W. Cleland

发表

The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations.

W. Cleland, 1963, Biochimica et biophysica acta.

Carbon-13 and deuterium isotope effects on the reaction catalyzed by glyceraldehyde-3-phosphate dehydrogenase.

W. Cleland, P. Canellas, 1991, Biochemistry.

Kinetic studies on chorismate mutase-prephenate dehydrogenase from Escherichia coli: models for the feedback inhibition of prephenate dehydrogenase by L-tyrosine.

J. Morrison, W. Cleland, J. Turnbull, 1991, Biochemistry.

pH dependency of the reactions catalyzed by chorismate mutase-prephenate dehydrogenase from Escherichia coli.

J. Morrison, W. Cleland, J. Turnbull, 1991, Biochemistry.

Use of nitrogen-15 and deuterium isotope effects to determine the chemical mechanism of phenylalanine ammonia-lyase.

W. Cleland, J. Hermes, P. Weiss, 1985, Biochemistry.

DITHIOTHREITOL, A NEW PROTECTIVE REAGENT FOR SH GROUPS.

W. Cleland, 1964, Biochemistry.

Rabbit muscle phosphofructokinase. I. Anomeric specificity; initial velocity kinetics.

W. Cleland, J. Bar-Tana, 1974, The Journal of biological chemistry.

Stereoselective preparation of deuterated reduced nicotinamide adenine nucleotides and substrates by enzymatic synthesis.

W. Cleland, P. Cook, R. Viola, 1979, Analytical biochemistry.

Symbiotic Nitrogen Fixation in the Fungus Gardens of Leaf-Cutter Ants

David M. Stevenson, Paul J. Weimer, Cameron R. Currie, 2009, Science.

The statistical analysis of enzyme kinetic data.

W. Cleland, W W Cleland, 1967, Advances in enzymology and related areas of molecular biology.

Probing the allosteric activation of pyruvate carboxylase using 2',3'-O-(2,4,6-trinitrophenyl) adenosine 5'-triphosphate as a fluorescent mimic of the allosteric activator acetyl CoA.

W. Cleland, J. Wallace, S. Jitrapakdee, 2011, Archives of biochemistry and biophysics.

The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations. 1963.

W. Cleland, W W Cleland, 1989, Biochimica et biophysica acta.

Catalytic mechanism of perosamine N-acetyltransferase revealed by high-resolution X-ray crystallographic studies and kinetic analyses.

W. Cleland, J. Thoden, H. Holden, 2012, Biochemistry.

Novel insights into the biotin carboxylase domain reactions of pyruvate carboxylase from Rhizobium etli.

W. Cleland, J. Wallace, S. Jitrapakdee, 2011, Biochemistry.

Domain Architecture of Pyruvate Carboxylase, a Biotin-Dependent Multifunctional Enzyme

I. Rayment, W. Cleland, J. Wallace, 2007, Science.

Bimodal substrate inhibition of lactate dehydrogenase. Factors affecting the enzyme in vivo.

W. Cleland, W. Ray, J. Burgner, 1978, Biochemistry.

A kinetic and isotope effect investigation of the urease-catalyzed hydrolysis of hydroxyurea.

W. Cleland, Lori I Robins, Mark A. Anderson, 2010, Biochemistry.

Kinetic and chemical mechanisms of yeast formate dehydrogenase.

W. Cleland, J. Blanchard, 1980, Biochemistry.

Nitrogen isotope effects as probes of the mechanism of D-amino acid oxidase [17]

W. Cleland, P. F. Fitzpatrick, K. Kurtz, 2000 .

Low-barrier hydrogen bonds and enzymatic catalysis.

W. Cleland, 2000, Archives of biochemistry and biophysics.

Metal ion catalyzed hydrolysis of ethyl p-nitrophenyl phosphate.

W. Cleland, A. Hengge, J. Rawlings, 2003, Journal of inorganic biochemistry.

The kinetics of pig heart triphosphopyridine nucleotide-isocitrate dehydrogenase. I. Initial velocity, substrate and product inhibition, and isotope exchange studies.

V. W. Thompson, W. Cleland, M. Uhr, 1974, The Journal of biological chemistry.

Isotope effects on the enzymatic and nonenzymatic reactions of chorismate.

D. Hilvert, O. Wiest, W. Cleland, 2005, Journal of the American Chemical Society.

Mechanism of Rubisco: The Carbamate as General Base

F. C. Hartman, W. Cleland, G. Lorimer, 1998 .

Symmetry and asymmetry in mandelate racemase catalysis.

G. L. Kenyon, W. Cleland, G. Hegeman, 1985, Biochemistry.

Inhibition of creatine kinase by chromium nucleotides.

W. Cleland, M. Schimerlik, 1973, The Journal of biological chemistry.

Enzyme kinetics: by Irwin H. Segel, published by Wiley and Sons, New York, £17.05 ($34.10) (xxii + 957 pages)

W. Cleland, D. Northrop, 1976 .

PRODUCT INHIBITION STUDIES ON YEAST AND LIVER ALCOHOL DEHYDROGENASES.

W. Cleland, C. C. Wratten, 1963, Biochemistry.

Determination of the mechanism of orotidine 5'-monophosphate decarboxylase by isotope effects.

W. Cleland, M. Rishavy, 2000, Biochemistry.

Mechanisms of phosphoryl and acyl transfer

W. Cleland, A. Hengge, 1995, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Secondary 15N isotope effects on the reactions catalyzed by alcohol and formate dehydrogenases.

W. Cleland, N. S. Rotberg, 1991, Biochemistry.

1,4‐Dithiothreitol

W. Cleland, 2001 .

The inhibition of acetate, pyruvate, and 3-phosphogylcerate kinases by chromium adenosine triphosphate.

