Year |
Citation |
Score |
2009 |
Brandt GS, Kneen MM, Chakraborty S, Baykal AT, Nemeria N, Yep A, Ruby DI, Petsko GA, Kenyon GL, McLeish MJ, Jordan F, Ringe D. Snapshot of a reaction intermediate: analysis of benzoylformate decarboxylase in complex with a benzoylphosphonate inhibitor. Biochemistry. 48: 3247-57. PMID 19320438 DOI: 10.1021/Bi801950K |
0.598 |
|
2009 |
Chakraborty S, Nemeria NS, Balakrishnan A, Brandt GS, Kneen MM, Yep A, McLeish MJ, Kenyon GL, Petsko GA, Ringe D, Jordan F. Detection and time course of formation of major thiamin diphosphate-bound covalent intermediates derived from a chromophoric substrate analogue on benzoylformate decarboxylase. Biochemistry. 48: 981-94. PMID 19140682 DOI: 10.1021/Bi801810H |
0.587 |
|
2009 |
Wang PF, Yep A, Kenyon GL, McLeish MJ. Using directed evolution to probe the substrate specificity of mandelamide hydrolase. Protein Engineering, Design & Selection : Peds. 22: 103-10. PMID 19074156 DOI: 10.1093/Protein/Gzn073 |
0.593 |
|
2008 |
Brandt GS, Nemeria N, Chakraborty S, McLeish MJ, Yep A, Kenyon GL, Petsko GA, Jordan F, Ringe D. Probing the active center of benzaldehyde lyase with substitutions and the pseudosubstrate analogue benzoylphosphonic acid methyl ester. Biochemistry. 47: 7734-43. PMID 18570438 DOI: 10.1021/Bi8004413 |
0.664 |
|
2008 |
Yeung CK, Yep A, Kenyon GL, McLeish MJ. Physical, kinetic and spectrophotometric studies of a NAD(P)-dependent benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633. Biochimica Et Biophysica Acta. 1784: 1248-55. PMID 18498778 DOI: 10.1016/J.Bbapap.2008.04.015 |
0.622 |
|
2008 |
Yep A, Kenyon GL, McLeish MJ. Saturation mutagenesis of putative catalytic residues of benzoylformate decarboxylase provides a challenge to the accepted mechanism. Proceedings of the National Academy of Sciences of the United States of America. 105: 5733-8. PMID 18398009 DOI: 10.1073/Pnas.0709657105 |
0.646 |
|
2008 |
Chakraborty S, Nemeria N, Yep A, McLeish MJ, Kenyon GL, Jordan F. Mechanism of benzaldehyde lyase studied via thiamin diphosphate-bound intermediates and kinetic isotope effects. Biochemistry. 47: 3800-9. PMID 18314961 DOI: 10.1021/Bi702302U |
0.604 |
|
2007 |
Nemeria N, Korotchkina L, McLeish MJ, Kenyon GL, Patel MS, Jordan F. Elucidation of the chemistry of enzyme-bound thiamin diphosphate prior to substrate binding: defining internal equilibria among tautomeric and ionization states. Biochemistry. 46: 10739-44. PMID 17715948 DOI: 10.1021/Bi700838Q |
0.656 |
|
2007 |
Bera AK, Polovnikova LS, Roestamadji J, Widlanski TS, Kenyon GL, McLeish MJ, Hasson MS. Mechanism-based inactivation of benzoylformate decarboxylase, a thiamin diphosphate-dependent enzyme. Journal of the American Chemical Society. 129: 4120-1. PMID 17367138 DOI: 10.1021/Ja068636Z |
0.62 |
|
2006 |
Yep A, Kenyon GL, McLeish MJ. Determinants of substrate specificity in KdcA, a thiamin diphosphate-dependent decarboxylase. Bioorganic Chemistry. 34: 325-36. PMID 17028071 DOI: 10.1016/J.Bioorg.2006.08.005 |
0.63 |
|
2006 |
Wang PF, Flynn AJ, Naor MM, Jensen JH, Cui G, Merz KM, Kenyon GL, McLeish MJ. Exploring the role of the active site cysteine in human muscle creatine kinase. Biochemistry. 45: 11464-72. PMID 16981706 DOI: 10.1021/Bi0607002 |
0.581 |
|
2006 |
Wang PF, Kenyon GL, McLeish MJ. Heterogeneity of Escherichia coli-expressed human muscle creatine kinase. Iubmb Life. 58: 421-8. PMID 16801217 DOI: 10.1080/15216540600779394 |
0.585 |
|
2006 |
Andricopulo AD, Akoachere MB, Krogh R, Nickel C, McLeish MJ, Kenyon GL, Arscott LD, Williams CH, Davioud-Charvet E, Becker K. Specific inhibitors of Plasmodium falciparum thioredoxin reductase as potential antimalarial agents. Bioorganic & Medicinal Chemistry Letters. 16: 2283-92. PMID 16458512 DOI: 10.1016/J.Bmcl.2006.01.027 |
0.545 |
|
2005 |
Kneen MM, Pogozheva ID, Kenyon GL, McLeish MJ. Exploring the active site of benzaldehyde lyase by modeling and mutagenesis. Biochimica Et Biophysica Acta. 1753: 263-71. PMID 16226928 DOI: 10.1016/J.Bbapap.2005.08.025 |
0.614 |
|
2005 |
Wang PF, Flynn AJ, McLeish MJ, Kenyon GL. Loop movement and catalysis in creatine kinase. Iubmb Life. 57: 355-62. PMID 16036620 DOI: 10.1080/15216540500091999 |
0.602 |
|
2005 |
