| Year |
Citation |
Score |
| 2017 |
Terzyan SS, Cook PF, Heroux A, Hanigan MH. Structure of 6-Diazo-5-Oxo-Norleucine-Bound Human Gamma-Glutamyl Transpeptidase 1, a Novel Mechanism of Inactivation. Protein Science : a Publication of the Protein Society. PMID 28378915 DOI: 10.1002/Pro.3172 |
0.47 |
|
| 2015 |
Vashishtha AK, West AH, Cook PF. Probing the chemical mechanism of saccharopine reductase from Saccharomyces cerevisiae using site-directed mutagenesis. Archives of Biochemistry and Biophysics. 584: 98-106. PMID 26342457 DOI: 10.1016/J.Abb.2015.08.023 |
0.85 |
|
| 2015 |
Hsu C, West AH, Cook PF. Evidence for an induced conformational change in the catalytic mechanism of homoisocitrate dehydrogenase for Saccharomyces cerevisiae: Characterization of the D271N mutant enzyme. Archives of Biochemistry and Biophysics. 584: 20-7. PMID 26325079 DOI: 10.1016/J.Abb.2015.08.016 |
0.533 |
|
| 2013 |
Nalabolu SR, Tai CH, Schnackerz KD, Cook PF. Mechanism of O-acetylserine sulfhydrylase fromSalmonella typhimurium LT-2. Amino Acids. 2: 119-25. PMID 24194279 DOI: 10.1007/Bf00806082 |
0.574 |
|
| 2013 |
Spyrakis F, Singh R, Cozzini P, Campanini B, Salsi E, Felici P, Raboni S, Benedetti P, Cruciani G, Kellogg GE, Cook PF, Mozzarelli A. Isozyme-specific ligands for O-acetylserine sulfhydrylase, a novel antibiotic target. Plos One. 8: e77558. PMID 24167577 DOI: 10.1371/Journal.Pone.0077558 |
0.332 |
|
| 2013 |
Wickham S, Regan N, West MB, Thai J, Cook PF, Terzyan SS, Li PK, Hanigan MH. Inhibition of human γ-glutamyl transpeptidase: development of more potent, physiologically relevant, uncompetitive inhibitors. The Biochemical Journal. 450: 547-57. PMID 23301618 DOI: 10.1042/Bj20121435 |
0.351 |
|
| 2013 |
Spyrakis F, Felici P, Bayden AS, Salsi E, Miggiano R, Kellogg GE, Cozzini P, Cook PF, Mozzarelli A, Campanini B. Fine tuning of the active site modulates specificity in the interaction of O-acetylserine sulfhydrylase isozymes with serine acetyltransferase. Biochimica Et Biophysica Acta. 1834: 169-81. PMID 23000429 DOI: 10.1016/J.Bbapap.2012.09.009 |
0.415 |
|
| 2012 |
Kumar VP, West AH, Cook PF. Supporting role of lysine 13 and glutamate 16 in the acid-base mechanism of saccharopine dehydrogenase from Saccharomyces cerevisiae. Archives of Biochemistry and Biophysics. 522: 57-61. PMID 22521736 DOI: 10.1016/J.Abb.2012.03.027 |
0.475 |
|
| 2012 |
Kumar VP, Thomas LM, Bobyk KD, Andi B, Cook PF, West AH. Evidence in support of lysine 77 and histidine 96 as acid-base catalytic residues in saccharopine dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 51: 857-66. PMID 22243403 DOI: 10.1021/Bi201808U |
0.825 |
|
| 2012 |
Wickham S, Regan N, West MB, Kumar VP, Thai J, Li PK, Cook PF, Hanigan MH. Divergent effects of compounds on the hydrolysis and transpeptidation reactions of γ-glutamyl transpeptidase. Journal of Enzyme Inhibition and Medicinal Chemistry. 27: 476-89. PMID 21864033 DOI: 10.3109/14756366.2011.597748 |
0.397 |
|
| 2012 |
Hanigan MH, Wickham S, Reagan N, West MB, Thai J, Cook PF, Li PK. Abstract 818: Targeting the redox-adaptive response in tumors to potentiate cancer therapy Cancer Research. 72: 818-818. DOI: 10.1158/1538-7445.Am2012-818 |
0.315 |
|
| 2011 |
Karsten WE, Reyes ZL, Bobyk KD, Cook PF, Chooback L. Mechanism of the aromatic aminotransferase encoded by the Aro8 gene from Saccharomyces cerevisiae. Archives of Biochemistry and Biophysics. 516: 67-74. PMID 21982920 DOI: 10.1016/J.Abb.2011.09.008 |
0.813 |
|
| 2011 |
Ekanayake DK, West AH, Cook PF. Contribution of K99 and D319 to substrate binding and catalysis in the saccharopine dehydrogenase reaction. Archives of Biochemistry and Biophysics. 514: 8-15. PMID 21819960 DOI: 10.1016/J.Abb.2011.07.013 |
0.828 |
|
| 2011 |
Bobyk KD, Kim SG, Kumar VP, Kim SK, West AH, Cook PF. The oxidation state of active site thiols determines activity of saccharopine dehydrogenase at low pH. Archives of Biochemistry and Biophysics. 513: 71-80. PMID 21798231 DOI: 10.1016/J.Abb.2011.07.009 |
0.843 |
|
| 2011 |
Kumar VP, West AH, Cook PF. Kinetic and chemical mechanisms of homocitrate synthase from Thermus thermophilus. The Journal of Biological Chemistry. 286: 29428-39. PMID 21733842 DOI: 10.1074/Jbc.M111.246355 |
0.472 |
|
| 2011 |
Mozzarelli A, Bettati S, Campanini B, Salsi E, Raboni S, Singh R, Spyrakis F, Kumar VP, Cook PF. The multifaceted pyridoxal 5'-phosphate-dependent O-acetylserine sulfhydrylase. Biochimica Et Biophysica Acta. 1814: 1497-510. PMID 21549222 DOI: 10.1016/J.Bbapap.2011.04.011 |
0.478 |
|
| 2011 |
Foley JH, Cook PF, Nesheim ME. Kinetics of activated thrombin-activatable fibrinolysis inhibitor (TAFIa)-catalyzed cleavage of C-terminal lysine residues of fibrin degradation products and removal of plasminogen-binding sites. The Journal of Biological Chemistry. 286: 19280-6. PMID 21467042 DOI: 10.1074/Jbc.M110.215061 |
0.465 |
|
| 2011 |
Wickham S, West MB, Cook PF, Hanigan MH. Gamma-glutamyl compounds: substrate specificity of gamma-glutamyl transpeptidase enzymes. Analytical Biochemistry. 414: 208-14. PMID 21447318 DOI: 10.1016/J.Ab.2011.03.026 |
0.397 |
|
| 2011 |
Schnackerz KD, Andi B, Cook PF. (31)P NMR spectroscopy senses the microenvironment of the 5'-phosphate group of enzyme-bound pyridoxal 5'-phosphate. Biochimica Et Biophysica Acta. 1814: 1447-58. PMID 21354475 DOI: 10.1016/J.Bbapap.2011.02.001 |
0.782 |
|
| 2011 |
Tyapochkin E, Kumar VP, Cook PF, Chen G. Reaction product affinity regulates activation of human sulfotransferase 1A1 PAP sulfation. Archives of Biochemistry and Biophysics. 506: 137-41. PMID 21111704 DOI: 10.1016/J.Abb.2010.11.018 |
0.425 |
|
| 2011 |
Salsi E, Guan R, Campanini B, Bettati S, Lin J, Cook PF, Mozzarelli A. Exploring O-acetylserine sulfhydrylase-B isoenzyme from Salmonella typhimurium by fluorescence spectroscopy. Archives of Biochemistry and Biophysics. 505: 178-85. PMID 20937239 DOI: 10.1016/J.Abb.2010.10.005 |
0.737 |
|
| 2010 |
Kaserer AO, Andi B, Cook PF, West AH. Kinetic studies of the yeast His-Asp phosphorelay signaling pathway. Methods in Enzymology. 471: 59-75. PMID 20946842 DOI: 10.1016/S0076-6879(10)71004-1 |
0.707 |
|
| 2010 |
Tian H, Guan R, Salsi E, Campanini B, Bettati S, Kumar VP, Karsten WE, Mozzarelli A, Cook PF. Identification of the structural determinants for the stability of substrate and aminoacrylate external Schiff bases in O-acetylserine sulfhydrylase-A. Biochemistry. 49: 6093-103. PMID 20550197 DOI: 10.1021/Bi100473V |