W. Cleland, C. Janson, 1974, The Journal of biological chemistry.

Measurement of isotope effects by the equilibrium perturbation technique.

W. Cleland, 1980, Methods in enzymology.

Use of pH studies to elucidate the chemical mechanism of yeast hexokinase.

W. Cleland, R. Viola, 1978, Biochemistry.

Some physical properties of palmityl-coenzyme A micelles.

W. Cleland, R. E. Barden, W. Zahler, 1968, Biochimica et biophysica acta.

Purification and mechanism of action of hog liver mevalonic kinase.

W. Cleland, J. Porter, J. Marr, 1970, The Journal of biological chemistry.

13C isotope effects as a probe of the kinetic mechanism and allosteric properties of Escherichia coli aspartate transcarbamylase.

W. Cleland, H. K. Schachman, M. O'Leary, 1992, Biochemistry.

Aldehyde-induced adenosine triphosphatase activities of fructose 6-phosphate and fructose kinases.

W. Cleland, R. Viola, 1980, Biochemistry.

Use of pH studies to elucidate the catalytic mechanism of rabbit muscle creatine kinase.

G. L. Kenyon, W. Cleland, P. Cook, 1981, Biochemistry.

Kinetic and Structural Analysis of α-d-Glucose-1-phosphate Cytidylyltransferase from Salmonella typhi*

W. Cleland, H. Holden, N. Koropatkin, 2005, Journal of Biological Chemistry.

Isotope exchange studies of the mechanism of the reaction catalyzed by adenosine triphosphate: creatine phosphotransferase.

J. Morrison, W. Cleland, 1966, The Journal of biological chemistry.

A kinetic investigation of phosphoenolpyruvate carboxylase from Zea mays.

W. Cleland, M. O'Leary, J. Janc, 1992, Biochemistry.

Mechanistic studies of phosphoenolpyruvate carboxylase from Zea mays utilizing formate as an alternate substrate for bicarbonate.

W. Cleland, M. O'Leary, J. Janc, 1992, Biochemistry.

Mechanistic studies of phosphoenolpyruvate carboxylase from Zea mays with (Z)- and (E)-3-fluorophosphoenolpyruvate as substrates.

W. Cleland, M. O'Leary, J. Urbauer, 1992, Biochemistry.

Stereospecificity of the metal--adenosine 5'-triphosphate complex in reactions of muscle pyruvate kinase.

A. Mildvan, W. Cleland, D. Dunaway-Mariano, 1979, Biochemistry.

Allosteric regulation of the biotin-dependent enzyme pyruvate carboxylase by acetyl-CoA.

W. Cleland, S. Jitrapakdee, P. Attwood, 2012, Biochemical Society transactions.

Secondary 18O isotope effects for hexokinase-catalyzed phosphoryl transfer from ATP.

Jeffrey P. Jones, W. Cleland, J. Jones, 1991, Biochemistry.

Conserved Glu40 and Glu433 of the biotin carboxylase domain of yeast pyruvate carboxylase I isoenzyme are essential for the association of tetramers.

G. Booker, W. Cleland, J. Wallace, 2007, The international journal of biochemistry & cell biology.

Regiospecificity assignment for the reaction of kanamycin nucleotidyltransferase from Staphylococcus aureus.

W. Cleland, B. Gerratana, L. Reinhardt, 2001, Biochemistry.

N-hydroxycarbamate is the substrate for the pyruvate kinase catalyzed phosphorylation of hydroxylamine.

W. Cleland, J. Hermes, P. Weiss, 1984, Biochemistry.

Alkaline phosphatase catalyzes the hydrolysis of glucose-6-phosphate via a dissociative mechanism

W. Cleland, P. Weiss, 1989 .

Reverse protonation is the key to general acid-base catalysis in enolase.

G. H. Reed, W. Cleland, P. Sims, 2003, Biochemistry.

A specific and sensitive assay for disulfides.

W. Cleland, W. Zahler, 1968, The Journal of biological chemistry.

The kinetics of pig heart triphosphopyridine nucleotide-isocitrate dehydrogenase. II. Dead-end and multiple inhibition studies.

W. Cleland, D. Northrop, 1974, The Journal of biological chemistry.

Determination of the chemical mechanism of glutamate dehydrogenase from pH studies.

W. Cleland, J. Rifé, 1980, Biochemistry.

Investigations of substrate specificity and reaction mechanism of several kinases using chromium(III) adenosine 5'-triphosphate and chromium(III) adenosine 5'-diphosphate.

W. Cleland, D. Dunaway-Mariano, 1980, Biochemistry.

Investigating the roles of putative active site residues in the oxalate decarboxylase from Bacillus subtilis.

W. Cleland, N. Richards, L. Reinhardt, 2007, Archives of biochemistry and biophysics.

Mechanistic studies of the flavoenzyme tryptophan 2-monooxygenase: deuterium and 15N kinetic isotope effects on alanine oxidation by an L-amino acid oxidase.

W. Cleland, Mark A. Anderson, P. Fitzpatrick, 2006, Biochemistry.

Heavy atom isotope effects on the reaction catalyzed by the oxalate decarboxylase from Bacillus subtilis.

Christopher H. Chang, W. Cleland, N. Richards, 2003, Journal of the American Chemical Society.

Phosphonate analogue substrates for enolase.

W. Cleland, V. Anderson, 1990, Biochemistry.

Use of isotope effects to deduce the chemical mechanism of fumarase.

