250-64. PMID 6805383 DOI: 10.1111/J.1749-6632.1982.Tb31201.X |
0.302 |
|
| 1982 |
Sammons RD, Ho HT, Frey PA. Evidence implicating cyclo-diphosphates as intermediates in reactions of nucleoside phosphorothioates with cyanogen bromide Journal of the American Chemical Society. 104: 5841-5842. DOI: 10.1021/Ja00385A073 |
0.33 |
|
| 1982 |
Richard JP, Frey PA. Synthesis of chiral [18O]phosphorothioate analogs of adenine nucleotides Journal of the American Chemical Society. 104: 3476-3481. DOI: 10.1021/Ja00376A038 |
0.498 |
|
| 1982 |
Frey PA. Chapter 5 Stereochemistry of enzymatic substitution at phosphorus New Comprehensive Biochemistry. 3: 201-248. DOI: 10.1016/S0167-7306(08)60396-8 |
0.347 |
|
| 1982 |
Frey PA. Stereochemistry of enzymatic reactions of phosphates Tetrahedron. 38: 1541-1567. DOI: 10.1016/0040-4020(82)80130-0 |
0.333 |
|
| 1982 |
RICHARD JP, FREY PA. ChemInform Abstract: SYNTHESIS OF CHIRAL (18O)PHOSPHOROTHIOATE ANALOGS OF ADENINE NUCLEOTIDES Chemischer Informationsdienst. 13. DOI: 10.1002/Chin.198239364 |
0.502 |
|
| 1980 |
Richard JP, Carr MC, Ives DH, Frey PA. The stereochemical course of thiophosphoryl group transfer catalyzed by adenosine kinase. Biochemical and Biophysical Research Communications. 94: 1052-6. PMID 6249295 DOI: 10.1016/0006-291X(80)90525-2 |
0.532 |
|
| 1980 |
Pliura DH, Schomburg D, Richard JP, Frey PA, Knowles JR. Stereochemical course of a phosphokinase using a chiral [18O]phosphorothioate. Comparison with the transfer of a chiral [16O,17O,18O]phosphoryl group. Biochemistry. 19: 325-9. PMID 6243477 DOI: 10.1021/Bi00543A012 |
0.515 |
|
| 1980 |
Wong YH, Winer FB, Frey PA. p-(Bromoacetamido)phenyl uridyl pyrophosphate: an active-site-directed irreversible inhibitor for uridine diphosphate galactose 4-epimerase. Biochemistry. 18: 5332-6. PMID 391265 DOI: 10.1021/Bi00591A011 |
0.336 |
|
| 1980 |
Sheu KF, Richard JP, Frey PA. Stereochemical courses of nucleotidyltransferase and phosphotransferase action. Uridine diphosphate glucose pyrophosphorylase, galactose-1-phosphate uridylyltransferase, adenylate kinase, and nucleoside diphosphate kinase. Biochemistry. 18: 5548-56. PMID 229894 DOI: 10.1021/Bi00592A004 |
0.483 |
|
| 1980 |
Wong YH, Frey PA. Uridine diphosphate galactose 4-epimerase. Alkylation of enzyme-bound diphosphopyridine nucleotide by p-(bromoacetamido)phenyl uridyl pyrophosphate, an active-site-directed irreversible inhibitor. Biochemistry. 18: 5337-41. PMID 229891 DOI: 10.1021/Bi00591A012 |
0.365 |
|
| 1979 |
Yang SL, Frey PA. Nucleophile in the active site of Escherichia coli galactose-1-phosphate uridylyltransferase: degradation of the uridylyl-enzyme intermediate to N3-phosphohistidine. Biochemistry. 18: 2980-4. PMID 380639 DOI: 10.1021/Bi00581A011 |
0.342 |
|
| 1979 |
RICHARD JP, HO H, FREY PA. ChemInform Abstract: SYNTHESIS OF NUCLEOSIDE (18O)PYROPHOSPHOROTHIOATES WITH CHIRAL (18O)PHOSPHOROTHIOATE GROUPS OF KNOWN CONFIGURATION. STEREOCHEMICAL ORIENTATIONS OF ENZYMIC PHOSPHORYLATIONS OF CHIRAL (18O)PHOSPHOROTHIOATES Chemischer Informationsdienst. 10. DOI: 10.1002/Chin.197909339 |
0.515 |
|
| 1978 |
Leung LS, Frey PA. Fluoropyruvate: an unusal substrate for Escherichia coli pyruvate dehydrogenase. Biochemical and Biophysical Research Communications. 81: 274-9. PMID 352344 DOI: 10.1016/0006-291X(78)91529-2 |
0.355 |
|
| 1978 |
Wong SS, Frey PA. Uridine diphosphate galactose 4-epimerase: Nucleotide and 8-anilino-1-naphthalenesulfonate binding properties of the substrate binding site Biochemistry. 17: 3551-3556. PMID 210796 DOI: 10.1021/Bi00610A020 |
0.308 |
|
| 1978 |
Richard JP, Frey PA. Stereochemical course of thiophosphoryl group transfer catalyzed by adenylate kinase Journal of the American Chemical Society. 100: 7757-7758. DOI: 10.1021/Ja00492A069 |
0.506 |
|
| 1978 |
Richard JP, Ho H, Frey PA. Synthesis of nucleoside [18O]pyrophosphorothioates with chiral [18O]phosphorothioate groups of known configuration. Stereochemical orientations of enzymic phosphorylations of chiral [18O]phosphorothioates Journal of the American Chemical Society. 100: 7756-7757. DOI: 10.1021/Ja00492A068 |