0.804 |
|
| 2010 |
Ekanayake DK, Andi B, Bobyk KD, West AH, Cook PF. Glutamates 78 and 122 in the active site of saccharopine dehydrogenase contribute to reactant binding and modulate the basicity of the acid-base catalysts. The Journal of Biological Chemistry. 285: 20756-68. PMID 20427272 DOI: 10.1074/Jbc.M110.119826 |
0.822 |
|
| 2010 |
Salsi E, Campanini B, Bettati S, Raboni S, Roderick SL, Cook PF, Mozzarelli A. A two-step process controls the formation of the bienzyme cysteine synthase complex. The Journal of Biological Chemistry. 285: 12813-22. PMID 20164178 DOI: 10.1074/Jbc.M109.075762 |
0.473 |
|
| 2010 |
Knuckley B, Causey CP, Pellechia PJ, Cook PF, Thompson PR. Haloacetamidine-based inactivators of protein arginine deiminase 4 (PAD4): Evidence that general acid catalysis promotes efficient inactivation Chembiochem. 11: 161-165. PMID 20014086 DOI: 10.1002/Cbic.200900698 |
0.462 |
|
| 2010 |
Salsi E, Bayden AS, Spyrakis F, Amadasi A, Campanini B, Bettati S, Dodatko T, Cozzini P, Kellogg GE, Cook PF, Roderick SL, Mozzarelli A. Design of O-acetylserine sulfhydrylase inhibitors by mimicking nature. Journal of Medicinal Chemistry. 53: 345-56. PMID 19928859 DOI: 10.1021/Jm901325E |
0.398 |
|
| 2010 |
LaChapelle S, Cook PF, Hanigan MH. Abstract 760: Sensitizing tumors to chemotherapy by inhibition of gamma-glutamyl transpeptidase Cancer Research. 70: 760-760. DOI: 10.1158/1538-7445.Am10-760 |
0.437 |
|
| 2009 |
Tyapochkin E, Cook PF, Chen G. para-Nitrophenyl sulfate activation of human sulfotransferase 1A1 is consistent with intercepting the E[middle dot]PAP complex and reformation of E[middle dot]PAPS. The Journal of Biological Chemistry. 284: 29357-64. PMID 19706609 DOI: 10.1074/Jbc.M109.049312 |
0.385 |
|
| 2009 |
Kaserer AO, Andi B, Cook PF, West AH. Effects of osmolytes on the SLN1-YPD1-SSK1 phosphorelay system from Saccharomyces cerevisiae. Biochemistry. 48: 8044-50. PMID 19618914 DOI: 10.1021/Bi900886G |
0.699 |
|
| 2009 |
Lin Y, West AH, Cook PF. Site-directed mutagenesis as a probe of the acid-base catalytic mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 48: 7305-12. PMID 19530703 DOI: 10.1021/Bi900175Z |
0.537 |
|
| 2009 |
Guan R, Nimmo SA, Schnackerz KD, Cook PF. (31)P NMR studies of O-acetylserine sulfhydrylase-B from Salmonella typhimurium. Archives of Biochemistry and Biophysics. 487: 85-90. PMID 19501038 DOI: 10.1016/J.Abb.2009.05.016 |
0.756 |
|
| 2009 |
Vashishtha AK, West AH, Cook PF. Chemical mechanism of saccharopine reductase from Saccharomyces cerevisiae. Biochemistry. 48: 5899-907. PMID 19449898 DOI: 10.1021/Bi900599S |
0.831 |
|
| 2009 |
Aktas DF, Cook PF. A lysine-tyrosine pair carries out acid-base chemistry in the metal ion-dependent pyridine dinucleotide-linked beta-hydroxyacid oxidative decarboxylases. Biochemistry. 48: 3565-77. PMID 19281248 DOI: 10.1021/Bi8022976 |
0.793 |
|
| 2009 |
Karsten WE, Cook PF. Detection of a gem-diamine and a stable quinonoid intermediate in the reaction catalyzed by serine-glyoxylate aminotransferase from Hyphomicrobium methylovorum. Biochimica Et Biophysica Acta. 1790: 575-80. PMID 19264108 DOI: 10.1016/J.Bbagen.2009.02.012 |
0.487 |
|
| 2009 |
King JB, West MB, Cook PF, Hanigan MH. A novel, species-specific class of uncompetitive inhibitors of gamma-glutamyl transpeptidase. The Journal of Biological Chemistry. 284: 9059-65. PMID 19203993 DOI: 10.1074/Jbc.M809608200 |
0.358 |
|
| 2008 |
Tyapochkin E, Cook PF, Chen G. Isotope exchange at equilibrium indicates a steady state ordered kinetic mechanism for human sulfotransferase. Biochemistry. 47: 11894-9. PMID 18928301 DOI: 10.1021/Bi801211T |
0.474 |
|
| 2008 |
Lin Y, West AH, Cook PF. Potassium is an activator of homoisocitrate dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 47: 10809-15. PMID 18785753 DOI: 10.1021/Bi801370H |
0.562 |
|
| 2008 |
Aktas DF, Cook PF. Role of residues in the adenosine binding site of NAD of the Ascaris suum malic enzyme. Biochimica Et Biophysica Acta. 1784: 2059-64. PMID 18725329 DOI: 10.1016/J.Bbapap.2008.07.014 |
0.826 |
|
| 2008 |
Qian J, Khandogin J, West AH, Cook PF. Evidence for a catalytic dyad in the active site of homocitrate synthase from Saccharomyces cerevisiae. Biochemistry. 47: 6851-8. PMID 18533686 DOI: 10.1021/Bi800087K |
0.825 |
|
| 2008 |
Guan R, Roderick SL, Huang B, Cook PF. Roles of histidines 154 and 189 and aspartate 139 in the active site of serine acetyltransferase from Haemophilus influenzae. Biochemistry. 47: 6322-8. PMID 18498176 DOI: 10.1021/Bi800075C |
0.771 |
|
| 2008 |
Vashishtha AK, West AH, Cook PF. Overall kinetic mechanism of saccharopine dehydrogenase (L-glutamate forming) from Saccharomyces cerevisiae. Biochemistry. 47: 5417-23. PMID 18416559 DOI: 10.1021/Bi800086G |
0.805 |
|
| 2008 |
Valderas MW, Andi B, Barrow WW, Cook PF. Examination of intrinsic sulfonamide resistance in Bacillus anthracis: a novel assay for dihydropteroate synthase. Biochimica Et Biophysica Acta. 1780: 848-53. PMID 18342015 DOI: 10.1016/J.Bbagen.2008.02.003 |
0.769 |
|
| 2008 |
Lin Y, Volkman J, Nicholas KM, Yamamoto T, Eguchi T, Nimmo SL, West AH, Cook PF. Chemical mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 47: 4169-80. PMID 18321070 DOI: 10.1021/Bi702361J |
0.521 |
|
| 2008 |
Tai CH, Rabeh WM, Guan R, Schnackerz KD, Cook PF. Role of Histidine-152 in cofactor orientation in the PLP-dependent O-acetylserine sulfhydrylase reaction. Archives of Biochemistry and Biophysics. 472: 115-25. PMID 18275838 DOI: 10.1016/J.Abb.2008.01.021 |
0.848 |
|
| 2008 |
Tai CH, Rabeh WM, Guan R, Schnackerz KD, Cook PF. Effect of mutation of lysine-120, located at the entry to the active site of O-acetylserine sulfhydrylase-A from Salmonella typhimurium. Biochimica Et Biophysica Acta. 1784: 629-37. PMID 18243146 DOI: 10.1016/J.Bbapap.2007.12.017 |
0.836 |
|
| 2008 |
Aktas DF, Cook PF. Proper positioning of the nicotinamide ring is crucial for the Ascaris suum malic enzyme reaction. Biochemistry. 47: 2539-46. PMID 18215074 DOI: 10.1021/Bi702261M |
0.831 |
|
| 2008 |
Cervellati C, Li L, Andi B, Guariento A, Dallocchio F, Cook PF. Proper orientation of the nicotinamide ring of NADP is important for the precatalytic conformational change in the 6-phosphogluconate dehydrogenase reaction. Biochemistry. 47: 1862-70. PMID 18205398 DOI: 10.1021/Bi7015684 |