W. Cleland, J. Blanchard, 1980, Biochemistry.

Initial Rate Enzyme Kinetics.Herbert J. Fromm

W. Cleland, 1977 .

Probing the catalytic roles of Arg548 and Gln552 in the carboxyl transferase domain of the Rhizobium etli pyruvate carboxylase by site-directed mutagenesis.

W. Cleland, J. Wallace, S. Jitrapakdee, 2010, Biochemistry.

Inhibition of isocitrate lyase by 3-nitropropionate, a reaction-intermediate analogue.

W. Cleland, J. Schloss, 1982, Biochemistry.

The effect of oligomeric environment on the kinetics of lactate dehydrogenase subunits.

W. Cleland, G. Ainslie, 1982, Archives of biochemistry and biophysics.

The enzymatic synthesis of psychosine.

E. P. Kennedy, W. Cleland, 1960, The Journal of biological chemistry.

Thiol and amino analogues as alternate substrates for glycerokinase from Candida mycoderma.

W. Cleland, W. Knight, 1989, Biochemistry.

Isotope effects on enzyme-catalyzed reactions : [proceedings of the Sixth Annual Harry Steenbock Symposium, held in Madison, Wisconsin, on June 4 and 5, 1976]

W. Cleland, M. O'Leary, D. Northrop, 1977 .

Substrate specificity and kinetic mechanism of Escherichia coli ribulokinase.

W. Cleland, B. Gerratana, L. V. Lee, 2001, Archives of biochemistry and biophysics.

Kinetic competence of enzymic intermediates: fact or fiction?

W. Cleland, 1990, Biochemistry.

13C isotope effect on the reaction catalyzed by prephenate dehydratase.

D. Hilvert, P. Kast, W. Cleland, 2010, Biochimica et biophysica acta.

Determination of the chemical mechanism of malic enzyme by isotope effects.

W. Cleland, W. Edens, J. Urbauer, 1997, Biochemistry.

Studies on the formation of oxalic acid by Aspergillus niger.

W. Cleland, M. J. Johnson, 1956, The Journal of biological chemistry.

Partition analysis and the concept of net rate constants as tools in enzyme kinetics.

W. Cleland, 1975, Biochemistry.

Structure, mechanism and regulation of pyruvate carboxylase.

I. Rayment, W. Cleland, J. Wallace, 2008, The Biochemical journal.

Statistical analysis of enzyme kinetic data.

W. Cleland, W W Cleland, 2006, Methods in enzymology.

1-Acylglycerol 3-phosphate acyltransferase from rat liver.

W. Cleland, R. E. Barden, 1969, The Journal of biological chemistry.

Enzyme kinetics revisited: a commentaryon “The kinetics of enzyme-catalyzed reactions with two or more substrates or products’ by W.W. Cleland Biochim. Biophys. Acta 67 (1963) 104 ff. with Biochim. Biophys. Acta 67 (1963) 173, 188 (summaries)

W. Cleland, 1989 .

Transition-state structures for enzymatic and alkaline phosphotriester hydrolysis.

F. Raushel, W. Cleland, S. R. Caldwell, 1991, Biochemistry.

Insights into the mechanism of flavoprotein-catalyzed amine oxidation from nitrogen isotope effects on the reaction of N-methyltryptophan oxidase.

W. Cleland, Mark A. Anderson, P. Fitzpatrick, 2007, Biochemistry.

What limits the rate of an enzyme-catalyzed reaction

W. Cleland, 1975 .

Characterization of the Transition-State Structures and Mechanisms for the Isomerization and Cleavage Reactions of Uridine 3‘-m-Nitrobenzyl Phosphate

W. Cleland, B. Gerratana, Andrea Sowa, 2000 .

Low-barrier hydrogen bonds and enzymic catalysis.

W. Cleland, W W Cleland, M M Kreevoy, 1994, Science.

Kinetic analysis of the individual reductive steps catalyzed by beta-hydroxy-beta-methylglutaryl-coenzyme A reductase obtained from yeast.

W. Cleland, J. Porter, R. E. Dugan, 1976, Biochemistry.

Acid Catalyzed Condensations. I. 1,3,5-Triarylbenzenes1

W. Cleland, R. Lyle, E. Dewitt, 1953 .

Preparation and properties of chromium (3)-nucleotide complexes for use in the study of enzyme mechanisms.

M. DePamphilis, W. Cleland, 1973, Biochemistry.

Secondary deuterium and nitrogen-15 isotope effects in enzyme-catalyzed reactions. Chemical mechanism of liver alcohol dehydrogenase.

N. Oppenheimer, W. Cleland, P. Cook, 1981, Biochemistry.

The specificity of chromium nucleotides as inhibitors of selected kinases.

W. Cleland, C. Janson, 1974, The Journal of biological chemistry.

Slow-binding inhibition: the general case.

J. Morrison, W. Cleland, M. Sculley, 1996, Biochimica et biophysica acta.

Investigation of substrate specificity of creatine kinase using chromium (III) and cobalt(III) complexes of adenosine 5'-diphosphate.

W. Cleland, V. Pecoraro, J. Rawlings, 1984, Biochemistry.

X-ray crystal and molecular structure and absolute configuration of (dihydrogen tripolyphosphato) tetraamminecobalt(III) monohydrate, Co(NH3)4H2P3O10.H2O. A model for a metal-nucleoside polyphosphate complex.

M. Sundaralingam, E. Merritt, W. Cleland, 1978, Biochemistry.

Phosphorus-31 NMR studies of complexes of adenosine triphosphate, adenosine diphosphate, tripolyphosphate, and pyrophosphate with cobalt(III) ammines

W. Cleland, R. Cornelius, P. A. Hart, 1977 .

Use of chromium-adenosine triphosphate and lyxose to elucidate the kinetic mechanism and coordination state of the nucleotide substrate for yeast hexokinase.

