W. Wallace Cleland - Publications

Affiliations: 
University of Wisconsin, Madison, Madison, WI 
Area:
Kinetics and mechanisms of enzymes
Website:
http://www.biochem.wisc.edu/faculty/cleland/

122 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
2013 Reinhardt LA, Thoden JB, Peters GS, Holden HM, Cleland WW. pH-rate profiles support a general base mechanism for galactokinase (Lactococcus lactis). Febs Letters. 587: 2876-81. PMID 23872454 DOI: 10.1016/J.Febslet.2013.07.017  1
2012 Thoden JB, Reinhardt LA, Cook PD, Menden P, Cleland WW, Holden HM. Catalytic mechanism of perosamine N-acetyltransferase revealed by high-resolution X-ray crystallographic studies and kinetic analyses. Biochemistry. 51: 3433-44. PMID 22443398 DOI: 10.1021/Bi300197H  1
2012 Smith BC, Anderson MA, Hoadley KA, Keck JL, Cleland WW, Denu JM. Structural and kinetic isotope effect studies of nicotinamidase (Pnc1) from Saccharomyces cerevisiae. Biochemistry. 51: 243-56. PMID 22229411 DOI: 10.1021/Bi2015508  1
2011 Zeczycki TN, Menefee AL, Jitrapakdee S, Wallace JC, Attwood PV, St Maurice M, Cleland WW. Activation and inhibition of pyruvate carboxylase from Rhizobium etli. Biochemistry. 50: 9694-707. PMID 21958066 DOI: 10.1021/Bi201276R  1
2011 Lietzan AD, Menefee AL, Zeczycki TN, Kumar S, Attwood PV, Wallace JC, Cleland WW, St Maurice M. Interaction between the biotin carboxyl carrier domain and the biotin carboxylase domain in pyruvate carboxylase from Rhizobium etli. Biochemistry. 50: 9708-23. PMID 21958016 DOI: 10.1021/Bi201277J  1
2011 Zeczycki TN, Menefee AL, Adina-Zada A, Jitrapakdee S, Surinya KH, Wallace JC, Attwood PV, St Maurice M, Cleland WW. Novel insights into the biotin carboxylase domain reactions of pyruvate carboxylase from Rhizobium etli. Biochemistry. 50: 9724-37. PMID 21957995 DOI: 10.1021/Bi2012788  1
2010 Marlier JF, Robins LI, Tucker KA, Rawlings J, Anderson MA, Cleland WW. A kinetic and isotope effect investigation of the urease-catalyzed hydrolysis of hydroxyurea. Biochemistry. 49: 8213-9. PMID 20695482 DOI: 10.1021/bi100890v  1
2009 Pinto-Tomás AA, Anderson MA, Suen G, Stevenson DM, Chu FS, Cleland WW, Weimer PJ, Currie CR. Symbiotic nitrogen fixation in the fungus gardens of leaf-cutter ants. Science (New York, N.Y.). 326: 1120-3. PMID 19965433 DOI: 10.1126/Science.1173036  0.68
2008 Marlier JF, Fogle EJ, Cleland WW. A heavy-atom isotope effect and kinetic investigation of the hydrolysis of semicarbazide by urease from jack bean (Canavalia ensiformis). Biochemistry. 47: 11158-63. PMID 18817416 DOI: 10.1021/bi801338c  1
2008 Jitrapakdee S, St Maurice M, Rayment I, Cleland WW, Wallace JC, Attwood PV. Structure, mechanism and regulation of pyruvate carboxylase. The Biochemical Journal. 413: 369-87. PMID 18613815 DOI: 10.1042/Bj20080709  1
2008 Van Vleet JL, Reinhardt LA, Miller BG, Sievers A, Cleland WW. Carbon isotope effect study on orotidine 5'-monophosphate decarboxylase: support for an anionic intermediate. Biochemistry. 47: 798-803. PMID 18081312 DOI: 10.1021/Bi701664N  1
2007 St Maurice M, Reinhardt L, Surinya KH, Attwood PV, Wallace JC, Cleland WW, Rayment I. Domain architecture of pyruvate carboxylase, a biotin-dependent multifunctional enzyme. Science (New York, N.Y.). 317: 1076-9. PMID 17717183 DOI: 10.1126/Science.1144504  1