Siegert P, McLeish MJ, Baumann M, Iding H, Kneen MM, Kenyon GL, Pohl M. Exchanging the substrate specificities of pyruvate decarboxylase from Zymomonas mobilis and benzoylformate decarboxylase from Pseudomonas putida. Protein Engineering, Design & Selection : Peds. 18: 345-57. PMID 15930043 DOI: 10.1093/Protein/Gzi035 |
0.631 |
|
2005 |
McLeish MJ, Kenyon GL. Relating structure to mechanism in creatine kinase. Critical Reviews in Biochemistry and Molecular Biology. 40: 1-20. PMID 15804623 DOI: 10.1080/10409230590918577 |
0.596 |
|
2004 |
Novak WR, Wang PF, McLeish MJ, Kenyon GL, Babbitt PC. Isoleucine 69 and valine 325 form a specificity pocket in human muscle creatine kinase. Biochemistry. 43: 13766-74. PMID 15504039 DOI: 10.1021/Bi049060Y |
0.793 |
|
2004 |
Gopalakrishna KN, Stewart BH, Kneen MM, Andricopulo AD, Kenyon GL, McLeish MJ. Mandelamide hydrolase from Pseudomonas putida: characterization of a new member of the amidase signature family. Biochemistry. 43: 7725-35. PMID 15196015 DOI: 10.1021/Bi049907Q |
0.642 |
|
2003 |
Davioud-Charvet E, McLeish MJ, Veine DM, Giegel D, Arscott LD, Andricopulo AD, Becker K, Müller S, Schirmer RH, Williams CH, Kenyon GL. Mechanism-based inactivation of thioredoxin reductase from Plasmodium falciparum by Mannich bases. Implication for cytotoxicity. Biochemistry. 42: 13319-30. PMID 14609342 DOI: 10.1021/Bi0353629 |
0.637 |
|
2003 |
McLeish MJ, Kneen MM, Gopalakrishna KN, Koo CW, Babbitt PC, Gerlt JA, Kenyon GL. Identification and characterization of a mandelamide hydrolase and an NAD(P)+-dependent benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633. Journal of Bacteriology. 185: 2451-6. PMID 12670968 DOI: 10.1128/Jb.185.8.2451-2456.2003 |
0.736 |
|
2003 |
Polovnikova ES, McLeish MJ, Sergienko EA, Burgner JT, Anderson NL, Bera AK, Jordan F, Kenyon GL, Hasson MS. Structural and kinetic analysis of catalysis by a thiamin diphosphate-dependent enzyme, benzoylformate decarboxylase. Biochemistry. 42: 1820-30. PMID 12590569 DOI: 10.1021/Bi026490K |
0.618 |
|
2002 |
Skillman AG, Maurer KW, Roe DC, Stauber MJ, Eargle D, Ewing TJ, Muscate A, Davioud-Charvet E, Medaglia MV, Fisher RJ, Arnold E, Gao HQ, Buckheit R, Boyer PL, Hughes SH, ... ... Kenyon GL, et al. A novel mechanism for inhibition of HIV-1 reverse transcriptase. Bioorganic Chemistry. 30: 443-58. PMID 12642128 DOI: 10.1016/S0045-2068(02)00502-3 |
0.455 |
|
2002 |
Lahiri SD, Wang PF, Babbitt PC, McLeish MJ, Kenyon GL, Allen KN. The 2.1 A structure of Torpedo californica creatine kinase complexed with the ADP-Mg(2+)-NO(3)(-)-creatine transition-state analogue complex. Biochemistry. 41: 13861-7. PMID 12437342 DOI: 10.1021/Bi026655P |
0.727 |
|
2002 |
Wang PF, Novak WR, Cantwell JS, Babbitt PC, McLeish MJ, Kenyon GL. Expression of Torpedo californica creatine kinase in Escherichia coli and purification from inclusion bodies. Protein Expression and Purification. 26: 89-95. PMID 12356475 DOI: 10.1016/S1046-5928(02)00512-0 |
0.787 |
|
2002 |
Kenyon GL, Gerlt JA. Bioorganic Chemistry: Introduction Bioorganic Chemistry. 30: 1-2. DOI: 10.1006/Bioo.2002.1236 |
0.408 |
|
2001 |
Wang PF, McLeish MJ, Kneen MM, Lee G, Kenyon GL. An unusually low pK(a) for Cys282 in the active site of human muscle creatine kinase. Biochemistry. 40: 11698-705. PMID 11570870 DOI: 10.1021/Bi011208F |
0.628 |
|
2001 |
Cantwell JS, Novak WR, Wang PF, McLeish MJ, Kenyon GL, Babbitt PC. Mutagenesis of two acidic active site residues in human muscle creatine kinase: implications for the catalytic mechanism. Biochemistry. 40: 3056-61. PMID 11258919 DOI: 10.1021/Bi0020980 |
0.795 |
|
2000 |
Sergienko EA, Wang J, Polovnikova L, Hasson MS, McLeish MJ, Kenyon GL, Jordan F. Spectroscopic detection of transient thiamin diphosphate-bound intermediates on benzoylformate decarboxylase. Biochemistry. 39: 13862-9. PMID 11076527 DOI: 10.1021/Bi001214W |
0.602 |
|
2000 |
Chen LH, White CB, Babbitt PC, McLeish MJ, Kenyon GL. A comparative study of human muscle and brain creatine kinases expressed in Escherichia coli. Journal of Protein Chemistry. 19: 59-66. PMID 10882173 DOI: 10.1023/A:1007047026691 |
0.703 |
|
1999 |
Krause SO, Gutheil WG, Simeonov AM, Matsunaga TO, Stauber MJ, Kenyon GL, Mckenna CE. Perspectives on the mechanism of ATP hydrolysis by nitrogenase Phosphorus, Sulfur and Silicon and Related Elements. 144: 513-516. DOI: 10.1080/10426509908546294 |
0.518 |
|
1999 |
Kenyon GL. Structure-function studies on creatine kinase Phosphorus, Sulfur and Silicon and Related Elements. 144: 509-512. DOI: 10.1080/10426509908546293 |