0.776 |
|
| 2007 |
Karsten WE, Cook PF. Multiple roles of arginine 181 in binding and catalysis in the NAD-malic enzyme from Ascaris suum. Biochemistry. 46: 14578-88. PMID 18027982 DOI: 10.1021/Bi701524Z |
0.526 |
|
| 2007 |
Andi B, Xu H, Cook PF, West AH. Crystal structures of ligand-bound saccharopine dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 46: 12512-21. PMID 17939687 DOI: 10.1021/Bi701428M |
0.823 |
|
| 2007 |
Raboni S, Mozzarelli A, Cook PF. Control of ionizable residues in the catalytic mechanism of tryptophan synthase from Salmonella typhimurium. Biochemistry. 46: 13223-34. PMID 17927213 DOI: 10.1021/Bi701152F |
0.563 |
|
| 2007 |
Chattopadhyay A, Meier M, Ivaninskii S, Burkhard P, Speroni F, Campanini B, Bettati S, Mozzarelli A, Rabeh WM, Li L, Cook PF. Structure, mechanism, and conformational dynamics of O-acetylserine sulfhydrylase from Salmonella typhimurium: comparison of A and B isozymes. Biochemistry. 46: 8315-30. PMID 17583914 DOI: 10.1021/Bi602603C |
0.785 |
|
| 2007 |
Xu H, West AH, Cook PF. Determinants of substrate specificity for saccharopine dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 46: 7625-36. PMID 17542618 DOI: 10.1021/Bi700269P |
0.788 |
|
| 2007 |
Lin Y, Alguindigue SS, Volkman J, Nicholas KM, West AH, Cook PF. Complete kinetic mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 46: 890-8. PMID 17223711 DOI: 10.1021/Bi062067Q |
0.494 |
|
| 2007 |
Xu H, Alguindigue SS, West AH, Cook PF. A proposed proton shuttle mechanism for saccharopine dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 46: 871-82. PMID 17223709 DOI: 10.1021/Bi061980O |
0.803 |
|
| 2006 |
Yu M, Magalhães MLB, Cook PF, Blanchard JS. Bisubstrate inhibition: Theory and application to N-acetyltransferases Biochemistry. 45: 14788-14794. PMID 17144672 DOI: 10.1021/Bi061621T |
0.373 |
|
| 2006 |
Li L, Zhang L, Cook PF. Role of the S128, H186, and N187 triad in substrate binding and decarboxylation in the sheep liver 6-phosphogluconate dehydrogenase reaction. Biochemistry. 45: 12680-6. PMID 17042485 DOI: 10.1021/Bi0613675 |
0.507 |
|
| 2006 |
Xu H, West AH, Cook PF. Overall kinetic mechanism of saccharopine dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 45: 12156-66. PMID 17002315 DOI: 10.1021/Bi0610808 |
0.811 |
|
| 2006 |
Qian J, West AH, Cook PF. Acid-base chemical mechanism of homocitrate synthase from Saccharomyces cerevisiae. Biochemistry. 45: 12136-43. PMID 17002313 DOI: 10.1021/Bi060889H |
0.809 |
|
| 2006 |
Li L, Cook PF. The 2′-phosphate of NADP is responsible for proper orientation of the nicotinamide ring in the oxidative decarboxylation reaction catalyzed by sheep liver 6-phosphogluconate dehydrogenase Journal of Biological Chemistry. 281: 36803-36810. PMID 16959777 DOI: 10.1074/Jbc.M604609200 |
0.527 |
|
| 2006 |
Xu H, Andi B, Qian J, West AH, Cook PF. The α-aminoadipate pathway for lysine biosynthesis in fungi Cell Biochemistry and Biophysics. 46: 43-64. PMID 16943623 DOI: 10.1385/Cbb:46:1:43 |
0.78 |
|
| 2006 |
Andi B, Cook PF, West AH. Crystal structure of the his-tagged saccharopine reductase from Saccharomyces cerevisiae at 1.7-Å resolution Cell Biochemistry and Biophysics. 46: 17-26. PMID 16943620 DOI: 10.1385/Cbb:46:1:17 |
0.75 |
|
| 2006 |
Karsten WE, Cook PF. An isothermal titration calorimetry study of the binding of substrates and ligands to the tartrate dehydrogenase from Pseudomonas putida reveals half-of-the-sites reactivity Biochemistry. 45: 9000-9006. PMID 16846243 DOI: 10.1021/Bi0607251 |
0.417 |
|
| 2006 |
Li L, Dworkowski FSN, Cook PF. Importance in catalysis of the 6-phosphate-binding site of 6-phosphogluconate in sheep liver 6-phosphogluconate dehydrogenase Journal of Biological Chemistry. 281: 25568-25576. PMID 16803886 DOI: 10.1074/Jbc.M601154200 |
0.529 |
|
| 2006 |
Gibson GE, Harris BG, Cook PF. Optimum activity of the phosphofructokinase from Ascaris suum requires more than one metal ion. Biochemistry. 45: 2453-60. PMID 16475835 DOI: 10.1021/Bi052191U |
0.368 |
|
| 2006 |
Rabeh WM, Mather T, Cook PF. A three-dimensional homology model of the O-acetylserine sulfhydrylase-B from Salmonella typhimurium. Protein and Peptide Letters. 13: 7-13. PMID 16454663 DOI: 10.2174/092986606774502126 |
0.719 |
|
| 2006 |
Qian J, West AH, Cook PF. Acid - base chemical mechanism of homocitrate synthase from Saccharomyces cerevisiae Biochemistry. 45: 12136-12143. DOI: 10.1021/bi060889h |
0.746 |
|
| 2005 |
Karsten WE, Ohshiro T, Izumi Y, Cook PF. Reaction of serine-glyoxylate aminotransferase with the alternative substrate ketomalonate indicates rate-limiting protonation of a quinonoid intermediate. Biochemistry. 44: 15930-6. PMID 16313196 DOI: 10.1021/Bi051407P |
0.497 |
|
| 2005 |
Campanini B, Speroni F, Salsi E, Cook PF, Roderick SL, Huang B, Bettati S, Mozzarelli A. Interaction of serine acetyltransferase with O-acetylserine sulfhydrylase active site: evidence from fluorescence spectroscopy. Protein Science : a Publication of the Protein Society. 14: 2115-24. PMID 15987896 DOI: 10.1110/Ps.051492805 |
0.489 |
|
| 2005 |
Andi B, West AH, Cook PF. Regulatory mechanism of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae: I. Kinetic studies Journal of Biological Chemistry. 280: 31624-31632. PMID 15897192 DOI: 10.1074/Jbc.M502846200 |
0.767 |
|
| 2005 |
Andi B, Cook PF. Regulatory mechanism of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae: II. Theory Journal of Biological Chemistry. 280: 31633-31640. PMID 15897191 DOI: 10.1074/Jbc.M502847200 |
0.777 |
|
| 2005 |
Rabeh WM, Alguindigue SS, Cook PF. Mechanism of the addition half of the O-acetylserine sulfhydrylase-A reaction. Biochemistry. 44: 5541-50. PMID 15807548 DOI: 10.1021/Bi047479I |
0.768 |
|
| 2005 |
Karsten WE, Liu D, Rao GSJ, Harris BG, Cook PF. A catalytic triad is responsible for acid-base chemistry in the Ascaris suum NAD-malic enzyme Biochemistry. 44: 3626-3635. PMID 15736972 DOI: 10.1021/Bi047826O |
0.702 |
|
| 2005 |
Cervellati C, Dallocchio F, Bergamini CM, Cook PF. Role of methionine-13 in the catalytic mechanism of 6-phosphogluconate dehydrogenase from sheep liver Biochemistry. 44: 2432-2440. PMID 15709755 DOI: 10.1021/Bi0476679 |
0.517 |
|
| 2005 |
Waldmann G, Cook PF, Schnackerz KD. Purification and properties of β-alanine synthase from calf liver Protein and Peptide Letters. 12: 69-73. PMID 15638804 DOI: 10.2174/0929866053405904 |
