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Thomas L. Nowak - Publications

Chemistry and Biochemistry University of Notre Dame, Notre Dame, IN, United States 
enzyme mechanisms, their regulation and structure and how they are interrelated

47 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2006 Holyoak T, Sullivan SM, Nowak T. Structural insights into the mechanism of PEPCK catalysis. Biochemistry. 45: 8254-63. PMID 16819824 DOI: 10.1021/Bi060269G  0.717
2004 Susan-Resiga D, Nowak T. Proton donor in yeast pyruvate kinase: chemical and kinetic properties of the active site Thr 298 to Cys mutant. Biochemistry. 43: 15230-15245. PMID 15568816 DOI: 10.1021/Bi049864D  0.76
2004 Holyoak T, Nowak T. pH Dependence of the reaction catalyzed by avian mitochondrial phosphoenolpyruvate carboxykinase. Biochemistry. 43: 7054-65. PMID 15170343 DOI: 10.1021/Bi049707E  0.672
2003 Susan-Resiga D, Nowak T. Monitoring active site alterations upon mutation of yeast pyruvate kinase using 205Tl+ NMR Journal of Biological Chemistry. 278: 40943-40952. PMID 12882975 DOI: 10.1074/Jbc.M306068200  0.726
2003 Susan-Resiga D, Nowak T. The proton transfer step catalyzed by yeast pyruvate kinase. Journal of Biological Chemistry. 278: 12660-12671. PMID 12562754 DOI: 10.1074/Jbc.M300257200  0.749
2002 Krautwurst H, Roschzttardtz H, Bazaes S, González-Nilo FD, Nowak T, Cardemil E. Lysine 213 and histidine 233 participate in Mn(II) binding and catalysis in Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase. Biochemistry. 41: 12763-70. PMID 12379119 DOI: 10.1021/Bi026241W  0.541
2002 Ríos SE, Nowak T. Role of cysteine 306 in the catalytic mechanism of Ascaris suum phosphoenolpyruvate carboxykinase. Archives of Biochemistry and Biophysics. 404: 25-37. PMID 12127066 DOI: 10.1016/S0003-9861(02)00236-9  0.745
2001 Bollenbach TJ, Nowak T. Kinetic Linked-Function Analysis of the Multiligand Interactions on Mg2+-Activated Yeast Pyruvate Kinase† Biochemistry. 40: 13097-13106. PMID 11669648 DOI: 10.1021/Bi010126O  0.426
2001 Bollenbach TJ, Nowak T. Thermodynamic Linked-Function Analysis of Mg2+-Activated Yeast Pyruvate Kinase† Biochemistry. 40: 13088-13096. PMID 11669647 DOI: 10.1021/Bi010125W  0.372
2001 Holyoak T, Nowak T. Structural investigation of the binding of nucleotide to phosphoenolpyruvate carboxykinase by NMR. Biochemistry. 40: 11037-47. PMID 11551200 DOI: 10.1021/Bi011374N  0.72
2001 Ramírez-Silva L, Ferreira ST, Nowak T, Tuena de Gómez-Puyou M, Gómez-Puyou A. Dimethylsulfoxide promotes K+-independent activity of pyruvate kinase and the acquisition of the active catalytic conformation. European Journal of Biochemistry / Febs. 268: 3267-74. PMID 11389729 DOI: 10.1042/Bst028A319A  0.452
2000 Hlavaty JJ, Nowak T. Characterization of the second metal site on avian phosphoenolpyruvate carboxykinase. Biochemistry. 39: 1373-1388. PMID 10684618 DOI: 10.1021/Bi991692A  0.352
1999 Vinarov DA, Nowak T. Role of His159 in yeast enolase catalysis. Biochemistry. 38: 12138-12149. PMID 10508418 DOI: 10.1021/Bi990760Q  0.39
1999 Bollenbach TJ, Mesecar AD, Nowak T. Role of lysine 240 in the mechanism of yeast pyruvate kinase catalysis. Biochemistry. 38: 9137-45. PMID 10413488 DOI: 10.1021/Bi990690N  0.613
1998 Vinarov DA, Nowak T. pH dependence of the reaction catalyzed by yeast Mg-enolase. Biochemistry. 37: 15238-15246. PMID 9790688 DOI: 10.1021/Bi981047O  0.397