0.31 |
|
1998 |
Hasson MS, Schlichting I, Moulai J, Taylor K, Barrett W, Kenyon GL, Babbitt PC, Gerlt JA, Petsko GA, Ringe D. Evolution of an enzyme active site: the structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolase. Proceedings of the National Academy of Sciences of the United States of America. 95: 10396-401. PMID 9724714 DOI: 10.1073/Pnas.95.18.10396 |
0.719 |
|
1998 |
Hasson MS, Muscate A, McLeish MJ, Polovnikova LS, Gerlt JA, Kenyon GL, Petsko GA, Ringe D. The crystal structure of benzoylformate decarboxylase at 1.6 A resolution: diversity of catalytic residues in thiamin diphosphate-dependent enzymes. Biochemistry. 37: 9918-30. PMID 9665697 DOI: 10.1021/Bi973047E |
0.722 |
|
1998 |
Friedman SH, Ganapathi PS, Rubin Y, Kenyon GL. Optimizing the binding of fullerene inhibitors of the HIV-1 protease through predicted increases in hydrophobic desolvation. Journal of Medicinal Chemistry. 41: 2424-9. PMID 9632374 DOI: 10.1021/Jm970689R |
0.592 |
|
1998 |
Wood TD, Guan Z, Borders CL, Chen LH, Kenyon GL, McLafferty FW. Creatine kinase: essential arginine residues at the nucleotide binding site identified by chemical modification and high-resolution tandem mass spectrometry. Proceedings of the National Academy of Sciences of the United States of America. 95: 3362-5. PMID 9520370 DOI: 10.1073/Pnas.95.7.3362 |
0.325 |
|
1997 |
Selzer PM, Chen X, Chan VJ, Cheng M, Kenyon GL, Kuntz ID, Sakanari JA, Cohen FE, McKerrow JH. Leishmania major: molecular modeling of cysteine proteases and prediction of new nonpeptide inhibitors. Experimental Parasitology. 87: 212-21. PMID 9371086 DOI: 10.1006/Expr.1997.4220 |
0.556 |
|
1997 |
Friedman SH, Kenyon GL. A computational strategy for the design of regiospecific syntheses of fullerene derivatives Journal of the American Chemical Society. 119: 447-448. DOI: 10.1021/Ja963041X |
0.549 |
|
1996 |
Babbitt PC, Hasson MS, Wedekind JE, Palmer DR, Barrett WC, Reed GH, Rayment I, Ringe D, Kenyon GL, Gerlt JA. The enolase superfamily: a general strategy for enzyme-catalyzed abstraction of the alpha-protons of carboxylic acids. Biochemistry. 35: 16489-501. PMID 8987982 DOI: 10.1021/Bi9616413 |
0.723 |
|
1996 |
Li R, Chen X, Gong B, Selzer PM, Li Z, Davidson E, Kurzban G, Miller RE, Nuzum EO, McKerrow JH, Fletterick RJ, Gillmor SA, Craik CS, Kuntz ID, Cohen FE, ... Kenyon GL, et al. Structure-based design of parasitic protease inhibitors. Bioorganic & Medicinal Chemistry. 4: 1421-7. PMID 8894100 DOI: 10.1016/0968-0896(96)00136-8 |
0.568 |
|
1996 |
Chen LH, Borders CL, Vásquez JR, Kenyon GL. Rabbit muscle creatine kinase: consequences of the mutagenesis of conserved histidine residues. Biochemistry. 35: 7895-902. PMID 8672491 DOI: 10.1021/Bi952798I |
0.381 |
|
1996 |
Schafer SL, Barrett WC, Kallarakal AT, Mitra B, Kozarich JW, Gerlt JA, Clifton JG, Petsko GA, Kenyon GL. Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the D270N mutant. Biochemistry. 35: 5662-9. PMID 8639525 DOI: 10.1021/Bi960174M |
0.562 |
|
1996 |
Highbarger LA, Gerlt JA, Kenyon GL. Mechanism of the reaction catalyzed by acetoacetate decarboxylase. Importance of lysine 116 in determining the pKa of active-site lysine 115. Biochemistry. 35: 41-6. PMID 8555196 DOI: 10.1021/Bi9518306 |
0.533 |
|
1996 |
Li R, Muscate A, Kenyon GL. Synthesis, characterization, and inhibitory activities of nucleoside α,β-imido triphosphate analogues on human immunodeficiency virus-1 reverse transcriptase Bioorganic Chemistry. 24: 251-261. DOI: 10.1006/Bioo.1996.0023 |
0.341 |
|
1996 |
Shah VJ, Cerpa R, Kuntz ID, Kenyon GL. Solid-phase synthesis of peptide-derived enantiospecific nucleic acid analogs Bioorganic Chemistry. 24: 201-206. DOI: 10.1006/Bioo.1996.0018 |
0.535 |
|
1996 |
Shah VJ, Kuntz ID, Kenyon GL. Synthesis of amino-acid-derived nucleo(side/tide) analogs for peptide- derived enantiospecific nucleic acid analogs Bioorganic Chemistry. 24: 194-200. DOI: 10.1006/Bioo.1996.0017 |
0.549 |
|
1995 |
Wood TD, Chen LH, White CB, Babbitt PC, Kenyon GL, McLafferty FW. Sequence verification of human creatine kinase (43 kDa) isozymes by high-resolution tandem mass spectrometry. Proceedings of the National Academy of Sciences of the United States of America. 92: 11451-5. PMID 8524781 DOI: 10.1073/Pnas.92.25.11451 |
0.548 |
|
1995 |