0.345 |
|
| 2005 |
Janiak-Spens F, Cook PF, West AH. Kinetic analysis of YPD1-dependent phosphotransfer reactions in the yeast osmoregulatory phosphorelay system Biochemistry. 44: 377-386. PMID 15628880 DOI: 10.1021/Bi048433S |
0.332 |
|
| 2005 |
Johnson CM, Roderick SL, Cook PF. The serine acetyltransferase reaction: acetyl transfer from an acylpantothenyl donor to an alcohol. Archives of Biochemistry and Biophysics. 433: 85-95. PMID 15581568 DOI: 10.1016/J.Abb.2004.08.014 |
0.525 |
|
| 2004 |
Johnson CM, Huang B, Roderick SL, Cook PF. Chemical mechanism of the serine acetyltransferase from Haemophilus influenzae. Biochemistry. 43: 15534-9. PMID 15581365 DOI: 10.1021/Bi048450H |
0.466 |
|
| 2004 |
Schnackerz KD, Dobritzsch D, Lindqvist Y, Cook PF. Dihydropyrimidine dehydrogenase: a flavoprotein with four iron-sulfur clusters. Biochimica Et Biophysica Acta. 1701: 61-74. PMID 15450176 DOI: 10.1016/J.Bbapap.2004.06.009 |
0.422 |
|
| 2004 |
Andi B, West AH, Cook PF. Kinetic mechanism of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae Biochemistry. 43: 11790-11795. PMID 15362863 DOI: 10.1021/Bi048766P |
0.773 |
|
| 2004 |
Johnson CM, Huang B, Roderick SL, Cook PF. Kinetic mechanism of the serine acetyltransferase from Haemophilus influenzae. Archives of Biochemistry and Biophysics. 429: 115-22. PMID 15313214 DOI: 10.1016/J.Abb.2004.06.006 |
0.431 |
|
| 2004 |
Staab JF, Bahn YS, Tai CH, Cook PF, Sundstrom P. Expression of transglutaminase substrate activity on Candida albicans germ tubes through a coiled, disulfide-bonded N-terminal domain of Hwp1 requires C-terminal glycosylphosphatidylinositol modification. The Journal of Biological Chemistry. 279: 40737-47. PMID 15262971 DOI: 10.1074/Jbc.M406005200 |
0.345 |
|
| 2004 |
Rabeh WM, Cook PF. Structure and mechanism of O-acetylserine sulfhydrylase Journal of Biological Chemistry. 279: 26803-26806. PMID 15073190 DOI: 10.1074/Jbc.R400001200 |
0.773 |
|
| 2004 |
Andi B, West AH, Cook PF. Stabilization and characterization of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae Archives of Biochemistry and Biophysics. 421: 243-254. PMID 14984204 DOI: 10.1016/J.Abb.2003.11.005 |
0.788 |
|
| 2003 |
Karsten WE, Pais JE, Rao GS, Harris BG, Cook PF. Ascaris suum NAD-malic enzyme is activated by L-malate and fumarate binding to separate allosteric sites. Biochemistry. 42: 9712-21. PMID 12911313 DOI: 10.1021/Bi034101W |
0.52 |
|
| 2003 |
Rao GSJ, Coleman DE, Karsten WE, Cook PF, Harris BG. Crystallographic studies on Ascaris suum NAD-malic enzyme bound to reduced cofactor and identification of an effector site Journal of Biological Chemistry. 278: 38051-38058. PMID 12853453 DOI: 10.1074/Jbc.M305145200 |
0.485 |
|
| 2003 |
Campanini B, Raboni S, Vaccari S, Zhang L, Cook PF, Hazlett TL, Mozzarelli A, Bettati S. Surface-exposed tryptophan residues are essential for O-acetylserine sulfhydrylase structure, function, and stability Journal of Biological Chemistry. 278: 37511-37519. PMID 12813039 DOI: 10.1074/Jbc.M305138200 |
0.433 |
|
| 2003 |
Cook PF. α,β-Elimination reaction of O-acetylserine sulfhydrylase. Is the pyridine ring required? Biochimica Et Biophysica Acta - Proteins and Proteomics. 1647: 66-69. PMID 12686110 DOI: 10.1016/S1570-9639(03)00052-9 |
0.477 |
|
| 2003 |
Gojkovic Z, Rislund L, Andersen B, Sandrini MPB, Cook PF, Schnackerz KD, Piškur J. Dihydropyrimidine amidohydrolases and dihydroorotases share the same origin and several enzymatic properties Nucleic Acids Research. 31: 1683-1692. PMID 12626710 DOI: 10.1093/Nar/Gkg258 |
0.517 |
|
| 2003 |
Daum S, Tai CH, Cook PF. Characterization of the S272A,D site-directed mutations of O-Acetylserine sulfhydrylase: Involvement of the pyridine ring in the α,β-elimination reaction Biochemistry. 42: 106-113. PMID 12515544 DOI: 10.1021/Bi0268044 |
0.563 |
|
| 2002 |
Karsten WE, Cook PF. Detection of intermediates in reactions catalyzed by PLP-dependent enzymes: O-acetylserine sulfhydrylase and serine-glyoxalate aminotransferase Methods in Enzymology. 354: 223-237. PMID 12418230 DOI: 10.1016/S0076-6879(02)54019-2 |
0.483 |
|
| 2002 |
Liu D, Hwang CC, Cook PF. Alternative substrates for malic enzyme: Oxidative decarboxylation of L-aspartate Biochemistry. 41: 12200-12203. PMID 12356322 DOI: 10.1021/Bi026322S |
0.697 |
|
| 2002 |
Karsten WE, Tipton PA, Cook PF. Tartrate dehydrogenase catalyzes the stepwise oxidative decarboxylation of D-malate with both NAD and thio-NAD Biochemistry. 41: 12193-12199. PMID 12356321 DOI: 10.1021/Bi026278G |
0.459 |
|
| 2002 |
Coleman DE, Rao GSJ, Goldsmith EJ, Cook PF, Harris BG. Crystal structure of the malic enzyme from Ascaris suum complexed with nicotinamide adenine dinucleotide at 2.3 Å resolution Biochemistry. 41: 6928-6938. PMID 12033925 DOI: 10.1021/Bi0255120 |
0.495 |
|
| 2001 |
Tai CH, Burkhard P, Gani D, Jenn T, Johnson C, Cook PF. Characterization of the allosteric anion-binding site of O-acetylserine sulfhydrylase. Biochemistry. 40: 7446-52. PMID 11412097 DOI: 10.1021/Bi015511S |
0.483 |
|
| 2001 |
Karsten WE, Ohshiro T, Izumi Y, Cook PF. Initial velocity, spectral, and pH studies of the serine-glyoxylate aminotransferase from Hyphomicrobiuim methylovorum. Archives of Biochemistry and Biophysics. 388: 267-75. PMID 11368164 DOI: 10.1006/Abbi.2001.2294 |
0.524 |
|
| 2000 |
Sakurai M, Cook PF, Haseman CA, Uyeda K. Glutamate 325 is a general acid-base catalyst in the reaction catalyzed by fructose-2,6-bisphosphatase Biochemistry. 39: 16238-16243. PMID 11123954 DOI: 10.1021/Bi0020170 |
0.541 |
|
| 2000 |
Burkhard P, Tai CH, Jansonius JN, Cook PF. Identification of an allosteric anion-binding site on O-acetylserine sulfhydrylase: structure of the enzyme with chloride bound. Journal of Molecular Biology. 303: 279-86. PMID 11023792 DOI: 10.1006/Jmbi.2000.4109 |
0.501 |
|
| 2000 |
Liu D, Karsten WE, Cook PF. Lysine 199 is the general acid in the NAD-malic enzyme reaction Biochemistry. 39: 11955-11960. PMID 11009609 DOI: 10.1021/Bi000790P |
0.72 |
|
| 2000 |
Tai CH, Cook PF. O-acetylserine sulfhydrylase Advances in Enzymology and Related Areas of Molecular Biology. 74: 185-234. PMID 10800596 DOI: 10.1002/9780470123201.Ch5 |
0.49 |
|
| 2000 |
Stanley TM, Johnson WH, Burks EA, Whitman CP, Hwang CC, Cook PF. Expression and stereochemical and isotope effect studies of active 4-oxalocrotonate decarboxylase. Biochemistry. 39: 718-26. PMID 10651637 DOI: 10.1021/Bi9918902 |