2007 Ralph EC, Hirschi JS, Anderson MA, Cleland WW, Singleton DA, Fitzpatrick PF. Insights into the mechanism of flavoprotein-catalyzed amine oxidation from nitrogen isotope effects on the reaction of N-methyltryptophan oxidase. Biochemistry. 46: 7655-64. PMID 17542620 DOI: 10.1021/Bi700482H  1
2006 Rawlings J, Cleland WW, Hengge AC. Metal-catalyzed phosphodiester cleavage: secondary 18O isotope effects as an indicator of mechanism. Journal of the American Chemical Society. 128: 17120-5. PMID 17177465 DOI: 10.1021/Ja065931A  1
2006 Ralph EC, Anderson MA, Cleland WW, Fitzpatrick PF. Mechanistic studies of the flavoenzyme tryptophan 2-monooxygenase: deuterium and 15N kinetic isotope effects on alanine oxidation by an L-amino acid oxidase. Biochemistry. 45: 15844-52. PMID 17176107 DOI: 10.1021/Bi061894O  1
2006 Cleland WW, Hengge AC. Enzymatic mechanisms of phosphate and sulfate transfer. Chemical Reviews. 106: 3252-78. PMID 16895327 DOI: 10.1021/Cr050287O  1
2006 Anderson MA, Cleland WW, Huang DT, Chan C, Shojaei M, Christopherson RI. 13C and 15N isotope effects for conversion of L-dihydroorotate to N-carbamyl-L-aspartate using dihydroorotase from hamster and Bacillus caldolyticus. Biochemistry. 45: 7132-9. PMID 16752903 DOI: 10.1021/Bi0604025  0.44
2006 Poyner RR, Anderson MA, Bandarian V, Cleland WW, Reed GH. Probing nitrogen-sensitive steps in the free-radical-mediated deamination of amino alcohols by ethanolamine ammonia-lyase. Journal of the American Chemical Society. 128: 7120-1. PMID 16734439 DOI: 10.1021/Ja060710Q  1
2005 Wright SK, DeClue MS, Mandal A, Lee L, Wiest O, Cleland WW, Hilvert D. Isotope effects on the enzymatic and nonenzymatic reactions of chorismate. Journal of the American Chemical Society. 127: 12957-64. PMID 16159290 DOI: 10.1021/Ja052929V  1
2005 Templeton MD, Reinhardt LA, Collyer CA, Mitchell RE, Cleland WW. Kinetic analysis of the L-ornithine transcarbamoylase from Pseudomonas savastanoi pv. phaseolicola that is resistant to the transition state analogue (R)-N delta-(N'-sulfodiaminophosphinyl)-L-ornithine. Biochemistry. 44: 4408-15. PMID 15766270 DOI: 10.1021/Bi047432X  1
2005 Marlier JF, Frey TG, Mallory JA, Cleland WW. Multiple isotope effect study of the acid-catalyzed hydrolysis of methyl formate. The Journal of Organic Chemistry. 70: 1737-44. PMID 15730296 DOI: 10.1021/jo0402733  1
2005 Koropatkin NM, Cleland WW, Holden HM. Kinetic and structural analysis of alpha-D-Glucose-1-phosphate cytidylyltransferase from Salmonella typhi. The Journal of Biological Chemistry. 280: 10774-80. PMID 15634670 DOI: 10.1074/Jbc.M414111200  1
2004 Allard ST, Cleland WW, Holden HM. High resolution X-ray structure of dTDP-glucose 4,6-dehydratase from Streptomyces venezuelae. The Journal of Biological Chemistry. 279: 2211-20. PMID 14570895 DOI: 10.1074/Jbc.M310134200  1
2003 Wright SK, Rishavy MA, Cleland WW. 2H, 13C, and 15N kinetic isotope effects on the reaction of the ammonia-rescued K258A mutant of aspartate aminotransferase. Biochemistry. 42: 8369-76. PMID 12846586 DOI: 10.1021/Bi030092F  1
2003 Sims PA, Larsen TM, Poyner RR, Cleland WW, Reed GH. Reverse protonation is the key to general acid-base catalysis in enolase. Biochemistry. 42: 8298-306. PMID 12846578 DOI: 10.1021/Bi0346345  1