Kallarakal AT, Mitra B, Kozarich JW, Gerlt JA, Clifton JG, Petsko GA, Kenyon GL. Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the K166R mutant. Biochemistry. 34: 2788-97. PMID 7893690 |
0.533 |
|
1995 |
Mitra B, Kallarakal AT, Kozarich JW, Gerlt JA, Clifton JG, Petsko GA, Kenyon GL. Mechanism of the reaction catalyzed by mandelate racemase: importance of electrophilic catalysis by glutamic acid 317. Biochemistry. 34: 2777-87. PMID 7893689 DOI: 10.1021/Bi00009A006 |
0.595 |
|
1995 |
Babbitt PC, Mrachko GT, Hasson MS, Huisman GW, Kolter R, Ringe D, Petsko GA, Kenyon GL, Gerlt JA. A functionally diverse enzyme superfamily that abstracts the alpha protons of carboxylic acids. Science (New York, N.Y.). 267: 1159-61. PMID 7855594 DOI: 10.1126/Science.7855594 |
0.724 |
|
1995 |
White CB, Chen Q, Kenyon GL, Babbitt PC. A novel activity of OmpT. Proteolysis under extreme denaturing conditions. The Journal of Biological Chemistry. 270: 12990-4. PMID 7768890 DOI: 10.1074/Jbc.270.22.12990 |
0.623 |
|
1995 |
Li R, Powers VM, Kozarich JW, Kenyon GL. Racemization of vinylglycolate catalyzed by mandelate racemase Journal of Organic Chemistry. 60: 3347-3351. DOI: 10.1021/Jo00116A017 |
0.336 |
|
1995 |
Ganapathi PS, Friedman SH, Kenyon GL, Rubin Y. Sequential "double-Michael" additions of dienolates with C60: Rapid access to sterically congested buckminsterfullerene derivatives with defined stereochemistry The Journal of Organic Chemistry. 60: 2954-2955. DOI: 10.1021/Jo00115A002 |
0.533 |
|
1995 |
Watts CR, Kerwin SM, Kenyon GL, Kuntz ID, Kallick DA. Rationally designed N,N′-bis[(N-p-guanidinobenzyl-N-methyl)aminocarbonyl]-1,3-diaminobenzene, "BIGBEN", binds to the minor groove of d(CGCGAATTCGCG)2 as determined by two-dimensional nuclear magnetic resonance spectroscopy Journal of the American Chemical Society. 117: 9941-9950. DOI: 10.1021/Ja00145A002 |
0.714 |
|
1995 |
Kenyon GL, Gerlt JA, Petsko GA, Kozarich JW. Mandelate Racemase: Structure-Function Studies of a Pseudosymmetric Enzyme Accounts of Chemical Research. 28: 178-186. DOI: 10.1021/Ar00052A003 |
0.563 |
|
1994 |
Gibson BW, Medzihradszky D, Hines WM, Auriola S, Kenyon GL. Mass spectrometric characterization of a series of adenosylated peptides acting as bisubstrate analogs of protein kinases. Journal of the American Society For Mass Spectrometry. 5: 443-51. PMID 24222599 DOI: 10.1016/1044-0305(94)85060-7 |
0.3 |
|
1994 |
Li Z, Chen X, Davidson E, Zwang O, Mendis C, Ring CS, Roush WR, Fegley G, Li R, Rosenthal PJ, Lee GK, Kenyon GL, Kuntz ID, Cohen FE. Anti-malarial drug development using models of enzyme structure Chemistry and Biology. 1: 31-37. PMID 9383368 DOI: 10.1016/1074-5521(94)90038-8 |
0.546 |
|
1994 |
Landro JA, Gerlt JA, Kozarich JW, Koo CW, Shah VJ, Kenyon GL, Neidhart DJ, Fujita S, Petsko GA. The role of lysine 166 in the mechanism of mandelate racemase from Pseudomonas putida: mechanistic and crystallographic evidence for stereospecific alkylation by (R)-alpha-phenylglycidate. Biochemistry. 33: 635-43. PMID 8292591 DOI: 10.1021/Bi00169A003 |
0.531 |
|
1993 |
Mujeeb A, Kerwin SM, Kenyon GL, James TL. Solution structure of a conserved DNA sequence from the HIV-1 genome: restrained molecular dynamics simulation with distance and torsion angle restraints derived from two-dimensional NMR spectra. Biochemistry. 32: 13419-31. PMID 8257678 DOI: 10.1021/Bi00212A007 |
0.565 |
|
1993 |
Petsko GA, Kenyon GL, Gerlt JA, Ringe D, Kozarich JW. On the origin of enzymatic species. Trends in Biochemical Sciences. 18: 372-6. PMID 8256284 DOI: 10.1016/0968-0004(93)90091-Z |
0.572 |
|
1993 |
Mitra B, Gerlt JA, Babbitt PC, Koo CW, Kenyon GL, Joseph D, Petsko GA. A novel structural basis for membrane association of a protein: construction of a chimeric soluble mutant of (S)-mandelate dehydrogenase from Pseudomonas putida. Biochemistry. 32: 12959-67. PMID 8241149 DOI: 10.1021/Bi00211A003 |
0.672 |
|
1993 |
Petsko G, Ringe D, Allen K, Lavie A, Gerhart-Mueller E, Clifton J, Hasson M, Fujita S, Sugio S, Xhang X, Davenport R, Lolis E, Neidhart D, Kenyon G, Gerlt J, et al. The structural enzymology of proton-transfer reactions Protein Engineering, Design and Selection. 6: 37. DOI: 10.1093/Protein/6.Supplement.37-A |
0.576 |
|
1993 |
Sijbesma R, Srdanov G, Wudl F, Castoro JA, Wilkins C, Friedman SH, DeCamp DL, Kenyon GL. Synthesis of a fullerene derivative for the inhibition of HIV enzymes Journal of the American Chemical Society. 115: 6510-6512. DOI: 10.1021/Ja00068A006 |