0.399 |
|
| 1999 |
Schnackerz KD, Tai CH, Pötsch RKW, Cook PF. Substitution of pyridoxal 5'-phosphate in D-serine dehydratase from Escherichia coli by cofactor analogues provides information on cofactor binding and catalysis Journal of Biological Chemistry. 274: 36935-36943. PMID 10601247 DOI: 10.1074/Jbc.274.52.36935 |
0.432 |
|
| 1999 |
Zhang L, Chooback L, Cook PF. Lysine 183 is the general base in the 6-phosphogluconate dehydrogenase-catalyzed reaction Biochemistry. 38: 11231-11238. PMID 10471272 DOI: 10.1021/Bi990433I |
0.516 |
|
| 1999 |
Burkhard P, Tai CH, Ristroph CM, Cook PF, Jansonius JN. Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium. Journal of Molecular Biology. 291: 941-53. PMID 10452898 DOI: 10.1006/Jmbi.1999.3002 |
0.463 |
|
| 1999 |
Karsten WE, Chooback L, Liu D, Hwang CC, Lynch C, Cook PF. Mapping the active site topography of the NAD-malic enzyme via alanine- scanning site-directed mutagenesis Biochemistry. 38: 10527-10532. PMID 10441149 DOI: 10.1021/Bi9906165 |
0.698 |
|
| 1999 |
Jagannatha Rao GS, Cook PF, Harris BG. Kinetic characterization of a T-state of Ascaris suum phosphofructokinase with heterotropic negative cooperativity by ATP eliminated Archives of Biochemistry and Biophysics. 365: 335-343. PMID 10328829 DOI: 10.1006/Abbi.1999.1183 |
0.554 |
|
| 1999 |
Karsten WE, Hwang CC, Cook PF. α-Secondary tritium kinetic isotope effects indicate hydrogen tunneling and coupled motion occur in the oxidation of L-malate by NAD-malic enzyme Biochemistry. 38: 4398-4402. PMID 10194359 DOI: 10.1021/Bi982439Y |
0.472 |
|
| 1999 |
Yuen MH, Mizuguchi H, Lee YH, Cook PF, Uyeda K, Hasemann CA. Crystal structure of the H256A mutant of rat testis fructose-6- phosphate,2-kinase/fructose-2,6-bisphosphatase: Fructose 6-phosphate in the active site leads to mechanisms for both mutant and wild type bisphosphatase activities Journal of Biological Chemistry. 274: 2176-2184. PMID 9890980 DOI: 10.1074/Jbc.274.4.2176 |
0.433 |
|
| 1999 |
Mizuguchi H, Cook PF, Tai CH, Hasemann CA, Uyeda K. Reaction mechanism of fructose-2,6-bisphosphatase: A mutation of nucleophilic catalyst, histidine 256, induces an alteration in the reaction pathway Journal of Biological Chemistry. 274: 2166-2175. PMID 9890979 DOI: 10.1074/Jbc.274.4.2166 |
0.469 |
|
| 1999 |
Benci S, Bettati S, Vaccari S, Schianchi G, Mozzarelli A, Cook PF. Conformational probes of O-acetylserine sulfhydrylase: Fluorescence of tryptophans 50 and 161 Journal of Photochemistry and Photobiology B: Biology. 48: 17-26. DOI: 10.1016/S1011-1344(99)00003-2 |
0.459 |
|
| 1998 |
Cook PF. Mechanism from isotope effects Isotopes in Environmental and Health Studies. 34: 3-17. PMID 9854842 |
0.32 |
|
| 1998 |
Hwang CC, Cook PF. Multiple isotope effects as a probe of proton and hydride transfer in the 6-phosphogluconate dehydrogenase reaction Biochemistry. 37: 15698-15702. PMID 9843374 DOI: 10.1021/Bi981288W |
0.366 |
|
| 1998 |
Karsten WE, Chooback L, Cook PF. Glutamate 190 is a general acid catalyst in the 6-phosphogluconate- dehydrogenase-catalyzed reaction Biochemistry. 37: 15691-15697. PMID 9843373 DOI: 10.1021/Bi9812827 |
0.446 |
|
| 1998 |
Mozzarelli A, Bettati S, Pucci AM, Burkhard P, Cook PF. Catalytic competence of O-acetylserine sulfhydrylase in the crystal probed by polarized absorption microspectrophotometry Journal of Molecular Biology. 283: 135-146. PMID 9761679 DOI: 10.1006/Jmbi.1998.2038 |
0.501 |
|
| 1998 |
Burkhard P, Rao GS, Hohenester E, Schnackerz KD, Cook PF, Jansonius JN. Three-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium. Journal of Molecular Biology. 283: 121-33. PMID 9761678 DOI: 10.1107/S0108767396094159 |
0.395 |
|
| 1998 |
Hwang CC, Berdis AJ, Karsten WE, Cleland WW, Cook PF. Oxidative decarboxylation of 6-phosphogluconate by 6-phosphogluconate dehydrogenase proceeds by a stepwise mechanism with NADP and APADP as oxidants. Biochemistry. 37: 12596-602. PMID 9730832 DOI: 10.1021/Bi980611S |
0.431 |
|
| 1998 |
Tai CH, Yoon MY, Kim SK, Rege VD, Nalabolu SR, Kredich NM, Schnackerz KD, Cook PF. Cysteine 42 is important for maintaining an integral active site for O- acetylserine sulfhydrylase resulting in the stabilization of the α- aminoacrylate intermediate Biochemistry. 37: 10597-10604. PMID 9692949 DOI: 10.1021/Bi980647K |
0.542 |
|
| 1998 |
Chooback L, Price NE, Karsten WE, Nelson J, Sundstrom P, Cook PF. Cloning, expression, purification, and characterization of the 6-phosphogluconate dehydrogenase from sheep liver Protein Expression and Purification. 13: 251-258. PMID 9675070 DOI: 10.1006/Prep.1998.0896 |
0.338 |
|
| 1998 |
Rosenbaum K, Jahnke K, Schnackerz KD, Cook PF. Secondary tritium and solvent deuterium isotope effects as a probe of the reaction catalyzed by porcine recombinant dihydropyrimidine dehydrogenase Biochemistry. 37: 9156-9159. PMID 9636062 DOI: 10.1021/Bi973098B |
0.415 |
|
| 1997 |
Cook PF. Mechanism from isotope effects. Isotopes in Environmental and Health Studies. 33: 3-17. PMID 22087477 DOI: 10.1080/10256019708036327 |
0.305 |
|
| 1997 |
Benci S, Vaccari S, Mozzarelli A, Cook PF. Time-resolved fluorescence of O-acetylserine sulfhydrylase catalytic intermediates Biochemistry. 36: 15419-15427. PMID 9398272 DOI: 10.1021/Bi970464I |
0.331 |
|
| 1997 |
Rosenbaum K, Schaffrath B, Hagen WR, Jahnke K, Gonzalez FJ, Cook PF, Schnackerz KD. Purification, characterization, and kinetics of porcine recombinant dihydropyrimidine dehydrogenase. Protein Expression and Purification. 10: 185-91. PMID 9226714 DOI: 10.1006/Prep.1997.0735 |
0.45 |
|
| 1997 |
Mizuguchi H, Cook PF, Hasemann CA, Uyeda K. Chemical mechanism of the fructose-6-phosphate,2-kinase reaction from the pH dependence of kinetic parameters of site-directed mutants of active site basic residues Biochemistry. 36: 8775-8784. PMID 9220964 DOI: 10.1021/Bi970639O |
0.551 |
|
| 1997 |
Chooback L, Karsten WE, Kulkarni G, Nalabolu SR, Harris BG, Cook PF. Expression, purification, and characterization of the recombinant NAD-malic enzyme from Ascaris suum Protein Expression and Purification. 10: 51-54. PMID 9179290 DOI: 10.1006/Prep.1996.0705 |
0.431 |
|
| 1996 |
Price NE, Cook PF. Kinetic and chemical mechanisms of the sheep liver 6-phosphogluconate dehydrogenase Archives of Biochemistry and Biophysics. 336: 215-223. PMID 8954568 DOI: 10.1006/Abbi.1996.0551 |