2003 Rawlings J, Cleland WW, Hengge AC. Metal ion catalyzed hydrolysis of ethyl p-nitrophenyl phosphate. Journal of Inorganic Biochemistry. 93: 61-5. PMID 12538053 DOI: 10.1016/S0162-0134(02)00435-X  1
2002 Snider MJ, Reinhardt L, Wolfenden R, Cleland WW. 15N kinetic isotope effects on uncatalyzed and enzymatic deamination of cytidine. Biochemistry. 41: 415-21. PMID 11772041 DOI: 10.1021/Bi011410I  1
2001 Lee LV, Gerratana B, Cleland WW. Substrate specificity and kinetic mechanism of Escherichia coli ribulokinase. Archives of Biochemistry and Biophysics. 396: 219-24. PMID 11747300 DOI: 10.1006/abbi.2001.2613  1
2001 Rishavy MA, Yang Z, Tong L, Cleland WW. Determination of the mechanism of human malic enzyme with natural and alternate dinucleotides by isotope effects. Archives of Biochemistry and Biophysics. 396: 43-8. PMID 11716460 DOI: 10.1006/Abbi.2001.2598  0.4
2001 Anderson MA, Shim H, Raushel FM, Cleland WW. Hydrolysis of phosphotriesters: determination of transition states in parallel reactions by heavy-atom isotope effects. Journal of the American Chemical Society. 123: 9246-53. PMID 11562204 DOI: 10.1021/Ja011025G  1
2001 Gerratana B, Cleland WW, Frey PA. Mechanistic roles of Thr134, Tyr160, and Lys 164 in the reaction catalyzed by dTDP-glucose 4,6-dehydratase. Biochemistry. 40: 9187-95. PMID 11478886 DOI: 10.1021/Bi0108249  1
2001 Poyner RR, Cleland WW, Reed GH. Role of metal ions in catalysis by enolase: an ordered kinetic mechanism for a single substrate enzyme. Biochemistry. 40: 8009-17. PMID 11434770 DOI: 10.1021/Bi0103922  1
2001 Neidhart D, Wei Y, Cassidy C, Lin J, Cleland WW, Frey PA. Correlation of low-barrier hydrogen bonding and oxyanion binding in transition state analogue complexes of chymotrypsin. Biochemistry. 40: 2439-47. PMID 11327865 DOI: 10.1021/Bi002535A  1
2001 Gerratana B, Frey PA, Cleland WW. Characterization of the transition-state structure of the reaction of kanamycin nucleotidyltransferase by heavy-atom kinetic isotope effects. Biochemistry. 40: 2972-7. PMID 11258909 DOI: 10.1021/Bi002557X  1
2001 Gerratana B, Cleland WW, Reinhardt LA. Regiospecificity assignment for the reaction of kanamycin nucleotidyltransferase from Staphylococcus aureus. Biochemistry. 40: 2964-71. PMID 11258908 DOI: 10.1021/bi0025565  1
2000 Rishavy MA, Hengge AC, Cleland WW. Lanthanide Catalyzed Cyclization of Uridine 3'-p-Nitrophenyl Phosphate. Bioorganic Chemistry. 28: 283-292. PMID 11133147 DOI: 10.1006/Bioo.2000.1179  1
2000 Hengge AC, Bruzik KS, Tobin AE, Cleland WW, Tsai MD. Kinetic Isotope Effects and Stereochemical Studies on a Ribonuclease Model: Hydrolysis Reactions of Uridine 3'-Nitrophenyl Phosphate. Bioorganic Chemistry. 28: 119-133. PMID 10915550 DOI: 10.1006/Bioo.2000.1170  1
2000 Rishavy MA, Cleland WW. 13C and (15)N kinetic isotope effects on the reaction of aspartate aminotransferase and the tyrosine-225 to phenylalanine mutant. Biochemistry. 39: 7546-51. PMID 10858304 DOI: 10.1021/Bi000458D  0.4
2000 Rishavy MA, Cleland WW, Lusty CJ. 15N isotope effects in glutamine hydrolysis catalyzed by carbamyl phosphate synthetase: evidence for a tetrahedral intermediate in the mechanism. Biochemistry. 39: 7309-15. PMID 10852731 DOI: 10.1021/Bi000435Z  0.4
2000 Rishavy MA, Cleland WW. Determination of the mechanism of orotidine 5'-monophosphate decarboxylase by isotope effects. Biochemistry. 39: 4569-74. PMID 10769111  0.4