1998 Hlavaty JJ, Nowak T. Chromium(III) modification of the first metal binding site of phosphoenolpyruvate carboxykinase. Biochemistry. 37: 8061-8070. PMID 9609700 DOI: 10.1021/Bi9807299  0.439
1998 Jurica MS, Mesecar A, Heath PJ, Shi W, Nowak T, Stoddard BL. The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate Structure. 6: 195-210. PMID 9519410 DOI: 10.1016/S0969-2126(98)00021-5  0.684
1997 Hlavaty JJ, Nowak T. Affinity Cleavage At The Metal-Binding Site Of Phosphoenolpyruvate Carboxykinase Biochemistry. 36: 15514-15525. PMID 9398280 DOI: 10.1021/Bi970574P  0.459
1997 Mesecar AD, Nowak T. Metal-ion-mediated allosteric triggering of yeast pyruvate kinase. 1. A multidimensional kinetic linked-function analysis Biochemistry. 36: 6792-6802. PMID 9184162 DOI: 10.1021/Bi962869T  0.666
1997 Hlavaty JJ, Nowak T. Formation and characterization of an active phosphoenolpyruvate carboxykinase-cobalt(III) complex. Biochemistry. 36: 3389-3403. PMID 9116019 DOI: 10.1021/Bi962255O  0.415
1992 Lee ME, Nowak T. Metal ion specificity at the catalytic site of yeast enolase. Biochemistry. 31: 2172-2180. PMID 1536858 DOI: 10.1021/Bi00122A039  0.35
1992 Lee BH, Nowak T. Influence of pH on the Mn2+ activation of and binding to yeast enolase: a functional study. Biochemistry. 31: 2165-2171. PMID 1536857 DOI: 10.1021/Bi00122A038  0.458
1992 Lee ME, Nowak T. 25Mg NMR studies of yeast enolase and rabbit muscle pyruvate kinase Archives of Biochemistry and Biophysics. 293: 264-273. PMID 1311162 DOI: 10.1016/0003-9861(92)90394-C  0.404
1992 Villafranca JJ, Nowak T. 2 Metal Ions at Enzyme Active Sites Enzymes. 20: 63-94. DOI: 10.1016/S1874-6047(08)60020-7  0.397
1991 Guidinger PF, Nowak T. An active-site lysine in avian liver phosphoenolpyruvate carboxykinase. Biochemistry. 30: 8851-8861. PMID 1909575 DOI: 10.1021/Bi00100A018  0.52
1990 Guidinger PF, Nowak T. Analogs of oxalacetate as potential substrates for phosphoenolpyruvate carboxykinase. Archives of Biochemistry and Biophysics. 278: 131-141. PMID 2321953 DOI: 10.1016/0003-9861(90)90241-P  0.424
1989 Hwang SH, Nowak T. Stereoselective ligand interactions of chicken liver phosphoenolpyruvate carboxykinase with fluorophosphoenolpyruvate Archives of Biochemistry and Biophysics. 269: 646-663. PMID 2919888 DOI: 10.1016/0003-9861(89)90150-1  0.397
1988 Kramer P, Nowak T. The Preparation and Characterization of Cr(III) and Co(III) Complexes of GDP and GTP and Their Interactions with Avian Phosphoenolpyruvate Carboxykinas Journal of Inorganic Biochemistry. 32: 135-151. PMID 3346664 DOI: 10.1016/0162-0134(88)80022-9  0.363
1987 Lee MH, Pettigrew DW, Sander EG, Nowak T. Bovine liver dihydropyrimidine amidohydrolase: pH dependencies of the steady-state kinetic and proton relaxation rate properties of the Mn(II)-containing enzyme Archives of Biochemistry and Biophysics. 259: 597-604. PMID 2827580 DOI: 10.1016/0003-9861(87)90526-1  0.433
1986 Hwang SH, Nowak T. Stereochemistry of phosphoenolpyruvate carboxylation catalyzed by phosphoenolpyruvate carboxykinase Biochemistry. 25: 5590-5595. PMID 3778875 DOI: 10.1021/Bi00367A037  0.314
1986 Rohrer SP, Saz HJ, Nowak T. 31P-NMR studies of the metabolisms of the parasitic helminths Ascaris suum and Fasciola hepatica Archives of Biochemistry and Biophysics. 248: 200-209. PMID 3729415 DOI: 10.1016/0003-9861(86)90417-0  0.319
1985 Duffy TH, Nowak T. 1H and 31P relaxation rate studies of the interaction of phosphoenolpyruvate and its analogues with avian phosphoenolpyruvate carboxykinase. Biochemistry. 24: 1152-1160. PMID 4096895 DOI: 10.1021/Bi00326A014  0.413