W. Cleland, K. Danenberg, 1975, Biochemistry.

The kinetic mechanism of glycerokinase.

W. Cleland, C. Janson, C A Janson, 1974, The Journal of biological chemistry.

Determining the chemical mechanisms of enzyme-catalyzed reactions by kinetic studies.

W. Cleland, 2006, Advances in enzymology and related areas of molecular biology.

Phosphoryl Transfer Reactions of Phosphodiesters:Characterization of Transition States by Heavy Atom Isotope Effects

W. Cleland, A. Hengge, 1991 .

Isotope effects: determination of enzyme transition state structure.

W. Cleland, 1995, Methods in enzymology.

A heavy-atom isotope effect and kinetic investigation of the hydrolysis of semicarbazide by urease from jack bean (Canavalia ensiformis).

W. Cleland, J. Marlier, E. Fogle, 2008, Biochemistry.

Enzymatic mechanisms of phosphate and sulfate transfer.

W. Cleland, A. Hengge, 2006, Chemical reviews.

Substrate activity of (adenosine triphosphato)tetraamminecobalt(III) with yeast hexokinase and separation of diastereomers using the enzyme.

W. Cleland, R. Cornelius, 1978, Biochemistry.

MECHANISM OF PHOSPHODIESTER CLEAVAGE WITH BETA -CYCLODEXTRIN

W. Cleland, A. Hengge, 1991 .

Mechanism of Rubisco: The Carbamate as General Base.

F. C. Hartman, W. Cleland, G. Lorimer, 1998, Chemical reviews.

Substrate synergism and the kinetic mechanism of yeast hexokinase.

F. Raushel, W. Cleland, R. Viola, 1982, Biochemistry.

Correlation of low-barrier hydrogen bonding and oxyanion binding in transition state analogue complexes of chymotrypsin.

P A Frey, P. Frey, W. Cleland, 2001, Biochemistry.

Determination of equilibrium 18O isotope effects on the deprotonation of phosphate and phosphate esters and the anomeric effect on deprotonation of glucose 6-phosphate

W. Cleland, P. Weiss, W. Knight, 1986 .

Meanings of Ki for conventional and alternate-substrate inhibitors.

W. Cleland, T. Spector, 1981, Biochemical pharmacology.

Preparation of chromium(III) and cobalt(III) nucleotides as chirality probes and inhibitors.

W. Cleland, 1982, Methods in enzymology.

Determination of the rate-limiting steps for malic enzyme by the use of isotope effects and other kinetic studies.

W. Cleland, C. Grimshaw, M. Schimerlik, 1977, Biochemistry.

pH variation of the kinetic parameters and the catalytic mechanism of malic enzyme.

W. Cleland, M. Schimerlik, 1977, Biochemistry.

Inhibition and alternate-substrate studies on the mechanism of malic enzyme.

W. Cleland, M. Schimerlik, 1977, Biochemistry.

Pigeon liver malic enzyme. V. Kinetic studies.

W. Cleland, R. Y. Hsu, H. Lardy, 1967, The Journal of biological chemistry.

Multiple isotope effects with alternative dinucleotide substrates as a probe of the malic enzyme reaction.

W. Cleland, P. Cook, P. Weiss, 1991, Biochemistry.

Isotope effect studies of chicken liver NADP malic enzyme: role of the metal ion and viscosity dependence.

W. Cleland, C. Grissom, 1988, Biochemistry.

Use of intermediate partitioning to calculate intrinsic isotope effects for the reaction catalyzed by malic enzyme.

W. Cleland, C. Grissom, 1985, Biochemistry.

pH variation of isotope effects in enzyme-catalyzed reactions. 2. Isotope-dependent step not pH dependent. Kinetic mechanism of alcohol dehydrogenase.

W. Cleland, P. Cook, W W Cleland, 1981, Biochemistry.

The Low Barrier Hydrogen Bond in Enzymatic Catalysis*

P A Frey, P. Frey, J. Gerlt, 1998, The Journal of Biological Chemistry.

Kinetic Studies with Liver Alcohol Dehydrogenase

W. Cleland, C. C. Wratten, 1965 .

KINETIC STUDIES OF GLUTAMIC OXALOACETIC TRANSAMINASE ISOZYMES.

W. Cleland, W W CLELAND, C P HENSON, 1964, Biochemistry.

Kinetic mechanism of glutamate dehydrogenase.

W. Cleland, J. Rifé, 1980, Biochemistry.

Mechanisms of aldehyde-induced adenosinetriphosphatase activities of kinases.

W. Cleland, A. Rendina, 1984, Biochemistry.

pH studies on the chemical mechanism of rabbit muscle pyruvate kinase. 2. Physiological substrates and phosphoenol-alpha-ketobutyrate.

W. Cleland, T. M. Dougherty, 1985, Biochemistry.

Determination of the mechanism of human malic enzyme with natural and alternate dinucleotides by isotope effects.

L. Tong, W. Cleland, Z. Yang, 2001, Archives of biochemistry and biophysics.

Secondary 18O and primary 13C isotope effects as a probe of transition-state structure for enzymatic decarboxylation of oxalacetate.

W. Cleland, G. Waldrop, J. Urbauer, 1994, Biochemistry.

Use of multiple isotope effects to determine enzyme mechanisms and intrinsic isotope effects. Malic enzyme and glucose-6-phosphate dehydrogenase.

W. Cleland, J. Hermes, M. O'Leary, 1982, Biochemistry.

Mechanistic deductions from isotope effects in multireactant enzyme mechanisms.