2000 Gerratana B, Sowa GA, Cleland WW. Characterization of the transition-state structures and mechanisms for the isomerization and cleavage reactions of uridine 3′-m-nitrobenzyl phosphate Journal of the American Chemical Society. 122: 12615-12621. DOI: 10.1021/ja003400v  1
2000 Kurtz KA, Rishavy MA, Cleland WW, Fitzpatrick PF. Nitrogen isotope effects as probes of the mechanism of D-amino acid oxidase [17] Journal of the American Chemical Society. 122: 12896-12897. DOI: 10.1021/Ja002528+  1
1999 Cassidy CS, Reinhardt LA, Cleland WW, Frey PA. Hydrogen bonding in complexes of carboxylic acids with 1-alkylimidazoles: Steric and isotopic effects on low barrier hydrogen bonding Journal of the Chemical Society. Perkin Transactions 2. 635-641. DOI: 10.1039/A806387G  1
1998 Urbauer JL, Bradshaw DE, Cleland WW. Determination of the kinetic and chemical mechanism of malic enzyme using (2R,3R)-erythro-fluoromalate as a slow alternate substrate. Biochemistry. 37: 18026-31. PMID 9922171 DOI: 10.1021/Bi981820F  0.48
1998 Urbauer JL, Bradshaw DE, Cleland WW. Synthesis of (2R,3R)-erythro- and (2R,3S)-threo-fluoromalate using malic dehydrogenase; stereoselectivity of malic dehydrogenase. Biochemistry. 37: 18018-25. PMID 9922170 DOI: 10.1021/Bi981819G  0.48
1998 Lin J, Westler WM, Cleland WW, Markley JL, Frey PA. Fractionation factors and activation energies for exchange of the low barrier hydrogen bonding proton in peptidyl trifluoromethyl ketone complexes of chymotrypsin. Proceedings of the National Academy of Sciences of the United States of America. 95: 14664-8. PMID 9843946 DOI: 10.1073/Pnas.95.25.14664  1
1998 Cleland WW, Frey PA, Gerlt JA. The low barrier hydrogen bond in enzymatic catalysis. The Journal of Biological Chemistry. 273: 25529-32. PMID 9748211 DOI: 10.1074/Jbc.273.40.25529  1
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  1
1998 Hess RA, Hengge AC, Cleland WW. Isotope effects on enzyme-catalyzed acyl transfer from p-nitrophenyl acetate: Concerted mechanisms and increased hyperconjugation in the transition state Journal of the American Chemical Society. 120: 2703-2709. DOI: 10.1021/Ja973413H  1
1998 Frey PA, Cleland WW. Are there strong hydrogen bonds in aqueous solutions? Bioorganic Chemistry. 26: 175-192. DOI: 10.1006/Bioo.1998.1097  1
1998 Cleland WW, Andrews TJ, Gutteridge S, Hartman FC, Lorimer GH. Mechanism of rubisco: The carbamate as general base Chemical Reviews. 98: 549-561.  1
1997 Edens WA, Urbauer JL, Cleland WW. Determination of the chemical mechanism of malic enzyme by isotope effects. Biochemistry. 36: 1141-7. PMID 9033405 DOI: 10.1021/Bi962128S  0.48
1997 Hess RA, Hengge AC, Cleland WW. Kinetic isotope effects for acyl transfer from p-nitrophenyl acetate to hydroxylamine show a pH-dependent change in mechanism Journal of the American Chemical Society. 119: 6980-6983. DOI: 10.1021/Ja970648K  1
1997 Sowa GA, Hengge AC, Cleland WW. 18O isotope effects support a concerted mechanism for ribonuclease A Journal of the American Chemical Society. 119: 2319-2320. DOI: 10.1021/ja963974t  1
1997 Rawlings J, Hengge AC, Cleland WW. Heavy-atom isotope effects on reactions of Co(III)-bound p-nitrophenyl phosphate: Nucleophilic displacements of p-nitrophenol and dissociation of p-nitrophenyl phosphate Journal of the American Chemical Society. 119: 542-549. DOI: 10.1021/Ja962448Z  1