0.513 |
|
| 1977 |
Speckhard DC, Ikeda BH, Wong SS, Frey PA. Acetylation stoichiometry of Escherichia coli pyruvate dehydrogenase complex. Biochemical and Biophysical Research Communications. 77: 708-13. PMID 332166 DOI: 10.1016/S0006-291X(77)80036-3 |
0.304 |
|
| 1977 |
Wong LJ, Sheu KF, Lee SL, Frey PA. Galactose-1-phosphate uridylyltransferase: isolation and properties of a uridylyl-enzyme intermediate. Biochemistry. 16: 1010-6. PMID 321007 DOI: 10.1021/Bi00624A032 |
0.383 |
|
| 1977 |
Wong SS, Frey PA. Fluorescence and nucleotide binding properties of Escherichia coli uridine diphosphate galactose 4-epimerase: Support for a model for nonstereospecific action Biochemistry. 16: 298-305. PMID 189796 DOI: 10.1021/Bi00621A022 |
0.3 |
|
| 1976 |
Wong SS, Frey PA. UDPgalactose 4-epimerase catalyzed oxygen dependent reduction of a free radical substrate analogue by two electron reducing agents [47] Journal of the American Chemical Society. 98: 7886-7887. PMID 791990 DOI: 10.1021/Ja00440A104 |
0.326 |
|
| 1974 |
Wong L, Frey PA. Galactose-1-phosphate uridylyltransferase: rate studies confirming a uridylyl-enzyme intermediate on the catalytic pathway. Biochemistry. 13: 3889-3894. PMID 4606575 DOI: 10.1021/Bi00716A011 |
0.343 |
|
| 1974 |
Davis JE, Nolan LD, Frey PA. UMP-dependent reduction of UDP-galactose 4-epimerase-NAD+ complex by sodium cyanoborohydride Biochimica Et Biophysica Acta (Bba) - Enzymology. 334: 442-447. DOI: 10.1016/0005-2744(74)90189-2 |
0.35 |
|
| 1972 |
FREY PA, KOKESH FC, WESTHEIMER FH. ChemInform Abstract: ′REPORTER-GRUPPE′ AN DER AKTIVEN STELLE VON ACETOACETAT-DECARBOXYLASE 1. MITT. DISSOZIATIONSKONSTANTE DES NITROPHENOLS 2. MITT. DISSOZIATIONSKONSTANTE DER AMINOGRUPPE Chemischer Informationsdienst. 3: no-no. DOI: 10.1002/Chin.197211121 |
0.624 |
|
| 1971 |
Essenberg MK, Frey PA, Abeles RH. Studies on the mechanism of hydrogen transfer in the coenzyme B12 dependent dioldehydrase reaction II. Journal of the American Chemical Society. 93: 1242-51. PMID 5545927 DOI: 10.1021/Ja00734A036 |
0.694 |
|
| 1971 |
Frey PA, Kokesh FC, Westheimer FH. A reporter group at the active site of acetoacetate decarboxylase. I. Ionization constant of the nitrophenol. Journal of the American Chemical Society. 93: 7266-9. PMID 5127415 DOI: 10.1021/Ja00755A024 |
0.648 |
|
| 1971 |
ESSENBERG MK, FREY PA, ABELES RH. ChemInform Abstract: MECHANISMUS DER WASSERSTOFFUEBERTRAGUNG BEI DER COENZYM B12-KATALYSIERTEN DIOLDEHYDRASE-RK. 2. MITT. Chemischer Informationsdienst. Organische Chemie. 2: no-no. DOI: 10.1002/Chin.197122114 |
0.656 |
|
| 1970 |
Frey PA, Essenberg MK, Abeles RH, Kerwar SS. Comments on a proposed mechanism of action of B12 coenzyme. Journal of the American Chemical Society. 92: 4488-9. PMID 5428391 DOI: 10.1021/Ja00717A074 |
0.658 |
|
| 1967 |
Frey PA, Kerwar SS, Abeles RH. The participation of the two non-equivalent C-5' hydrogens of B 12-coenzyme in the catalytic process. Biochemical and Biophysical Research Communications. 29: 873-9. PMID 6077819 DOI: 10.1016/0006-291X(67)90301-4 |
0.648 |
|
| 1967 |
Frey PA, Essenberg MK, Abeles RH. Studies on the mechanism of hydrogen transfer in the cobamide coenzyme-dependent dioldehydrase reaction. The Journal of Biological Chemistry. 242: 5369-77. PMID 6065100 |
0.67 |
|
| 1966 |
Wagner OW, Lee HA, Frey PA, Abeles RH. Studies on the mechanism of action of cobamide coenzymes. Chemical properties of the enzyme-coenzyme complex. The Journal of Biological Chemistry. 241: 1751-62. PMID 5945850 |
0.658 |
|
| 1966 |
Abeles RH, Frey PA. Role of B12 coenzymes in the dioldehydrase reaction. Federation Proceedings. 25: 1639-41. PMID 5927397 |
0.653 |
|
| 1966 |
Frey PA, Abeles RH. The role of the B12 coenzyme in the conversion of 1,2-propanediol to propionaldehyde. The Journal of Biological Chemistry. 241: 2732-3. PMID 5911645 |
0.63 |
|
| 1966 |
Zagalak B, Frey PA, Karabatsos GL, Abeles RH. The stereochemistry of the conversion of D and L 1,2-propanediols to propionaldehyde. The Journal of Biological Chemistry. 241: 3028-35. PMID 4287906 |
0.618 |
|
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