0.596 |
|
1993 |
Friedman SH, Decamp DL, Sijbesma RP, Srdanov G, Wudl F, Kenyon GL. Inhibition of the HIV-1 protease by fullerene derivatives: Model building studies and experimental verification Journal of the American Chemical Society. 115: 6506-6509. DOI: 10.1021/Ja00068A005 |
0.599 |
|
1993 |
Sijbesma R, Srdanov G, Wudl F, Castoro JA, Wilkins C, Friedman SH, Decamp DL, Kenyon GL. Synthesis of a fullerene derivative for the Inhibition of HIV enzymes Journal of the American Chemical Society. 115: 6510-6512. |
0.56 |
|
1992 |
White KC, Babbitt PC, Buechter DD, Kenyon GL. The principal islet of the Coho salmon (Oncorhyncus kisutch) contains the BB isoenzyme of creatine kinase. Journal of Protein Chemistry. 11: 489-94. PMID 1449598 DOI: 10.1007/Bf01025026 |
0.598 |
|
1992 |
Babbitt PC, Kenyon GL, Martin BM, Charest H, Slyvestre M, Scholten JD, Chang KH, Liang PH, Dunaway-Mariano D. Ancestry of the 4-chlorobenzoate dehalogenase: analysis of amino acid sequence identities among families of acyl:adenyl ligases, enoyl-CoA hydratases/isomerases, and acyl-CoA thioesterases. Biochemistry. 31: 5594-604. PMID 1351742 DOI: 10.1021/Bi00139A024 |
0.586 |
|
1992 |
Chen LH, Kenyon GL, Curtin F, Harayama S, Bembenek ME, Hajipour G, Whitman CP. 4-Oxalocrotonate tautomerase, an enzyme composed of 62 amino acid residues per monomer. The Journal of Biological Chemistry. 267: 17716-21. PMID 1339435 |
0.614 |
|
1992 |
Mujeeb A, Kerwin SM, Egan W, Kenyon GL, James TL. A potential gene target in HIV-1: rationale, selection of a conserved sequence, and determination of NMR distance and torsion angle constraints. Biochemistry. 31: 9325-38. PMID 1327112 DOI: 10.1021/Bi00154A002 |
0.524 |
|
1992 |
Gerlt JA, Kozarich JW, Kenyon GL, Gassman PG. Electrophilic catalysis can explain the unexpected acidity of carbon acids in enzyme-catalyzed reactions. [Erratum to document cited in CA115(25):274439b] Journal of the American Chemical Society. 114: 4016-4016. DOI: 10.1021/Ja00036A083 |
0.553 |
|
1992 |
Landro JA, Kenyon GL, Kozarich JW. Mechanism-based inactivation of mandelate racemase by propargylglycolate Bioorganic and Medicinal Chemistry Letters. 2: 1411-1418. DOI: 10.1016/S0960-894X(00)80523-5 |
0.385 |
|
1992 |
Gerlt JA, Kenyon GL, Kozarich JW, Neidhart DJ, Petsko GA, Powers VM. Mandelate racemase and class-related enzymes Current Opinion in Structural Biology. 2: 736-742. DOI: 10.1016/0959-440X(92)90209-P |
0.569 |
|
1991 |
Landro JA, Kallarakal AT, Ransom SC, Gerlt JA, Kozarich JW, Neidhart DJ, Kenyon GL. Mechanism of the reaction catalyzed by mandelate racemase. 3. Asymmetry in reactions catalyzed by the H297N mutant. Biochemistry. 30: 9274-81. PMID 1909893 DOI: 10.1021/Bi00102A020 |
0.57 |
|
1991 |
Neidhart DJ, Howell PL, Petsko GA, Powers VM, Li RS, Kenyon GL, Gerlt JA. Mechanism of the reaction catalyzed by mandelate racemase. 2. Crystal structure of mandelate racemase at 2.5-A resolution: identification of the active site and possible catalytic residues. Biochemistry. 30: 9264-73. PMID 1892834 DOI: 10.1021/Bi00102A019 |
0.552 |
|
1991 |
Powers VM, Koo CW, Kenyon GL, Gerlt JA, Kozarich JW. Mechanism of the reaction catalyzed by mandelate racemase. 1. Chemical and kinetic evidence for a two-base mechanism. Biochemistry. 30: 9255-63. PMID 1892833 DOI: 10.1021/Bi00102A018 |
0.532 |
|
1991 |
Gerlt JA, Kozarich JW, Kenyon GL, Gassman PG. Electrophilic catalysis can explain the unexpected acidity of carbon acids in enzyme-catalyzed reactions Journal of the American Chemical Society. 113: 9667-9669. DOI: 10.1021/Ja00025A039 |
0.568 |
|
1990 |
Ma QF, Kenyon GL, Markham GD. Specificity of S-adenosylmethionine synthetase for ATP analogues mono- and disubstituted in bridging positions of the polyphosphate chain. Biochemistry. 29: 1412-6. PMID 2334705 DOI: 10.1021/Bi00458A011 |
0.353 |
|
1990 |
Tsou AY, Ransom SC, Gerlt JA, Buechter DD, Babbitt PC, Kenyon GL. Mandelate pathway of Pseudomonas putida: sequence relationships involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli. Biochemistry. 29: 9856-62. PMID 2271624 DOI: 10.1021/Bi00494A015 |
0.682 |
|
1990 |
Neidhart DJ, Kenyon GL, Gerlt JA, Petsko GA. Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologous. Nature. 347: 692-4. PMID 2215699 DOI: 10.1038/347692A0 |
0.594 |
|
1990 |