1996 Sculley MJ, Morrison JF, Cleland WW. Slow-binding inhibition: the general case. Biochimica Et Biophysica Acta. 1298: 78-86. PMID 8948491 DOI: 10.1016/S0167-4838(96)00118-5  1
1995 Cleland WW, Hengge AC. Mechanisms of phosphoryl and acyl transfer. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 9: 1585-94. PMID 8529838 DOI: 10.1096/Fasebj.9.15.8529838  1
1994 Waldrop GL, Braxton BF, Urbauer JL, Cleland WW, Kiick DM. Secondary 18O and primary 13C isotope effects as a probe of transition-state structure for enzymatic decarboxylation of oxalacetate. Biochemistry. 33: 5262-7. PMID 8172901 DOI: 10.1021/Bi00183A032  1
1994 Cleland WW, Kreevoy MM. Low-barrier hydrogen bonds and enzymic catalysis. Science (New York, N.Y.). 264: 1887-90. PMID 8009219 DOI: 10.1126/Science.8009219  1
1993 Rawlings J, Speckhard DC, Cleland WW. Characterization of isomers of monoamminechromium-ATP and their use in mapping enzyme active sites. Biochemistry. 32: 11204-10. PMID 8218184  0.56
1992 Parmentier LE, O'Leary MH, Schachman HK, Cleland WW. 13C isotope effect studies of Escherichia coli aspartate transcarbamylase in the presence of the bisubstrate analog N-(phosphonoacetyl)-L-aspartate. Biochemistry. 31: 6598-602. PMID 1633172 DOI: 10.1021/Bi00143A033  1
1992 Waldrop GL, Turnbull JL, Parmentier LE, Lee S, O'Leary MH, Cleland WW, Schachman HK. The contribution of threonine 55 to catalysis in aspartate transcarbamoylase. Biochemistry. 31: 6592-7. PMID 1633171 DOI: 10.1021/Bi00143A032  1
1992 Waldrop GL, Turnbull JL, Parmentier LE, O'Leary MH, Cleland WW, Schachman HK. Steady-state kinetics and isotope effects on the mutant catalytic trimer of aspartate transcarbamoylase containing the replacement of histidine 134 by alanine. Biochemistry. 31: 6585-91. PMID 1633170 DOI: 10.1021/Bi00143A031  1
1992 Parmentier LE, Weiss PM, O'Leary MH, Schachman HK, Cleland WW. 13C and 15N isotope effects as a probe of the chemical mechanism of Escherichia coli aspartate transcarbamylase. Biochemistry. 31: 6577-84. PMID 1633169 DOI: 10.1021/Bi00143A030  1
1992 Parmentier LE, O'Leary MH, Schachman HK, Cleland WW. 13C isotope effects as a probe of the kinetic mechanism and allosteric properties of Escherichia coli aspartate transcarbamylase. Biochemistry. 31: 6570-6. PMID 1633168 DOI: 10.1021/Bi00143A029  1
1992 Janc JW, Urbauer JL, O'Leary MH, Cleland WW. Mechanistic studies of phosphoenolpyruvate carboxylase from Zea mays with (Z)- and (E)-3-fluorophosphoenolpyruvate as substrates. Biochemistry. 31: 6432-40. PMID 1633157 DOI: 10.1021/Bi00143A011  0.48
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  0.48
1991 Jones JP, Weiss PM, Cleland WW. Secondary 18O isotope effects for hexokinase-catalyzed phosphoryl transfer from ATP. Biochemistry. 30: 3634-9. PMID 2015221  0.48
1991 Turnbull J, Morrison JF, Cleland WW. Kinetic studies on chorismate mutase-prephenate dehydrogenase from Escherichia coli: models for the feedback inhibition of prephenate dehydrogenase by L-tyrosine. Biochemistry. 30: 7783-8. PMID 1868056 DOI: 10.1021/Bi00245A017  0.72
1991 Turnbull J, Cleland WW, Morrison JF. pH dependency of the reactions catalyzed by chorismate mutase-prephenate dehydrogenase from Escherichia coli. Biochemistry. 30: 7777-82. PMID 1868055 DOI: 10.1021/Bi00245A016  0.72
