10 Mechanism of NAD-Dependent Enzymes
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[1] J. Burbaum,et al. Internal thermodynamics of enzymes determined by equilibrium quench: values of Kint for enolase and creatine kinase. , 1989, Biochemistry.
[2] J J Burbaum,et al. Evolutionary optimization of the catalytic effectiveness of an enzyme. , 1989, Biochemistry.
[3] J. Slama,et al. Inhibition of NAD glycohydrolase and ADP-ribosyl transferases by carbocyclic analogues of oxidized nicotinamide adenine dinucleotide. , 1989, Biochemistry.
[4] I. Pastan,et al. Pseudomonas exotoxin: chimeric toxins. , 1989, The Journal of biological chemistry.
[5] K. T. Eisses. On the oxidation of aldehydes by alcohol dehydrogenase of Drosophila melanogaster: Evidence for the gem-diol as the reacting substrate , 1989 .
[6] J. Klinman. Quantum mechanical effects in enzyme-catalysed hydrogen transfer reactions. , 1989, Trends in biochemical sciences.
[7] S. Narumiya,et al. Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase. , 1989, The Journal of biological chemistry.
[8] C. Locht,et al. Identification of amino acid residues essential for the enzymatic activities of pertussis toxin. , 1989, Proceedings of the National Academy of Sciences of the United States of America.
[9] P. Frey,et al. UDP-galactose 4-epimerase. Phosphorus-31 nuclear magnetic resonance analysis of NAD+ and NADH bound at the active site. , 1989, Biochemistry.
[10] C. J. Murray,et al. Hydrogen tunneling in enzyme reactions. , 1989, Science.
[11] L. Ljungdahl,et al. Temperature-dependent enantiospecificity of secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus , 1989 .
[12] J. Vandekerckhove,et al. Purification of the 22 kDa protein substrate of botulinum ADP‐ribosyltransferase C3 from porcine brain cytosol and its characterization as a GTP‐binding protein highly homologous to the rho gene product , 1989, FEBS letters.
[13] H. Muirhead,et al. A specific, highly active malate dehydrogenase by redesign of a lactate dehydrogenase framework. , 1988, Science.
[14] P. Ludden,et al. Purification and properties of dinitrogenase reductase ADP-ribosyltransferase from the photosynthetic bacterium Rhodospirillum rubrum. , 1988, The Journal of biological chemistry.
[15] R. Rappuoli,et al. Subunit S1 of pertussis toxin: mapping of the regions essential for ADP-ribosyltransferase activity. , 1988, Proceedings of the National Academy of Sciences of the United States of America.
[16] K. Nakao,et al. Purification and properties of the cytosolic substrate for botulinum ADP-ribosyltransferase. Identification as an Mr 22,000 guanine nucleotide-binding protein. , 1988, The Journal of biological chemistry.
[17] S. Benner,et al. Stereochemical Profile of the Dehydrogenases of Drosophila melanogaster , 1988 .
[18] P. Zbinden,et al. Crystal Structures of Two Simple N-Substituted Dihydronicotinamides: Possible Implications for Stereoelectronic Arguments in Enzymology , 1988 .
[19] S. van Heyningen,et al. Thiol reagents are substrates for the ADP‐ribosyltransferase activity of pertussis toxin , 1988, FEBS letters.
[20] P. Karplus,et al. Crystallographic analysis of the binding of NADPH, NADPH fragments, and NADPH analogues to glutathione reductase. , 1988, Biochemistry.
[21] V. Anderson,et al. Hydride transfer catalyzed by lactate dehydrogenase displays absolute stereospecificity at C4 of the nicotinamide ring , 1988 .
[22] B. Plapp,et al. Carboxyl groups near the active site zinc contribute to catalysis in yeast alcohol dehydrogenase. , 1988, The Journal of biological chemistry.
[23] S. Tanuma,et al. Eukaryotic mono(ADP-ribosyl)transferase that ADP-ribosylates GTP-binding regulatory Gi protein. , 1988, The Journal of biological chemistry.
[24] F. Schuber,et al. Chemical evidence in favor of a stabilized oxocarbonium-ion intermediate in the NAD+ glycohydrolase-catalyzed reactions , 1988 .
[25] N. Oppenheimer,et al. Pyridine nucleotide chemistry: a new mechanism for the hydroxide-catalyzed hydrolysis of the nicotinamide-glycosyl bond , 1988 .
[26] K. Aktories,et al. Botulinum ADP-ribosyltransferase C3. Purification of the enzyme and characterization of the ADP-ribosylation reaction in platelet membranes. , 1988, European journal of biochemistry.
[27] P. Frey,et al. Uridine diphosphate galactose 4-epimerase. pH dependence of the reduction of NAD+ by a substrate analog. , 1988, The Journal of biological chemistry.