Neidhart DC, Howell PL, Petsko GA, Gerlt JA, Kozarich JW, Powers VM, Kenyon GL. Restructuring catalysis in the mandelate pathway. Biochemical Society Symposium. 57: 135-41. PMID 2099737 |
0.545 |
|
1990 |
Rowley GL, Ma QF, Bathurst IC, Barr PJ, Kenyon GL. Stabilization and activation of recombinant human immunodeficiency virus-1 reverse transcriptase-P66. Biochemical and Biophysical Research Communications. 167: 673-9. PMID 1690991 DOI: 10.1016/0006-291X(90)92078-E |
0.369 |
|
1990 |
Babbitt PC, West BL, Buechter DD, Kuntz ID, Kenyon GL. Removal of a proteolytic activity associated with aggregates formed from expression of creatine kinase in Escherichia coli leads to improved recovery of active enzyme. Bio/Technology (Nature Publishing Company). 8: 945-9. PMID 1370005 DOI: 10.1038/Nbt1090-945 |
0.695 |
|
1989 |
Mejillano MR, Jahansouz H, Matsunaga TO, Kenyon GL, Himes RH. Formation and utilization of formyl phosphate by N10-formyltetrahydrofolate synthetase: evidence for formyl phosphate as an intermediate in the reaction. Biochemistry. 28: 5136-45. PMID 2548602 DOI: 10.1021/Bi00438A034 |
0.417 |
|
1989 |
Tsou AY, Ransom SC, Gerlt JA, Powers VM, Kenyon GL. Selection and characterization of a mutant of the cloned gene for mandelate racemase that confers resistance to an affinity label by greatly enhanced production of enzyme. Biochemistry. 28: 969-75. PMID 2496759 DOI: 10.1021/Bi00429A008 |
0.548 |
|
1989 |
McKenna CE, Gutheil WG, Kenyon GL, Matsunaga TO. Mass spectrometric analysis of phosphate from β,γ-[18O]ATP hydrolyzed by Azotobacter vinelandii nitrogenase: Direct evidence for PγOPβ bond cleavage Bioorganic Chemistry. 17: 377-384. DOI: 10.1016/0045-2068(89)90039-4 |
0.534 |
|
1989 |
Ma QF, Reynolds MA, Kenyon GL. Syntheses and characterizations of adenosine 5′-(α,β-N-methylimido)di and triphosphates and adenosine 5′-(β,γ-N-methylimido)triphosphate-Comparisons with their nonmethylated analogs Bioorganic Chemistry. 17: 194-206. DOI: 10.1016/0045-2068(89)90019-9 |
0.326 |
|
1988 |
Reynolds LJ, Garcia GA, Kozarich JW, Kenyon GL. Differential reactivity in the processing of [p-(halomethyl)benzoyl] formates by benzoylformate decarboxylase, a thiamin pyrophosphate dependent enzyme. Biochemistry. 27: 5530-8. PMID 3179267 DOI: 10.1021/Bi00415A022 |
0.369 |
|
1988 |
Neidhart DJ, Powers VM, Kenyon GL, Tsou AY, Ransom SC, Gerlt JA, Petsko GA. Preliminary x-ray data on crystals of mandelate racemase. The Journal of Biological Chemistry. 263: 9268-70. PMID 3132459 |
0.442 |
|
1988 |
Ransom SC, Gerlt JA, Powers VM, Kenyon GL. Cloning, DNA sequence analysis, and expression in Escherichia coli of the gene for mandelate racemase from Pseudomonas putida. Biochemistry. 27: 540-5. PMID 2831968 DOI: 10.1021/Bi00402A006 |
0.545 |
|
1988 |
Ma QF, Babbitt PC, Kenyon GL. Adenosine 5'-[.alpha.,.beta.-imido]triphosphate, a substrate for T7 RNA polymerase and rabbit muscle creatine kinase [Erratum to document cited in CA109(1):6886j] Journal of the American Chemical Society. 110: 8267-8267. DOI: 10.1021/Ja00232A068 |
0.567 |
|
1988 |
Ma QF, Babbitt PC, Kenyon GL. Adenosine 5'-[.alpha.,.beta.-imido]triphosphate, a substrate for T7 RNA polymerase and rabbit muscle creatine kinase Journal of the American Chemical Society. 110: 4060-4061. DOI: 10.1021/Ja00220A068 |
0.569 |
|
1988 |
Lin DT, Powers VM, Reynolds LJ, Whitman CP, Kozarich JW, Kenyon GL. Evidence for the generation of .alpha.-carboxy-.alpha.-hydroxy-p-xylylene from p-(bromomethyl)mandelate by mandelate racemase Journal of the American Chemical Society. 110: 323-324. DOI: 10.1021/Ja00209A069 |
0.544 |
|
1988 |
MA Q, BABBITT PC, KENYON GL. ChemInform Abstract: Adenosine 5′-(α,β-Imido)triphosphate, a Substrate for T7 RNA Polymerase and Rabbit Muscle Creatine Kinase. Cheminform. 19. DOI: 10.1002/chin.198839305 |
0.524 |
|
1988 |
Lin DT, Powers VM, Reynolds LJ, Whitman CP, Kozarich JW, Kenyon GL. Evidence for the generation of α-carboxy-α-hydroxy-p-xylylene from p-(bromomethyl)mandelate by mandelate racemase Journal of the American Chemical Society. 110: 323-324. |
0.493 |
|
1987 |
Rosevear PR, Powers VM, Dowhan D, Mildvan AS, Kenyon GL. Nuclear overhauser effect studies on the conformation of magnesium adenosine 5'-triphosphate bound to rabbit muscle creatine kinase. Biochemistry. 26: 5338-44. PMID 3499934 DOI: 10.1021/Bi00391A018 |
0.34 |
|
1987 |