1991 Caldwell SR, Raushel FM, Weiss PM, Cleland WW. Transition-state structures for enzymatic and alkaline phosphotriester hydrolysis. Biochemistry. 30: 7444-50. PMID 1649629 DOI: 10.1021/Bi00244A011  0.96
1991 Knight WB, Sem DS, Smith K, Miziorko HM, Rendina AR, Cleland WW. Phosphorylated thiosugars: synthesis, properties, and reactivity in enzymatic reactions. Biochemistry. 30: 4970-7. PMID 1645186  1
1990 Anderson VE, Cleland WW. Phosphonate analogue substrates for enolase. Biochemistry. 29: 10498-503. PMID 2271661  0.76
1990 Turnbull J, Cleland WW, Morrison JF. Chorismate mutase-prephenate dehydrogenase from Escherichia coli. 1. Kinetic characterization of the dehydrogenase reaction by use of alternative substrates. Biochemistry. 29: 10245-54. PMID 2271652 DOI: 10.1021/Bi00496A014  0.72
1990 Haromy TP, Rawlings J, Cleland WW, Sundaralingam M. Structures of the monohydrate and dihydrate of (bidentate pyrophosphato) trans-diammine cis-diaqua chromium (III). Acta Crystallographica. Section C, Crystal Structure Communications. 46: 2369-74. PMID 1964789 DOI: 10.1107/S0108270190005947  1
1989 Kiick DM, Cleland WW. Steady-state kinetic studies of the metal ion-dependent decarboxylation of oxalacetate catalyzed by pyruvate kinase. Archives of Biochemistry and Biophysics. 270: 647-54. PMID 2705784  0.48
1989 Weiss PM, Boerner RJ, Cleland WW. Enzymatic synthesis and inhibitory characteristics of tartronate semialdehyde phosphate. Biochemistry. 28: 1634-41. PMID 2655697  0.48
1989 Knight WB, Cleland WW. Thiol and amino analogues as alternate substrates for glycerokinase from Candida mycoderma. Biochemistry. 28: 5728-34. PMID 2550062  1
1989 Speckhard DC, Knight WB, Rawlings J, Cleland WW. Triamminemonoaquocobalt(III) complexes of pyrophosphate and adenosine diphosphate (ADP). Journal of Inorganic Biochemistry. 36: 99-106. PMID 2547896 DOI: 10.1016/0162-0134(89)80017-0  1
1988 Grissom CB, Cleland WW. Isotope effect studies of the chemical mechanism of pig heart NADP isocitrate dehydrogenase. Biochemistry. 27: 2934-43. PMID 3401457  1
1988 Grissom CB, Cleland WW. Isotope effect studies of chicken liver NADP malic enzyme: role of the metal ion and viscosity dependence. Biochemistry. 27: 2927-34. PMID 3401456  1
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  1
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  1
1987 Grissom CB, Cleland WW. 2-Keto-3-fluoroglutarate: a useful mechanistic probe of 2-keto-glutarate-dependent enzyme systems. Biochimica Et Biophysica Acta. 916: 437-45. PMID 2891378 DOI: 10.1016/0167-4838(87)90190-7  1
1985 Grissom CB, Cleland WW. Use of intermediate partitioning to calculate intrinsic isotope effects for the reaction catalyzed by malic enzyme. Biochemistry. 24: 944-8. PMID 3995001  1
1985 Hermes JD, Weiss PM, Cleland WW. Use of nitrogen-15 and deuterium isotope effects to determine the chemical mechanism of phenylalanine ammonia-lyase Biochemistry. 24: 2959-2967. PMID 3893533 DOI: 10.1021/bi00333a023  1
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  1
1985 Pecoraro VL, Rendina AR, Cleland WW. Determination of the screw sense specificity of bovine liver fructokinase. Biochemistry. 24: 1619-22. PMID 2988605 DOI: 10.1021/Bi00328A008  0.64