0.476 |
|
| 1996 |
Rege VD, Kredich NM, Tai CH, Karsten WE, Schnackerz KD, Cook PF. A change in the internal aldimine lysine (K42) in O-acetylserine sulfhydrylase to alanine indicates its importance in transimination and as a general base catalyst Biochemistry. 35: 13485-13493. PMID 8873618 DOI: 10.1021/Bi961517J |
0.511 |
|
| 1996 |
Tipton PA, Quinn TP, Peisach J, Cook PF. Role of the divalent metal ion in the NAD:malic enzyme reaction: an ESEEM determination of the ground state conformation of malate in the E:Mn:malate complex. Protein Science : a Publication of the Protein Society. 5: 1648-54. PMID 8844853 DOI: 10.1002/Pro.5560050818 |
0.484 |
|
| 1996 |
Cook PF, Tai CH, Hwang CC, Woehl EU, Dunn MF, Schnackerz KD. Substitution of pyridoxal 5'-phosphate in the O-acetylserine sulfhydrylase from Salmonella typhimurium by cofactor analogs provides a test of the mechanism proposed for formation of the α-aminoacrylate intermediate Journal of Biological Chemistry. 271: 25842-25849. PMID 8824215 DOI: 10.1074/Jbc.271.42.25842 |
0.547 |
|
| 1996 |
Schmitt U, Jahnke K, Rosenbaum K, Cook PF, Schnackerz KD. Purification and characterization of dihydropyrimidine dehydrogenase from Alcaligenes eutrophus. Archives of Biochemistry and Biophysics. 332: 175-82. PMID 8806723 DOI: 10.1006/Abbi.1996.0330 |
0.483 |
|
| 1996 |
Treptau T, Piram P, Cook PF, Rodriguez PH, Hoffmann R, Jung S, Thalhofer HP, Harris BG, Hofer HW. Comparison of the substrate specificities of cAMP-dependent protein kinase from bovine heart and Ascaris suum muscle. Biological Chemistry Hoppe-Seyler. 377: 203-9. PMID 8722322 DOI: 10.1515/Bchm3.1996.377.3.203 |
0.303 |
|
| 1996 |
Strambini GB, Cioni P, Cook PF. Tryptophan luminescence as a probe of enzyme conformation along the O-acetylserine sulfhydrylase reaction pathway. Biochemistry. 35: 8392-400. PMID 8679597 DOI: 10.1021/Bi952919E |
0.42 |
|
| 1996 |
Woehl EU, Tai CH, Dunn MF, Cook PF. Formation of the alpha-aminoacrylate immediate limits the overall reaction catalyzed by O-acetylserine sulfhydrylase. Biochemistry. 35: 4776-83. PMID 8664267 DOI: 10.1021/Bi952938O |
0.442 |
|
| 1996 |
Hwang CC, Woehl EU, Minter DE, Dunn MF, Cook PF. Kinetic isotope effects as a probe of the beta-elimination reaction catalyzed by O-acetylserine sulfhydrylase. Biochemistry. 35: 6358-65. PMID 8639581 DOI: 10.1021/Bi9602472 |
0.452 |
|
| 1996 |
Gibson GE, Harris BG, Cook PF. Isotope partitioning with Ascaris suum phosphofructokinase is consistent with an ordered kinetic mechanism Biochemistry. 35: 5451-5457. PMID 8611535 DOI: 10.1021/Bi952898O |
0.504 |
|
| 1996 |
Schnackerz KD, Cook PF. Resolution of pyridoxal 5'-phosphate from O-acetylserine sulfhydrylase from Salmonella typhimurium and reconstitution of apoenzyme with cofactor and cofactor analogues as a probe of the cofactor binding site. Archives of Biochemistry and Biophysics. 324: 71-7. PMID 7503562 DOI: 10.1006/Abbi.1995.9927 |
0.557 |
|
| 1995 |
Karsten WE, Gavva SR, Park SH, Cook PF. Metal ion activator effects on intrinsic isotope effects for hydride transfer from decarboxylation in the reaction catalyzed by the NAD-malic enzyme from Ascaris suum. Biochemistry. 34: 3253-60. PMID 7880820 DOI: 10.1021/Bi00010A015 |
0.403 |
|
| 1995 |
Payne MA, Rao GS, Harris BG, Cook PF. Acid-base catalytic mechanism and pH dependence of fructose 2,6-bisphosphate activation of the Ascaris suum phosphofructokinase. Biochemistry. 34: 7781-7. PMID 7794888 DOI: 10.1021/Bi00024A001 |
0.397 |
|
| 1995 |
Yoon MY, Thayer-Cook KA, Berdis AJ, Karsten WE, Schnackerz KD, Cook PF. Acid-base chemical mechanism of aspartase from Hafnia alvei. Archives of Biochemistry and Biophysics. 320: 115-22. PMID 7793969 DOI: 10.1006/Abbi.1995.1348 |
0.493 |
|
| 1995 |
Rao GS, Schnackerz KD, Harris BG, Cook PF. A pH-dependent allosteric transition in Ascaris suum phosphofructokinase distinct from that observed with fructose 2,6-bisphosphate. Archives of Biochemistry and Biophysics. 322: 410-6. PMID 7574715 DOI: 10.1006/Abbi.1995.1482 |
0.475 |
|
| 1995 |
Tai CH, Nalabolu SR, Simmons JW, Jacobson TM, Cook PF. Acid-base chemical mechanism of O-acetylserine sulfhydrylases-A and -B from pH studies. Biochemistry. 34: 12311-22. PMID 7547974 DOI: 10.1021/Bi00038A027 |
0.52 |
|
| 1995 |
Schnackerz KD, Tai CH, Simmons JW, Jacobson TM, Rao GS, Cook PF. Identification and spectral characterization of the external aldimine of the O-acetylserine sulfhydrylase reaction. Biochemistry. 34: 12152-60. PMID 7547955 DOI: 10.1021/Bi00038A008 |
0.465 |
|
| 1995 |
Lagueux J, Ménard L, Candas B, Brochu G, Potvin F, Verreault A, Cook PF, Poirier GG. Equilibrium model in an in vitro poly(ADP-ribose) turnover system. Biochimica Et Biophysica Acta. 1264: 201-8. PMID 7495864 DOI: 10.1016/0167-4781(95)00143-5 |
0.41 |
|
| 1995 |
Karsten WE, Lai C, Cook PF. Inverse Solvent Isotope Effects in the NAD-Malic Enzyme Reaction Are the Result of the Viscosity Difference between D2O and H2O: Implications for Solvent Isotope Effect Studies Journal of the American Chemical Society. 117: 5914-5918. DOI: 10.1021/Ja00127A002 |
0.402 |
|
| 1994 |
Leu LS, Cook PF. Kinetic mechanism of serine transacetylase from Salmonella typhimurium. Biochemistry. 33: 2667-71. PMID 8117730 DOI: 10.1021/Bi00175A040 |
0.433 |
|
| 1994 |
Karsten WE, Cook PF. Stepwise versus concerted oxidative decarboxylation catalyzed by malic enzyme: a reinvestigation. Biochemistry. 33: 2096-103. PMID 8117666 DOI: 10.1021/Bi00174A016 |
0.496 |
|
| 1994 |
Bertagnolli BL, Cook PF. Lanthanide pyrophosphates as substrates for the pyrophosphate-dependent phosphofructokinases from Propionibacterium freudenreichii and Phaseolus aureus: evidence for a second metal ion required for reaction. Biochemistry. 33: 1663-7. PMID 8110768 DOI: 10.1021/Bi00173A007 |
0.38 |
|
| 1993 |
Rao GS, Mottonen J, Goldsmith EJ, Cook PF. Crystallization and preliminary X-ray data for the A-isozyme of O-acetylserine sulfhydrylase from Salmonella typhimurium. Journal of Molecular Biology. 231: 1130-2. PMID 8515470 DOI: 10.1006/Jmbi.1993.1358 |
0.365 |
|
| 1993 |
Jahnke K, Podschun B, Schnackerz KD, Kautz J, Cook PF. Acid-base catalytic mechanism of dihydropyrimidinase from pH studies. Biochemistry. 32: 5160-6. PMID 8494893 DOI: 10.1021/Bi00070A027 |
0.532 |
|
| 1993 |
Berdis AJ, Cook PF. Chemical mechanism of 6-phosphogluconate dehydrogenase from Candida utilis from pH studies. Biochemistry. 32: 2041-6. PMID 8448162 DOI: 10.1021/Bi00059A022 |