Beilan HS, Browne DT, Kenyon GL. Synthesis of cystine-3,3′-13C-3,3,3′,3′-d4 for use in incorporation into proteins Bioorganic Chemistry. 15: 109-114. DOI: 10.1016/0045-2068(87)90012-5 |
0.693 |
|
1986 |
Babbitt PC, Kenyon GL, Kuntz ID, Cohen FE, Baxter JD, Benfield PA, Buskin JD, Gilbert WA, Hauschka SD, Hossle JP, Ordahl CP, Pearson ML, Perriard JC, Pickering LA, Putney SD, et al. Comparisons of creatine kinase primary structures Journal of Protein Chemistry. 5: 1-14. DOI: 10.1007/Bf01025580 |
0.683 |
|
1985 |
Whitman CP, Hegeman GD, Cleland WW, Kenyon GL. Symmetry and asymmetry in mandelate racemase catalysis. Biochemistry. 24: 3936-42. PMID 2996586 DOI: 10.1021/Bi00336A020 |
0.555 |
|
1985 |
Leyh TS, Goodhart PJ, Nguyen AC, Kenyon GL, Reed GH. Structures of manganese(II) complexes with ATP, ADP, and phosphocreatine in the reactive central complexes with creatine kinase: electron paramagnetic resonance studies with oxygen-17-labeled ligands. Biochemistry. 24: 308-16. PMID 2983754 DOI: 10.1021/Bi00323A011 |
0.346 |
|
1985 |
Whitman CP, Craig JC, Kenyon GL. Synthesis, chiroptical properties and absolute configuration of α-phenylglycidic acid Tetrahedron. 41: 1183-1192. DOI: 10.1016/S0040-4020(01)96519-6 |
0.595 |
|
1985 |
Bruice TW, Kenyon GL. Alkyl alkanethiolsulfonate sulfhydryl reagents: β-Sulfhydryl-modified derivatives of l-cysteine as substrates for trypsin and α-chymotrypsin Bioorganic Chemistry. 13: 77-87. DOI: 10.1016/0045-2068(85)90010-0 |
0.38 |
|
1984 |
Dietrich RF, Kenyon GL. Synthesis and investigation with creatine kinase of trans-2-imino-1,3-diazabicyclo[3.3.0]octane-8-carboxylic acid, a bicyclic analog of creatine Bioorganic Chemistry. 12: 221-228. DOI: 10.1016/0045-2068(84)90005-1 |
0.345 |
|
1984 |
REYNOLDS MA, GERLT JA, DEMOU PC, OPPENHEIMER NJ, KENYON GL. ChemInform Abstract: NITROGEN-15 AND OXYGEN-17 NMR STUDIES OF THE PROTON BINDING SITES IN IMIDODIPHOSPHATE, TETRAETHYL IMIDODIPHOSPHATE, AND ADENYLYL IMIDODIPHOSPHATE Chemischer Informationsdienst. 15. DOI: 10.1002/chin.198404050 |
0.449 |
|
1984 |
GERLT JA, REYNOLDS MA, DEMOU PC, KENYON GL. ChemInform Abstract: OXYGEN-17 NMR SPECTRAL PROPERTIES OF PYROPHOSPHATE, SIMPLE PHOSPHONATES, AND THIOPHOSPHATE AND PHOSPHONATE ANALOGUES OF ATP Chemischer Informationsdienst. 15. DOI: 10.1002/chin.198404049 |
0.453 |
|
1984 |
Whitman CP, Kenyon GL, Hegeman GD. Affinity labeling of mandelate racemase by S(+)-α-phenylglycidate Federation Proceedings. 43: no. 3435. |
0.497 |
|
1983 |
Beilan HS, Kenyon GL, Browne DT. Incorporation of specifically labeled cysteine into Escherichia coli protein. Analytical Biochemistry. 128: 169-74. PMID 6342463 DOI: 10.1016/0003-2697(83)90358-5 |
0.721 |
|
1983 |
Kenyon GL, Reed GH. Creatine kinase: structure-activity relationships. Advances in Enzymology and Related Areas of Molecular Biology. 54: 367-426. PMID 6342340 DOI: 10.1002/9780470122990.Ch6 |
0.303 |
|
1983 |
Kenyon GL. Enzyme catalysis and regulation Trends in Biochemical Sciences. 8: 345-346. DOI: 10.1016/0968-0004(83)90122-6 |
0.349 |
|
1983 |
Reynolds MA, Gerlt JA, Demou PC, Oppenheimer NJ, Kenyon GL. Nitrogen-15 and oxygen-17 NMR studies of the proton binding sites in imidodiphosphate, tetraethyl imidodiphosphate, and adenylyl imidodiphosphate Journal of the American Chemical Society. 105: 6475-6481. DOI: 10.1002/Chin.198404050 |
0.506 |
|
1983 |
Gerlt JA, Reynolds MA, Demou PC, Kenyon GL. Oxygen-17 NMR spectral properties of pyrophosphate, simple phosphonates, and thiophosphate and phosphonate analogues of ATP Journal of the American Chemical Society. 105: 6469-6475. DOI: 10.1002/Chin.198404049 |
0.509 |
|
1982 |
Mentzer WC, Lewis S, Pennathur-Das R, Halpin RA, Cerrone KL, Lubin B, Kenyon GL. Formation of 5-carbomethoxyvaleramidine during hydrolysis of the protein cross-linking agent dimethyl adipimidate Journal of Protein Chemistry. 1: 141-155. DOI: 10.1007/Bf01025636 |
0.3 |
|
1981 |
Rosevear PR, Desmeules P, Kenyon GL, Mildvan AS. Nuclear magnetic resonance studies of the role of histidine residues at the active site of rabbit muscle creatine kinase. Biochemistry. 20: 6155-64. PMID 7306503 DOI: 10.1021/Bi00524A038 |
0.313 |
|
1980 |
Dietrich RF, Miller RB, Kenyon GL, Leyh TS, Reed GH. Conformationally restricted creatine analogues and substrate specificity of rabbit muscle creatine kinase. Biochemistry. 19: 3180-6. PMID 6250555 DOI: 10.1021/Bi00555A011 |
0.323 |
|
1980 |