W. Cleland, P. Cook, 1981, Biochemistry.

Rat liver pyruvate carboxylase. II. Kinetic studies of the forward reaction.

W. Cleland, H. Lardy, M. Wagner, 1971, The Journal of biological chemistry.

Activation and inhibition of pyruvate carboxylase from Rhizobium etli.

W. Cleland, J. Wallace, S. Jitrapakdee, 2011, Biochemistry.

Use of primary deuterium and 15N isotope effects to deduce the relative rates of steps in the mechanisms of alanine and glutamate dehydrogenases.

W. Cleland, P. Cook, P. Weiss, 1988, Biochemistry.

Primary and secondary deuterium isotope effects on equilibrium constants for enzyme-catalyzed reactions.

W. Cleland, J. Blanchard, P. Cook, 1980, Biochemistry.

Isotope effect studies of the chemical mechanism of pig heart NADP isocitrate dehydrogenase.

W. Cleland, C. Grissom, 1988, Biochemistry.

pH variation of isotope effects in enzyme-catalyzed reactions. 1. Isotope- and pH-dependent steps the same.

W. Cleland, P. Cook, 1981, Biochemistry.

Equilibrium perturbation by isotope substitution.

W. Cleland, M. Schimerlik, J. Rifé, 1975, Biochemistry.

[7] Isocitrate dehydrogenase (TPN-specific) from pig heart

V. W. Thompson, W. Cleland, R. E. Barden, 1969 .

Variation of transition-state structure as a function of the nucleotide in reactions catalyzed by dehydrogenases. 2. Formate dehydrogenase.

W. Cleland, J. Hermes, M. O'Leary, 1984, Biochemistry.

Variation of transition-state structure as a function of the nucleotide in reactions catalyzed by dehydrogenases. 1. Liver alcohol dehydrogenase with benzyl alcohol and yeast aldehyde dehydrogenase with benzaldehyde.

W. Cleland, M. A. Fisher, M. Scharschmidt, 1984, Biochemistry.

[19] Initial velocity analysis for terreactant mechanisms

W. Cleland, R. Viola, 1982 .

Use of isotope effects to elucidate enzyme mechanisms.

W. Cleland, 1982, CRC critical reviews in biochemistry.

Carbon-13 and deuterium isotope effects on oxalacetate decarboxylation by pyruvate carboxylase.

W. Cleland, P. Tipton, P. Attwood, 1986, Biochemistry.

Mechanisms of decarboxylation of carboxybiotin

W. Cleland, P. Tipton, 1988 .

The Use of Isotope Effects to Determine Enzyme Mechanisms

W. Cleland, W W Cleland, 2003, Journal of Biological Chemistry.

The use of isotope effects to determine enzyme mechanisms.

W. Cleland, M. O'Leary, 2003, The Journal of biological chemistry.

3 Steady-State Kinetics

W. Cleland, 1990 .

The use of isotope effects in the detailed analysis of catalytic mechanisms of enzymes

W. Cleland, 1987 .

The kinetics of enzyme-catalyzed reactions with two or more substrates or products. II. Inhibition: nomenclature and theory.

W. Cleland, W W CLELAND, 1963, Biochimica et biophysica acta.

1 Steady State Kinetics

W. Cleland, W. W. Cleland, 1970 .

Carbon isotope effects on the metal ion catalyzed decarboxylation of oxalacetate

W. Cleland, C. Grissom, 1986 .

Magnitude of the equilibrium isotope effect on carbon-tritium bond synthesis.

W. Cleland, H. Meloche, C. Monti, 1977, Biochimica et biophysica acta.

Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase.

W. Cleland, C. Grimshaw, 1981, Biochemistry.

The kinetics of enzyme-catalyzed reactions with two or more substrates or products. II. Inhibition: nomenclature and theory.

W. Cleland, W. Wallace Cleland, W.W Cleland, 1963, Biochimica et biophysica acta.

The kinetics of enzyme-catalyzed reactions with two or more substrates or products. III. Prediction of initial velocity and inhibition patterns by inspection.

W. Cleland, W W CLELAND, 1963, Biochimica et biophysica acta.

Tracer experiments on the mechanism of citric acid formation by Aspergillus niger.

W. Cleland, M. J. Johnson, 1954, The Journal of biological chemistry.

Differential regulation of the yeast isozymes of pyruvate carboxylase and the locus of action of acetyl CoA.

W. Cleland, J. Wallace, S. Jitrapakdee, 2007, The international journal of biochemistry & cell biology.

Enzyme Mechanisms from Isotope Effects

W. Cleland, 2005 .

Computer Programmes for Processing Enzyme Kinetic Data

W. Cleland, W. W. CLELAND, W. W. CLELAND, 1963, Nature.

Studies of the microsomal acylation of L-glycerol-3-phosphate. I. The specificity of the rat brain enzyme.

W. Cleland, E. Sánchez de Jiménez, E.Sánchez De Jiménez, 1969, Biochimica et biophysica acta.

Studies on the microsomal acylation of L-glycerol-3-phosphate. 3. Time course of the reaction.

W. Cleland, W. Zahler, 1969, Biochimica et biophysica acta.

Bovine liver fructokinase: purification and kinetic properties.

F. Raushel, W. Cleland, 1977, Biochemistry.

A novel method for determining rate constants for dehydration of aldehyde hydrates.

W. Cleland, J. Hermes, A. Rendina, 1984, Biochemistry.

[20] Substrate inhibition

W. Cleland, 1979 .

Preparation and properties of chromium(III) adenosine 5'-triphosphate, chromium(III) adenosine 5'-diphosphate, and related chromium(III) complexes.