1985 Lee MH, Goody RS, Nowak T. Guanosine thiophosphate derivatives as substrate analogues for phosphoenolpyruvate carboxykinase. Biochemistry. 24: 7594-7602. PMID 3912004 DOI: 10.1021/Bi00347A014  0.399
1984 Duffy TH, Nowak T. Stereoselectivity of interaction of phosphoenolpyruvate analogues with various phosphoenolpyruvate-utilizing enzymes. Biochemistry. 23: 661-670. PMID 6712918 DOI: 10.1021/Bi00299A012  0.523
1984 Lee MH, Nowak T. Phosphorus-31 nuclear relaxation rate studies of the nucleotides on phosphoenolpyruvate carboxykinase Biochemistry. 23: 6506-6513. PMID 6529566 DOI: 10.1021/Bi00321A036  0.466
1983 Hoving H, Nowak T, Robillard GT. Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: Stereospecificity of proton transfer in the phosphorylation of enzyme I from (Z)-phosphoenolbutyrate Biochemistry. 22: 2832-2838. PMID 6347253 DOI: 10.1021/Bi00281A010  0.401
1982 Baek YH, Nowak T. Kinetic evidence for a dual cation role for muscle pyruvate kinase Archives of Biochemistry and Biophysics. 217: 491-497. PMID 7138020 DOI: 10.1016/0003-9861(82)90529-X  0.486
1981 Nowak T, Maurer PJ. Fluoride inhibition of yeast enolase. 2. Structural and kinetic properties of the ligand complexes determined by nuclear relaxation rate studies Biochemistry. 20: 6901-6911. PMID 7032583 DOI: 10.1021/Bi00527A025  0.41
1981 Maurer PJ, Nowak T. Fluoride inhibition of yeast enolase. 1. Formation of the ligand complexes Biochemistry. 20: 6894-6900. PMID 7032582 DOI: 10.1021/Bi00527A024  0.391
1981 Nowak T, Suelter C. Pyruvate kinase: activation by and catalytic role of the monovalent and divalent cations. Molecular and Cellular Biochemistry. 35: 65-75. PMID 7015112 DOI: 10.1007/Bf02354821  0.48
1979 Robison PD, Nowak T, Levy HR. Magnetic resonance studies of the anthranilate synthetase-phosphoribosyltransferase enzyme complex from Salmonella typhimurium Archives of Biochemistry and Biophysics. 193: 252-263. PMID 222217 DOI: 10.1016/0003-9861(79)90029-8  0.534
1978 Nowak T. The structure of the fluorophosphate-pyruvate kinase complex investigated by 31P relaxation rate studies☆ Archives of Biochemistry and Biophysics. 186: 343-350. PMID 637564 DOI: 10.1016/0003-9861(78)90444-7  0.468
1977 Nowak T, Lee MJ. Reciprocal cooperative effects of multiple ligand binding to pyruvate kinase. Biochemistry. 16: 1343-1350. PMID 557338 DOI: 10.1021/Bi00626A016  0.456
1973 Nowak T, Mildvan AS, Kenyon GL. Nuclear relaxation and kinetic studies of the role of Mn2+ in the mechanism of enolase Biochemistry. 12: 1690-1701. PMID 4572991 DOI: 10.1021/Bi00733A005  0.558
1973 Mildvan AS, Nowak T, Fung CH. Nuclear relaxation studies of the role of the divalent cation in the mechanism of pyruvate kinase and enolase: inner sphere and second sphere complexes Annals of the New York Academy of Sciences. 192-210. PMID 4522427 DOI: 10.1111/J.1749-6632.1973.Tb15261.X  0.59
1972 Nowak T, Mildvan AS. Nuclear magnetic resonance studies of the function of potassium in the mechanism of pyruvate kinase. Biochemistry. 11: 2819-28. PMID 5064959 DOI: 10.1021/Bi00765A014  0.526
1972 Nowak T, Mildvan AS. Nuclear magnetic resonance studies of selectively hindered internal motion of substrate analogs at the active site of pyruvate kinase Biochemistry. 11: 2813-2818. PMID 4625313 DOI: 10.1021/Bi00765A013  0.577
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