Marsh FJ, Weiner P, Douglas JE, Kollman PA, Kenyon GL, Gerlt JA. Theoretical calculations on the geometric destabilization of 3′,5′- and 2′,3′-cyclic nucleotides Journal of the American Chemical Society. 102: 1660-1665. DOI: 10.1021/Ja00525A034 |
0.492 |
|
1980 |
Dietrich RF, Marletta MA, Kenyon GL. Carbon-13 nuclear magnetic resonance studies of creatine, creatinine and some of their analogs Organic Magnetic Resonance. 13: 79-88. DOI: 10.1002/Mrc.1270130202 |
0.517 |
|
1980 |
MARSH FJ, WEINER P, DOUGLAS JE, KOLLMANN PA, KENYON GL, GERLT JA. ChemInform Abstract: THEORETICAL CALCULATIONS OF HYDROLYSIS ENERGIES OF “HIGH-ENERGY” MOLECULES. 3. HEORETICAL CALCULATIONS ON THE GEOMETRIC DESTABILIZATION OF 3′,5′- A D 2′,3′-CYCLIC NUCLEOTIDES Chemischer Informationsdienst. 11. DOI: 10.1002/chin.198023068 |
0.432 |
|
1979 |
Marletta MA, Kenyon GL. Affinity labeling of creatine kinase by N-(2,3-epoxypropyl)-N-amidinoglycine. The Journal of Biological Chemistry. 254: 1879-86. PMID 422560 |
0.44 |
|
1977 |
Kenyon GL, Hegeman GD. [62] Mandelate racemase Methods in Enzymology. 46: 541-548. PMID 909443 DOI: 10.1016/S0076-6879(77)46066-X |
0.401 |
|
1977 |
Sharp TR, Hegeman GD, Kenyon GL. Mandelate racemase from Pseudomonas putida. Absence of detectable intermolecular proton transfer accompanying racemization Biochemistry. 16: 1123-1128. DOI: 10.1021/Bi00625A015 |
0.3 |
|
1975 |
Nishimura JS, Kenyon GL, Smith DJ. Reversible modification of the sulfhydryl groups of Escherichia coli succinic thiokinase with methanethiolating reagents, 5,5′-dithio-bis(2-nitrobenzoic acid), p-hydroxymercuribenzoate, and ethylmercurithiosalicylate Archives of Biochemistry and Biophysics. 170: 461-467. PMID 1103736 DOI: 10.1016/0003-9861(75)90141-1 |
0.403 |
|
1975 |
Maggio ET, Kenyon GL, Mildvan AS, Hegeman GD. Mandelate racemase from Pseudomonas putida. Magnetic resonance and kinetic studies of the mechanism of catalysis Biochemistry. 14: 1131-1139. PMID 164210 DOI: 10.1021/Bi00677A006 |
0.359 |
|
1975 |
Smith DJ, Maggio ET, Kenyon GL. Simple alkanethiol groups for temporary blocking of sulfhydryl groups of enzymes Biochemistry. 14: 766-771. PMID 163643 DOI: 10.1021/Bi00675A019 |
0.364 |
|
1974 |
Fee JA, Hegeman GD, Kenyon GL. Mandelate racemase from Pseudomonas putida. Affinity labeling of the enzyme by D,L-α-phenylglycidate in the presence of magnesium ion Biochemistry. 13: 2533-2538. PMID 4831902 DOI: 10.1021/Bi00709A009 |
0.301 |
|
1973 |
Browne DT, Kenyon GL, Packer EL, Sternlicht H, Wilson DM. Studies of macromolecular structure by 13 C nuclear magnetic resonance. II. A specific labeling approach to the study of histidine residues in proteins. Journal of the American Chemical Society. 95: 1316-23. PMID 4569190 DOI: 10.1021/Ja00785A050 |
0.695 |
|
1973 |
Browne DT, Kenyon GL, Packer EL, Wilson DM, Sternlicht H. A study of the dynamic state of histidine residues in tryptophan synthetase subunit by 13 C nuclear magnetic resonance. Biochemical and Biophysical Research Communications. 50: 42-7. PMID 4567085 DOI: 10.1016/0006-291X(73)91060-7 |
0.672 |
|
1972 |
Stubbe JA, Kenyon GL. Analogs of phosphoenolpyruvate. Substrate specificities of enolase and pyruvate kinase from rabbit muscle. Biochemistry. 11: 338-45. PMID 5062057 DOI: 10.1021/Bi00753A005 |
0.524 |
|
1971 |
Stubbe JA, Kenyon GL. Analogs of phosphoenolpyruvate. On the specificity of pyruvate kinase from rabbit muscle. Biochemistry. 10: 2669-77. PMID 5105182 DOI: 10.1021/Bi00790A003 |
0.498 |
|
1970 |
Hegeman GD, Rosenberg EY, Kenyon GL. Mandelic acid racemase from Pseudomonas putida. Purification and properties of the enzyme Biochemistry. 9: 4029-4036. PMID 4989844 DOI: 10.1021/Bi00823A001 |
0.364 |
|
1970 |
Browne DT, Kenyon GL, Hegeman GD. Incorporation of monofluorotryptophans into protein during the growth of Escherichia coli Biochemical and Biophysical Research Communications. 39: 13-19. PMID 4910032 DOI: 10.1016/0006-291X(70)90750-3 |
0.657 |
|
1966 |
Kenyon GL, Westheimer FH. The stereochemical course of the fragmentation of β-halophosphonates Journal of the American Chemical Society. 88: 3561-3565. DOI: 10.1021/Ja00967A017 |
0.487 |
|
1966 |
Kenyon GL, Westheimer FH. The stereochemistry of unsaturated phosphonic acids Journal of the American Chemical Society. 88: 3557-3561. DOI: 10.1021/Ja00967A016 |
0.528 |
|
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