W. Cleland, D. Dunaway-Mariano, 1980, Biochemistry.

Purification and kinetic studies of beef liver cytoplasmic aconitase.

W. Cleland, C. Henson, 1967, The Journal of biological chemistry.

pH profiles and isotope effects for aconitases from Saccharomycopsis lipolytica, beef heart, and beef liver. alpha-Methyl-cis-aconitate and threo-Ds-alpha-methylisocitrate as substrates.

W. Cleland, J. Schloss, J V Schloss, 1984, Biochemistry.

Relationship of the oxidation state of the iron-sulfur cluster of aconitase to activity and substrate binding.

W. Cleland, H. Beinert, R. Ramsay, 1981, Biochemistry.

Nitro analogues of citrate and isocitrate as transition-state analogues for aconitase.

W. Cleland, J. Schloss, D. J. Porter, 1980, Biochemistry.

THE PARTIAL PURIFICATION, PROPERTIES, AND MECHANISM OF ACTION OF PIG LIVER ISOPENTENYL PYROPHOSPHATE ISOMERASE.

W. Cleland, J. Porter, D. Shah, 1965, The Journal of biological chemistry.

Optimizing coupled enzyme assays.

W. Cleland, 1979, Analytical biochemistry.

Kinetic studies of yeast nucleoside diphosphate kinase.

W. Cleland, W W Cleland, E Garces, 1969, Biochemistry.

Energetics of substrate binding, catalysis, and product release.

W. Cleland, D. Northrop, 1999, Methods in enzymology.

Reaction intermediate analogues for enolase.

W. Cleland, P. Weiss, V. Anderson, 1984, Biochemistry.

Lanthanide-adenosine 5'-triphosphate complexes: determination of their dissociation constants and mechanism of action as inhibitors of yeast hexokinase

J. Morrison, W. Cleland, 1983 .

Kinetic and isotope-exchange studies on shikimate dehydrogenase from Pisum sativum.

W. Cleland, D. Balinsky, A. W. Dennis, 1971, Biochemistry.

Enzyme kinetics revisited: a commentary on 'The Kinetics of Enzyme-Catalyzed Reactions With Two or More Substrates or Products'.

W. Cleland, W W Cleland, 1989, Biochimica et Biophysica Acta.

Kinetic studies of Escherichia coli galactokinase.

W. Cleland, J. Gulbinsky, 1968, Biochemistry.

Enzyme Kinetics and Mechanism

Paul F. Cook, W. Cleland, P. Cook, 2007 .

Enthalpic Studies of Complex Formation between Carboxylic Acids and 1-Alkylimidazoles

W. Cleland, K. Sacksteder, L. Reinhardt, 1998 .

Mechanisms of enzymatic and acid-catalyzed decarboxylations of prephenate.

J. Morrison, W. Cleland, J. Hermes, 1984, Biochemistry.

Use of multiple isotope effects to study the mechanism of 6-phosphogluconate dehydrogenase.

W. Cleland, J. Hermes, A. Rendina, 1984, Biochemistry.

Low-barrier hydrogen bonds and low fractionation factor bases in enzymatic reactions.

W. Cleland, 1992, Biochemistry.

The use of pH studies to determine chemical mechanisms of enzyme-catalyzed reactions.

W. Cleland, 1982, Methods in enzymology.

Influence of salt, substrate, and cofactor concentrations on the kinetic and mechanistic behavior of phosphoglycerate mutase.

S. Grisolía, W. Cleland, 1968, Biochemistry.

Stability constants of Mg2+ and Cd2+ complexes of adenine nucleotides and thionucleotides and rate constants for formation and dissociation of MgATP and MgADP.

W. Cleland, J. Hermes, V. Pecoraro, 1984, Biochemistry.

Studies on the microsomal acylation of L-glycerol-3-phosphate. II. The specificity and properties of the rat liver enzyme.

W. Cleland, H. Abou-Issa, 1969, Biochimica et biophysica acta.

The use of isotope effects to determine transition-state structure for enzymic reactions.

W. Cleland, 1982, Methods in enzymology.

The catalytic base of enolase is a sulfhydryl group

W. Cleland, P. Weiss, R. J. Boerner, 1987 .

2-Keto-3-fluoroglutarate: a useful mechanistic probe of 2-keto-glutarate-dependent enzyme systems.

W. Cleland, C. Grissom, 1987, Biochimica et biophysica acta.

Understanding enzymic catalysis: the importance of short, strong hydrogen bonds.

P. Frey, J. Gerlt, W. Cleland, 1997, Chemistry & biology.

Evidence from nitrogen-15 and solvent deuterium isotope effects on the chemical mechanism of adenosine deaminase.

W. Cleland, J. Hermes, P. Cook, 1987, Biochemistry.

Kinetics and mechanism of benzoylformate decarboxylase using 13C and solvent deuterium isotope effects on benzoylformate and benzoylformate analogues.

G. L. Kenyon, Paul Cook, W. Cleland, 1988, Biochemistry.

The low-barrier hydrogen bond in enzymic catalysis

W. Cleland, 2010 .

Kinetic Isotope Effects for Acyl Transfer from p-Nitrophenyl Acetate to Hydroxylamine Show a pH-Dependent Change in Mechanism

W. Cleland, A. Hengge, R. Hess, 1997 .

Metal-catalyzed phosphodiester cleavage: secondary 18O isotope effects as an indicator of mechanism.

W. Cleland, A. Hengge, J. Rawlings, 2006, Journal of the American Chemical Society.

AN ALLOSTERIC REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE OXIDASE FROM MYCOBACTERIUM TUBERCULOSIS.

W. Cleland, A. Worcel, D. Goldman, 1965, The Journal of biological chemistry.

Interaction of metal(III)-adenosine 5'-triphosphate complexes with yeast hexokinase.