1984 Pecoraro VL, Rawlings J, Cleland WW. Investigation of substrate specificity of creatine kinase using chromium (III) and cobalt(III) complexes of adenosine 5'-diphosphate. Biochemistry. 23: 153-8. PMID 6546349 DOI: 10.1021/Bi00296A025  1
1984 Weiss PM, Hermes JD, Dougherty TM, Cleland WW. N-hydroxycarbamate is the substrate for the pyruvate kinase catalyzed phosphorylation of hydroxylamine Biochemistry. 23: 4346-4350. PMID 6487603 DOI: 10.1021/bi00314a015  1
1984 Hermes JD, Tipton PA, Fisher MA, O'Leary MH, Morrison JF, Cleland WW. Mechanisms of enzymatic and acid-catalyzed decarboxylations of prephenate. Biochemistry. 23: 6263-75. PMID 6395898 DOI: 10.1021/bi00320a057  0.72
1984 Rendina AR, Hermes JD, Cleland WW. Use of multiple isotope effects to study the mechanism of 6-phosphogluconate dehydrogenase Biochemistry. 23: 6257-6262. PMID 6395897 DOI: 10.1021/bi00320a056  1
1984 Hermes JD, Morrical SW, O'Leary MH, Cleland WW. Variation of transition-state structure as a function of the nucleotide in reactions catalyzed by dehydrogenases. 2. Formate dehydrogenase Biochemistry. 23: 5479-5488. PMID 6391544 DOI: 10.1021/Bi00318A016  1
1984 Anderson VE, Weiss PM, Cleland WW. Reaction intermediate analogues for enolase. Biochemistry. 23: 2779-86. PMID 6380574 DOI: 10.1021/Bi00307A038  0.76
1984 Pecoraro VL, Hermes JD, Cleland WW. Stability constants of Mg2+ and Cd2+ complexes of adenine nucleotides and thionucleotides and rate constants for formation and dissociation of MgATP and MgADP. Biochemistry. 23: 5262-71. PMID 6334536  1
1984 Rendina AR, Hermes JD, Cleland WW. A novel method for determining rate constants for dehydration of aldehyde hydrates Biochemistry. 23: 5148-5156. PMID 6095890 DOI: 10.1021/bi00317a011  1
1982 Viola RE, Cleland WW. Initial velocity analysis for terreactant mechanisms. Methods in Enzymology. 87: 353-66. PMID 7176920 DOI: 10.1016/S0076-6879(82)87021-3  1
1982 Hermes JD, Roeske CA, O'Leary MH, Cleland WW. Use of multiple isotope effects to determine enzyme mechanisms and intrinsic isotope effects. Malic enzyme and glucose-6-phosphate dehydrogenase Biochemistry. 21: 5106-5114. PMID 7138850 DOI: 10.1021/bi00263a040  1
1982 Viola RE, Raushel FM, Rendina AR, Cleland WW. Substrate synergism and the kinetic mechanism of yeast hexokinase. Biochemistry. 21: 1295-302. PMID 7041974 DOI: 10.1021/Bi00535A029  1
1981 Ramsay RR, Dreyer JL, Schloss JV, Jackson RH, Coles CJ, Beinert H, Cleland WW, Singer TP. Relationship of the oxidation state of the iron-sulfur cluster of aconitase to activity and substrate binding. Biochemistry. 20: 7476-82. PMID 7326240 DOI: 10.1021/Bi00529A023  1
1981 Cook PF, Kenyon GL, Cleland WW. Use of pH studies to elucidate the catalytic mechanism of rabbit muscle creatine kinase. Biochemistry. 20: 1204-10. PMID 7013788 DOI: 10.1021/Bi00508A023  1
1980 Blanchard JS, Cleland WW. Use of isotope effects to deduce the chemical mechanism of fumarase. Biochemistry. 19: 4506-13. PMID 7407088  1
1980 Dunaway-Mariano D, Cleland WW. Preparation and properties of chromium(III) adenosine 5′-triphosphate, chromium(III) adenosine 5′-diphosphate, and related chromium(III) complexes Biochemistry. 19: 1496-1505. PMID 7053080 DOI: 10.1021/Bi00548A037  1
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  1