0.435 |
|
| 1993 |
Berdis AJ, Cook PF. Overall kinetic mechanism of 6-phosphogluconate dehydrogenase from Candida utilis. Biochemistry. 32: 2036-40. PMID 8448161 DOI: 10.1021/Bi00059A021 |
0.445 |
|
| 1993 |
Rajapaksa R, Abu-Soud H, Raushel FM, Harris BG, Cook PF. Pre-steady-state kinetics reveal a slow isomerization of the enzyme-NAD complex in the NAD-malic enzyme reaction. Biochemistry. 32: 1928-34. PMID 8448150 DOI: 10.1021/Bi00059A007 |
0.535 |
|
| 1993 |
Cook PF, Yoon MY, Hara S, McClure GD. Product dependence of deuterium isotope effects in enzyme-catalyzed reactions. Biochemistry. 32: 1795-802. PMID 8439540 DOI: 10.1021/Bi00058A013 |
0.387 |
|
| 1993 |
Kulkarni G, Cook PF, Harris BG. Cloning and nucleotide sequence of a full-length cDNA encoding Ascaris suum malic enzyme. Archives of Biochemistry and Biophysics. 300: 231-7. PMID 8424657 DOI: 10.1006/Abbi.1993.1032 |
0.319 |
|
| 1993 |
Berdis AJ, Cook PF. The 2'-phosphate of NADP is critical for optimum productive binding to 6-phosphogluconate dehydrogenase from Candida utilis. Archives of Biochemistry and Biophysics. 305: 551-8. PMID 8373193 DOI: 10.1006/Abbi.1993.1460 |
0.501 |
|
| 1993 |
Qamar R, Cook PF. pH dependence of the kinetic mechanism of the adenosine 3',5'-monophosphate dependent protein kinase catalytic subunit in the direction of magnesium adenosine 5'-diphosphate phosphorylation. Biochemistry. 32: 6802-6. PMID 8329403 DOI: 10.1021/Bi00077A035 |
0.438 |
|
| 1993 |
McClure GD, Qamar R, Cook PF. A method for counting active sites of cyclic AMP-dependent protein kinase. Journal of Enzyme Inhibition. 7: 151-7. PMID 7509870 DOI: 10.3109/14756369309040757 |
0.38 |
|
| 1992 |
Clancy LL, Rao GS, Finzel BC, Muchmore SW, Holland DR, Watenpaugh KD, Krishnamurthy HM, Sweet RM, Cook PF, Harris BG. Crystallization of the NAD-dependent malic enzyme from the parasitic nematode Ascaris suum. Journal of Molecular Biology. 226: 565-9. PMID 1640469 DOI: 10.1016/0022-2836(92)90971-L |
0.419 |
|
| 1992 |
Cook PF, Hara S, Nalabolu S, Schnackerz KD. pH dependence of the absorbance and 31P NMR spectra of O-acetylserine sulfhydrylase in the absence and presence of O-acetyl-L-serine. Biochemistry. 31: 2298-303. PMID 1540585 DOI: 10.1021/Bi00123A013 |
0.503 |
|
| 1992 |
Lai CJ, Harris BG, Cook PF. Mechanism of activation of the NAD-malic enzyme from Ascaris suum by fumarate Archives of Biochemistry and Biophysics. 299: 214-219. PMID 1444459 DOI: 10.1016/0003-9861(92)90266-Y |
0.451 |
|
| 1992 |
Qamar R, Yoon MY, Cook PF. Kinetic mechanism of the adenosine 3',5'-monophosphate dependent protein kinase catalytic subunit in the direction of magnesium adenosine 5'-diphosphate phosphorylation. Biochemistry. 31: 9986-92. PMID 1327136 DOI: 10.1021/Bi00156A018 |
0.415 |
|
| 1991 |
Gavva SR, Harris BG, Weiss PM, Cook PF. Modification of a thiol at the active site of the Ascaris suum NAD-malic enzyme results in changes in the rate-determining steps for oxidative decarboxylation of L-malate. Biochemistry. 30: 5764-9. PMID 2043616 DOI: 10.1021/Bi00237A019 |
0.498 |
|
| 1991 |
Weiss PM, Gavva SR, Harris BG, Urbauer JL, Cleland WW, Cook PF. Multiple isotope effects with alternative dinucleotide substrates as a probe of the malic enzyme reaction. Biochemistry. 30: 5755-63. PMID 2043615 DOI: 10.1021/Bi00237A018 |
0.45 |
|
| 1991 |
Rao GS, Cook PF, Harris BG. Modification of the ATP inhibitory site of the Ascaris suum phosphofructokinase results in the stabilization of an inactive T state. Biochemistry. 30: 9998-10004. PMID 1832959 DOI: 10.1021/BI00105A026 |
0.366 |
|
| 1991 |
Mallick S, Harris BG, Cook PF. Kinetic mechanism of NAD:malic enzyme from Ascaris suum in the direction of reductive carboxylation. Journal of Biological Chemistry. 266: 2732-2738. DOI: 10.1016/s0021-9258(18)49906-1 |
0.396 |
|
| 1989 |
Park SH, Harris BG, Cook PF. Substrate activation by malate induced by oxalate in the Ascaris suum NAD-malic enzyme reaction. Biochemistry. 28: 6334-40. PMID 2790001 DOI: 10.1021/Bi00441A027 |
0.515 |
|
| 1989 |
Cho YK, Cook PF. pH dependence of the kinetic parameters for the pyrophosphate-dependent phosphofructokinase reaction supports a proton-shuttle mechanism. Biochemistry. 28: 4155-60. PMID 2548569 DOI: 10.1021/Bi00436A005 |
0.545 |
|
| 1988 |
Weiss PM, Garcia GA, Kenyon GL, Cleland WW, Cook PF. Kinetics and mechanism of benzoylformate decarboxylase using 13C and solvent deuterium isotope effects on benzoylformate and benzoylformate analogues. Biochemistry. 27: 2197-205. PMID 3378056 DOI: 10.1021/bi00406a058 |
0.411 |
|
| 1988 |
Cini JK, Cook PF, Gracy RW. Molecular basis for the isozymes of bovine glucose-6-phosphate isomerase Archives of Biochemistry and Biophysics. 263: 96-106. PMID 3369868 DOI: 10.1016/0003-9861(88)90617-0 |
0.411 |
|
| 1988 |
Chen CY, Harris BG, Cook PF. Isotope partitioning for NAD-malic enzyme from Ascaris suum confirms a steady-state random kinetic mechanism. Biochemistry. 27: 212-9. PMID 3280016 DOI: 10.1021/Bi00401A032 |
0.333 |
|
| 1988 |
Weiss PM, Chen CY, Cleland WW, Cook PF. Use of primary deuterium and 15N isotope effects to deduce the relative rates of steps in the mechanisms of alanine and glutamate dehydrogenases. Biochemistry. 27: 4814-22. PMID 3139028 DOI: 10.1021/Bi00413A035 |
0.449 |
|
| 1988 |
Bhatnagar A, Das B, Gavva SR, Cook PF, Srivastava SK. The kinetic mechanism of human placental aldose reductase and aldehyde reductase II. Archives of Biochemistry and Biophysics. 261: 264-74. PMID 3128169 DOI: 10.1016/0003-9861(88)90341-4 |
0.458 |
|
| 1988 |
Kong CT, Cook PF. Isotope partitioning in the adenosine 3′,5′-monophosphate dependent protein kinase reaction indicates a steady-state random kinetic mechanism Biochemistry. 27: 4795-4799. PMID 3048391 DOI: 10.1021/Bi00413A032 |
0.301 |
|
| 1988 |
Cho YK, Matsunaga TO, Kenyon GL, Bertagnolli BL, Cook PF. Isotope exchange as a probe of the kinetic mechanism of pyrophosphate-dependent phosphofructokinase. Biochemistry. 27: 3320-5. PMID 2839232 |
0.311 |
|
| 1988 |
Cho YK, Cook PF. Inactivation of pyrophosphate-dependent phosphofructokinase from Propionibacterium freudenreichii by pyridoxal 5'-phosphate. Determination of the pH dependence of enzyme-reactant dissociation constants from protection against inactivation. Journal of Biological Chemistry. 263: 5135-5140. DOI: 10.1016/s0021-9258(18)60690-8 |