J. Morrison, W. Cleland, R. Viola, 1980, Biochemistry.

HYDROGEN BONDING IN COMPLEXES OF CARBOXYLIC ACIDS WITH 1-ALKYLIMIDAZOLES :STERIC AND ISOTOPIC EFFECTS ON LOW BARRIER HYDROGEN BONDING

P. Frey, W. Cleland, C. Cassidy, 1999 .

The substrate and anomeric specificity of fructokinase.

F. Raushel, W. Cleland, 1973, The Journal of biological chemistry.

Phosphorylated aminosugars: synthesis, properties, and reactivity in enzymatic reactions.

D. Sem, W. Cleland, 1991, Biochemistry.

Hydrolysis of phosphotriesters: determination of transition states in parallel reactions by heavy-atom isotope effects.

F. Raushel, M. Anderson, W. Cleland, 2001, Journal of the American Chemical Society.

Chorismate mutase-prephenate dehydrogenase from Escherichia coli. 1. Kinetic characterization of the dehydrogenase reaction by use of alternative substrates.

J. Morrison, W. Cleland, J. Turnbull, 1990, Biochemistry.

Rat liver pyruvate carboxylase. 3. Isotopic exchange studies of the first partial reaction.

W. Cleland, H. Lardy, W. R. McClure, 1971, The Journal of biological chemistry.

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.

W. Cleland, M. Templeton, C. Collyer, 2005, Biochemistry.

15N isotope effects in glutamine hydrolysis catalyzed by carbamyl phosphate synthetase: evidence for a tetrahedral intermediate in the mechanism.

W. Cleland, C. J. Lusty, M. Rishavy, 2000, Biochemistry.

Substrate inhibition.

W. Cleland, 1979, Methods in enzymology.

Derivation of rate equations for multisite ping-pong mechanisms with ping-pong reactions at one or more sites.

W. Cleland, W W Cleland, 1973, The Journal of biological chemistry.

Fatty acid synthetase. A steady state kinetic analysis of the reaction catalyzed by the enzyme from pigeon liver.

W. Cleland, J. Porter, S. S. Katiyar, 1975, The Journal of biological chemistry.

Mechanism of action of the nonspecific phosphomonoesterase from potatoes.

W. Cleland, R. Y. Hsu, L. Anderson, 1966, Biochemistry.

Rabbit muscle phosphofructokinase. II. Product and dead end inhibition.

W. Cleland, J. Bar-Tana, 1974, The Journal of biological chemistry.

Oxamate is an alternative substrate for pyruvate carboxylase from Rhizobium etli.

W. Cleland, Tonya N. Zeczycki, J. Marlier, 2013, Biochemistry.

Synthesis of various chelating celluloses and their application in removing Al3 from ATP.

W. Cleland, J. Schloss, A. Aulabaugh, 1982, Analytical biochemistry.

Secondary 18 O isotope effects as a tool for studying reactions of phosphate mono‐, di‐, and triesters1

W. Cleland, 1990, The FASEB Journal.

Secondary 18O Isotope Effects as a Tool for Studying Reactions of Phosphate Mono‐, Di‐, and Triesters

W. Cleland, 1991 .

Steady-state kinetic studies of the metal ion-dependent decarboxylation of oxalacetate catalyzed by pyruvate kinase.

W. Cleland, D. M. Kiick, 1989, Archives of biochemistry and biophysics.

Fractionation factors and activation energies for exchange of the low barrier hydrogen bonding proton in peptidyl trifluoromethyl ketone complexes of chymotrypsin.

P. Frey, W. M. Westler, J. Markley, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Are There Strong Hydrogen Bonds in Aqueous Solutions

P. Frey, W. Cleland, 1998 .

A structural element that facilitates proton-coupled electron transfer in oxalate decarboxylase.

Karen N. Allen, W. Cleland, N. Richards, 2012, Biochemistry.

Use of isotope effects to determine enzyme mechanisms

W. Cleland, 2007 .

Evidence from multiple isotope effect determinations for coupled hydrogen motion and tunneling in the reaction catalyzed by glucose-6-phosphonate dehydrogenase

W. Cleland, J. Hermes, 1984 .

Studies on the tyrosine aminotransferase mechanism.

W. Cleland, G. Litwack, 1968, Biochemistry.

Heavy Atom Isotope Effects Reveal a Highly Polarized Transition State for Chorismate Mutase

D. Hilvert, P. Kast, O. Wiest, 1999 .

Interaction between the biotin carboxyl carrier domain and the biotin carboxylase domain in pyruvate carboxylase from Rhizobium etli.

W. Cleland, J. Wallace, P. Attwood, 2011, Biochemistry.

Purification and kinetic studies of the citrate cleavage enzyme.

W. Cleland, W W Cleland, D M Plowman, 1967, The Journal of biological chemistry.

RING OPENING AND CLOSING RATES FOR THIOSUGARS

W. Cleland, R. Whistler, C. Grimshaw, 1979 .

Phosphorylated thiosugars: synthesis, properties, and reactivity in enzymatic reactions.

D. Sem, W. Cleland, H. Miziorko, 1991, Biochemistry.

Alteration of the concentrations of dilute palmityl-CoA solutions by surface adsorption.

W. Cleland, R. E. Barden, 1969, Biochemical and biophysical research communications.

Kinetics of aminoacyl-tRNA synthetases catalyzed ATP-PPi exchange.

W. Cleland, D. Santi, R. Webster, 1974, Methods in enzymology.

Catalytic mechanism of biotin carboxylase: steady-state kinetic investigations.