1980 Blanchard JS, Cleland WW. Kinetic and chemical mechanisms of yeast formate dehydrogenase. Biochemistry. 19: 3543-50. PMID 6996706  1
1980 Viola RE, Morrison JF, Cleland WW. Interaction of metal(III)-adenosine 5'-triphosphate complexes with yeast hexokinase. Biochemistry. 19: 3131-7. PMID 6996699 DOI: 10.1021/Bi00555A003  1
1980 Dunaway-Mariano D, Cleland WW. Investigations of substrate specificity and reaction mechanism of several kinases using chromium(III) adenosine 5′-triphosphate and chromium(III) adenosine 5′-diphosphate Biochemistry. 19: 1506-1515. PMID 6248105 DOI: 10.1021/Bi00548A038  1
1980 Viola RE, Cleland WW. Aldehyde-induced adenosine triphosphatase activities of fructose 6-phosphate and fructose kinases. Biochemistry. 19: 1861-6. PMID 6246937 DOI: 10.1021/Bi00550A600  1
1979 Dunaway-Mariano D, Benovic JL, Cleland WW, Gupta RK, Mildvan AS. Stereospecificity of the metal-adenosine 5′-triphosphate complex in reactions of muscle pyruvate kinase Biochemistry. 18: 4347-4354. PMID 486426 DOI: 10.1021/Bi00587A013  1
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  1
1978 Viola RE, Cleland WW. Use of pH studies to elucidate the chemical mechanism of yeast hexokinase. Biochemistry. 17: 4111-7. PMID 30473 DOI: 10.1021/Bi00613A001  1
1977 Schimerlik MI, Cleland WW. Inhibition and alternate-substrate studies on the mechanism of malic enzyme. Biochemistry. 16: 565-70. PMID 836801 DOI: 10.1021/Bi00623A001  1
1977 Raushel FM, Cleland WW. Bovine liver fructokinase: purification and kinetic properties. Biochemistry. 16: 2169-75. PMID 193556 DOI: 10.1021/Bi00629A020  0.96
1977 Raushel FM, Cleland WW. Determination of the rate-limiting steps and chemical mechanism of fructokinase by isotope exchange, isotope partitioning, and pH studies. Biochemistry. 16: 2176-81. PMID 16640 DOI: 10.1021/Bi00629A021  0.96
1977 Schimerlik MI, Grimshaw CE, Cleland WW. Determination of the rate-limiting steps for malic enzyme by the use of isotope effects and other kinetic studies. Biochemistry. 16: 571-6. PMID 13820 DOI: 10.1021/Bi00623A002  1
1975 Schimerlik MI, Rife JE, Cleland WW. Equilibrium perturbation by isotope substitution. Biochemistry. 14: 5347-54. PMID 1191642 DOI: 10.1021/Bi00695A020  1
1974 Santi DV, Webster RW, Cleland WW. [49] Kinetics of aminoacyl-tRNA synthetases catalyzed ATP-PPi exchange Methods in Enzymology. 29: 620-627. PMID 4368856 DOI: 10.1016/0076-6879(74)29054-2  1
1973 DePamphilis ML, Cleland WW. Preparation and properties of chromium (3)-nucleotide complexes for use in the study of enzyme mechanisms. Biochemistry. 12: 3714-24. PMID 4596147 DOI: 10.1021/bi00743a022  1
1973 Raushel FM, Cleland WW. The substrate and anomeric specificity of fructokinase. The Journal of Biological Chemistry. 248: 8174-7. PMID 4356621  0.96
1964 Henson CP, Cleland WW. Kinetic studies of glutamic oxaloacetic transaminase isozymes Biochemistry. 3: 338-345. PMID 14155095 DOI: 10.1021/bi00891a007  1
1956 CLELAND WW, JOHNSON MJ. Studies on the formation of oxalic acid by Aspergillus niger. The Journal of Biological Chemistry. 220: 595-606. PMID 13331918  1
1954 CLELAND WW, JOHNSON MJ. Tracer experiments on the mechanism of citric acid formation by Aspergillus niger. The Journal of Biological Chemistry. 208: 679-89. PMID 13174578  1
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