0.371 |
|
| 1987 |
Rao GSJ, Kong CT, Benjamin RC, Harris BG, Cook PF. Modification of an arginine residue essential for the activity of NAD-malic enzyme from Ascaris suum Archives of Biochemistry and Biophysics. 255: 8-13. PMID 3592670 DOI: 10.1016/0003-9861(87)90288-8 |
0.509 |
|
| 1987 |
Weiss PM, Cook PF, Hermes JD, Cleland WW. Evidence from nitrogen-15 and solvent deuterium isotope effects on the chemical mechanism of adenosine deaminase Biochemistry. 26: 7378-7384. PMID 3427079 DOI: 10.1021/Bi00397A027 |
0.416 |
|
| 1987 |
Yoon MY, Cook PF. Chemical mechanism of the adenosine cyclic 3',5'-monophosphate dependent protein kinase from pH studies. Biochemistry. 26: 4118-25. PMID 2820483 DOI: 10.1021/Bi00387A056 |
0.473 |
|
| 1986 |
Park SH, Harris BG, Cook PF. pH dependence of kinetic parameters for oxalacetate decarboxylation and pyruvate reduction reactions catalyzed by malic enzyme. Biochemistry. 25: 3752-9. PMID 3741834 DOI: 10.1021/Bi00361A004 |
0.523 |
|
| 1986 |
Kiick DM, Harris BG, Cook PF. Protonation mechanism and location of rate-determining steps for the Ascaris suum nicotinamide adenine dinucleotide-malic enzyme reaction from isotope effects and pH studies. Biochemistry. 25: 227-36. PMID 3513825 DOI: 10.1021/Bi00349A032 |
0.468 |
|
| 1986 |
Bertagnolli BL, Younathan ES, Voll RJ, Cook PF. Kinetic studies on the activation of pyrophosphate-dependent phosphofructokinase from mung bean by fructose 2,6-bisphosphate and related compounds. Biochemistry. 25: 4682-7. PMID 3021199 DOI: 10.1021/Bi00364A034 |
0.512 |
|
| 1986 |
Bertagnolli BL, Younathan ES, Voll RJ, Pittman CE, Cook PF. Carbohydrate substrate specificity of bacterial and plant pyrophosphate-dependent phosphofructokinases. Biochemistry. 25: 4674-81. PMID 3021198 DOI: 10.1021/Bi00364A033 |
0.455 |
|
| 1985 |
Park SH, Kiick DM, Harris BG, Cook PF. Kinetic mechanism in the direction of oxidative decarboxylation for NAD-malic enzyme from Ascaris suum. Biochemistry. 23: 5446-53. PMID 6509028 DOI: 10.1021/Bi00318A011 |
0.416 |
|
| 1985 |
Rao JG, Harris BG, Cook PF. Diethylpyrocarbonate inactivation of NAD-malic enzyme from Ascaris suum. Archives of Biochemistry and Biophysics. 241: 67-74. PMID 4026323 DOI: 10.1016/0003-9861(85)90362-5 |
0.495 |
|
| 1985 |
Nuiry II, Cook PF. The pH dependence of the reductive carboxylation of pyruvate by malic enzyme. Biochimica Et Biophysica Acta. 829: 295-8. PMID 3995057 DOI: 10.1016/0167-4838(85)90201-8 |
0.491 |
|
| 1984 |
Kiick DM, Allen BL, Rao JG, Harris BG, Cook PF. Determination of dissociation constants for enzyme-reactant complexes for NAD-malic enzyme by modulation of the thiol inactivation rate. Biochemistry. 23: 5454-9. PMID 6509029 DOI: 10.1021/Bi00318A012 |
0.52 |
|
| 1984 |
Nuiry II, Hermes JD, Weiss PM, Chen CY, Cook PF. Kinetic mechanism and location of rate-determining steps for aspartase from Hafnia alvei. Biochemistry. 23: 5168-75. PMID 6509019 DOI: 10.1021/Bi00317A013 |
0.385 |
|
| 1984 |
Bertagnolli BL, Cook PF. Kinetic mechanism of pyrophosphate-dependent phosphofructokinase from Propionibacterium freudenreichii. Biochemistry. 23: 4101-8. PMID 6091737 DOI: 10.1021/Bi00313A014 |
0.361 |
|
| 1983 |
Taylor KB, Cook PF, Cleland WW. Solvent isotope effects on the reaction catalyzed by yeast hexokinase. European Journal of Biochemistry. 134: 571-4. PMID 6349994 DOI: 10.1111/J.1432-1033.1983.Tb07604.X |
0.361 |
|
| 1982 |
Grimshaw CE, Cook PF, Cleland WW. Use of isotope effects and pH studies to determine the chemical mechanism of Bacillus subtilis L-alanine dehydrogenase. Biochemistry. 20: 5655-61. PMID 6794612 DOI: 10.1021/Bi00523A003 |
0.381 |
|
| 1982 |
Cook PF, Neville ME, Vrana KE, Hartl FT, Roskoski R. Adenosine cyclic 3',5'-monophosphate dependent protein kinase: kinetic mechanism for the bovine skeletal muscle catalytic subunit. Biochemistry. 21: 5794-9. PMID 6295440 DOI: 10.1021/Bi00266A011 |
0.364 |
|
| 1982 |
Cook PF. Kinetic studies to determine the mechanism of regulation of bovine liver glutamate dehydrogenase by nucleotide effectors. Biochemistry. 21: 113-6. PMID 6120719 DOI: 10.1021/Bi00530A020 |
0.437 |
|
| 1981 |
Cook PF, Oppenheimer NJ, Cleland WW. Secondary deuterium and nitrogen-15 isotope effects in enzyme-catalyzed reactions. Chemical mechanism of liver alcohol dehydrogenase. Biochemistry. 20: 1817-25. PMID 7013802 DOI: 10.1021/Bi00510A016 |
0.381 |
|
| 1981 |
Cook PF, Cleland WW. pH variation of isotope effects in enzyme-catalyzed reactions. 2. Isotope-dependent step not pH dependent. Kinetic mechanism of alcohol dehydrogenase. Biochemistry. 20: 1805-16. PMID 7013801 DOI: 10.1021/Bi00510A015 |
0.456 |
|
| 1981 |
Cook PF, Cleland WW. pH variation of isotope effects in enzyme-catalyzed reactions. 1. Isotope- and pH-dependent steps the same. Biochemistry. 20: 1797-805. PMID 7013800 DOI: 10.1021/Bi00510A014 |
0.431 |
|
| 1981 |
Cook PF, Cleland WW. Mechanistic deductions from isotope effects in multireactant enzyme mechanisms. Biochemistry. 20: 1790-6. PMID 7013799 DOI: 10.1021/Bi00510A013 |
0.449 |
|
| 1980 |
Cook PF, Blanchard JS, Cleland WW. Primary and secondary deuterium isotope effects on equilibrium constants for enzyme-catalyzed reactions. Biochemistry. 19: 4853-8. PMID 7000186 DOI: 10.1021/Bi00562A023 |
0.31 |
|
| 1979 |
Viola RE, Cook PF, Cleland WW. Stereoselective preparation of deuterated reduced nicotinamide adenine nucleotides and substrates by enzymatic synthesis. Analytical Biochemistry. 96: 334-40. PMID 224725 DOI: 10.1016/0003-2697(79)90590-6 |
0.381 |
|
| 1978 |
Cook PF, Wedding RT. Cysteine synthetase from Salmonella typhimurium LT-2. Aggregation, kinetic behavior, and effect of modifiers. The Journal of Biological Chemistry. 253: 7874-9. PMID 359557 |
0.563 |
|
| 1977 |
Cook PF, Wedding RT. Overall mechanism and rate equation for O-acetylserine sulfhydrylase. The Journal of Biological Chemistry. 252: 3459. PMID 863890 |
0.606 |
|
| 1977 |
Cook PF, Wedding RT. salmonella typhimurium/enzymol. Archives of Biochemistry and Biophysics. 178: 293-302. PMID 319757 DOI: 10.1016/0003-9861(77)90194-1 |
0.643 |
|
| 1976 |
Cook PF, Wedding RT. A reaction mechanism from steady state kinetic studies for O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2. The Journal of Biological Chemistry. 251: 2023-9. PMID 773932 |
0.671 |
|
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