W. Cleland, P. Tipton, 1988, Biochemistry.

Insight into the carboxyl transferase domain mechanism of pyruvate carboxylase from Rhizobium etli.

W. Cleland, J. Wallace, S. Jitrapakdee, 2009, Biochemistry.

pH properties and chemical mechanism of action of 3-hydroxy-3-methylglutaryl coenzyme A reductase.

W. Cleland, J. Porter, D. Veloso, 1981, Biochemistry.

Carbon-13 isotope effects on reactions involving carbamate and carbamoyl phosphate.

W. Cleland, P. Tipton, 1988, Archives of Biochemistry and Biophysics.

Carbon-13 and deuterium isotope effects on the catalytic reactions of biotin carboxylase.

W. Cleland, P. Tipton, 1988, Biochemistry.

13C isotope effect studies of Escherichia coli aspartate transcarbamylase in the presence of the bisubstrate analog N-(phosphonoacetyl)-L-aspartate.

W. Cleland, H. K. Schachman, M. O'Leary, 1992, Biochemistry.

pH‐rate profiles support a general base mechanism for galactokinase (Lactococcus lactis)

W. Cleland, J. Thoden, H. Holden, 2013, FEBS letters.

13C and 15N isotope effects as a probe of the chemical mechanism of Escherichia coli aspartate transcarbamylase.

W. Cleland, H. K. Schachman, P. Weiss, 1992, Biochemistry.

High Resolution X-ray Structure of dTDP-Glucose 4,6-Dehydratase from Streptomyces venezuelae*

W. Cleland, H. Holden, S. Allard, 2004, Journal of Biological Chemistry.

Decarboxylation of oxalacetate by pyruvate carboxylase.

W. Cleland, P. Attwood, 1986, Biochemistry.

pH profile for the mutarotation of 6-thio-d-fructose

W. Cleland, R. Whistler, C. Grimshaw, 1980 .

pH studies on the chemical mechanism of rabbit muscle pyruvate kinase. 1. Alternate substrates oxalacetate, glycolate, hydroxylamine, and fluoride.

W. Cleland, T. M. Dougherty, 1985, Biochemistry.

Roles of Arg427 and Arg472 in the binding and allosteric effects of acetyl CoA in pyruvate carboxylase.

W. Cleland, J. Wallace, S. Jitrapakdee, 2012, Biochemistry.

Role of metal ions in catalysis by enolase: an ordered kinetic mechanism for a single substrate enzyme.

G. H. Reed, W. Cleland, R. Poyner, 2001, Biochemistry.

Structural and kinetic isotope effect studies of nicotinamidase (Pnc1) from Saccharomyces cerevisiae.

Brian C. Smith, J. Denu, W. Cleland, 2012, Biochemistry.

Insights into the mechanism and regulation of pyruvate carboxylase by characterisation of a biotin-deficient mutant of the Bacillus thermodenitrificans enzyme.

W. Cleland, J. Wallace, S. Jitrapakdee, 2008, The international journal of biochemistry & cell biology.

Use of isotope effects and pH studies to determine the chemical mechanism of Bacillus subtilis L-alanine dehydrogenase.

W. Cleland, P. Cook, C. Grimshaw, 1981, Biochemistry.

Steady-state kinetics and isotope effects on the mutant catalytic trimer of aspartate transcarbamoylase containing the replacement of histidine 134 by alanine.

W. Cleland, H. K. Schachman, J. Turnbull, 1992, Biochemistry.

13 C, 15 N, and 18 O equilibrium isotope effects and fractionation factors

W. Cleland, M. Rishavy, 1999 .

Structures of the meridional and facial isomers of triamminechromium pyrophosphate dihydrate.

M. Sundaralingam, W. Cleland, T. Haromy, 1990, Acta Crystallographica Section C: Crystal Structure Communications.

Oxidative decarboxylation of 6-phosphogluconate by 6-phosphogluconate dehydrogenase proceeds by a stepwise mechanism with NADP and APADP as oxidants.

W. Cleland, C. Hwang, P. Cook, 1998, Biochemistry.

On low-barrier hydrogen bonds and enzyme catalysis.

P A Kollman, P. Kollman, P. Frey, 1995, Science.

Determination of the screw sense specificity of bovine liver fructokinase.

W. Cleland, V. Pecoraro, A. Rendina, 1985, Biochemistry.

18O Isotope Effects Support a Concerted Mechanism for Ribonuclease A

W. Cleland, A. Hengge, G. Sowa, 1997 .

Enzymatic Mechanisms of Phosphate and Sulfate Transfer

W. Cleland, A. Hengge, 2006 .

Determination of the rate-limiting steps and chemical mechanism of fructokinase by isotope exchange, isotope partitioning, and pH studies.

F. Raushel, W. Cleland, 1977, Biochemistry.

Properties of 3-hydroxypropionaldehyde 3-phosphate.

W. Cleland, A. Gallopo, 1979, Archives of biochemistry and biophysics.

APPENDIX INHIBITION PATTERNS OBTAINED WHERE AN INHIBITOR IS PRESENT IN CONSTANT PROPORTION TO VARIABLE SUBSTRATE

M. Gross, W. Cleland, J. E. Folk, 1973 .

[7] Kinetic method for determination of dissociation constants nucleotide complexes

W. Cleland, 1995 .

A kinetic method for determining dissociation constants for metal complexes of adenosine 5'-triphosphate and adenosine 5'-diphosphate.

J. Morrison, W. Cleland, 1980, Biochemistry.

15N kinetic isotope effects on uncatalyzed and enzymatic deamination of cytidine.

R. Wolfenden, M. Snider, W. Cleland, 2002, Biochemistry.