[28] J. Vandekerckhove,et al. Botulinum C2 toxin ADP-ribosylates cytoplasmic beta/gamma-actin in arginine 177. , 1988, The Journal of biological chemistry.
[29] J. Slama,et al. Carbanicotinamide adenine dinucleotide: synthesis and enzymological properties of a carbocyclic analogue of oxidized nicotinamide adenine dinucleotide. , 1988, Biochemistry.
[30] D. Burns,et al. Structural characterization of pertussis toxin A subunit. , 1987, The Journal of biological chemistry.
[31] R. Collier,et al. Exotoxin A of Pseudomonas aeruginosa: substitution of glutamic acid 553 with aspartic acid drastically reduces toxicity and enzymatic activity , 1987, Journal of bacteriology.
[32] T. Taniguchi,et al. Reaction mechanism for automodification of poly(ADP-ribose) synthetase. , 1987, Biochemical and biophysical research communications.
[33] B. Persson,et al. Characteristics of alcohol/polyol dehydrogenases. The zinc-containing long-chain alcohol dehydrogenases. , 1987, European journal of biochemistry.
[34] S. Benner,et al. Free energy differences between enzyme bound states. , 1987, Journal of theoretical biology.
[35] H. Kaslow,et al. Sulfhydryl-alkylating reagents inactivate the NAD glycohydrolase activity of pertussis toxin. , 1987, Biochemistry.
[36] R. Collier,et al. Active site of Pseudomonas aeruginosa exotoxin A. Glutamic acid 553 is photolabeled by NAD and shows functional homology with glutamic acid 148 of diphtheria toxin. , 1987, The Journal of biological chemistry.
[37] N. Oppenheimer,et al. Pyridine coenzyme analogues. Synthesis and characterization of alpha- and beta-nicotinamide arabinoside adenine dinucleotides. , 1987, Biochemistry.
[38] H. Jörnvall,et al. Mammalian alcohol dehydrogenases of separate classes: intermediates between different enzymes and intraclass isozymes. , 1987, Proceedings of the National Academy of Sciences of the United States of America.
[39] Yun-Dong Wu,et al. Theoretical transition structures for hydride transfer to methyleneiminium ion from methylamine and dihydropyridine. On the nonlinearity of hydride transfers , 1987 .
[40] F. Schuber,et al. Application of linear free-energy relationships to the mechanistic probing of nonenzymatic and NAD+-glycohydrolase-catalyzed hydrolysis of pyridine dinucleotides , 1987 .
[41] S. Narumiya,et al. ADP-ribosylation of a Mr 21,000 membrane protein by type D botulinum toxin. , 1987, The Journal of biological chemistry.
[42] H. Levy,et al. Modification of glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides with the 2',3'-dialdehyde derivative of NADP+ (oNADP+). , 1987, The Journal of biological chemistry.
[43] N. Oppenheimer,et al. Remote nitrogen-15 isotope effects on addition of cyanide to NAD. , 1987, Biochemistry.
[44] A. Ohno,et al. NAD(P)+-NAD(P)H models. LXI: An interconversion between central and axial chiralities as an evidence for a functional model of chemical evolution of an enzyme , 1986 .
[45] M. Ozdemirli,et al. On the nature of cellular ADP-ribosyltransferase from rat liver specific for elongation factor 2. , 1986, Biochemical and biophysical research communications.
[46] N. Oppenheimer,et al. Amino acid specific ADP-ribosylation: substrate specificity of an ADP-ribosylarginine hydrolase from turkey erythrocytes. , 1986, Biochemistry.
[47] N. Oppenheimer. The stereospecificity of oxidation of alpha-[4R-2H]NADH by dehydrogenases. , 1986, The Journal of biological chemistry.
[48] H. Adolph,et al. Coenzyme stereospecificity of alcohol/polyol dehydrogenases: conservation of protein types vs. functional constraints , 1986 .
[49] J. Moss,et al. Pertussis toxin-catalyzed ADP-ribosylation of transducin. Cysteine 347 is the ADP-ribose acceptor site. , 1985, The Journal of biological chemistry.
[50] N. Oppenheimer,et al. Photoaffinity labeling of diphtheria toxin fragment A with NAD: structure of the photoproduct at position 148. , 1985, Proceedings of the National Academy of Sciences of the United States of America.
[51] S. Taylor,et al. Ribitol dehydrogenase of Klebsiella aerogenes. Sequence and properties of wild-type and mutant strains. , 1985, The Biochemical journal.
[52] J. Moss,et al. Kinetic mechanisms of two NAD:arginine ADP-ribosyltransferases: the soluble, salt-stimulated transferase from turkey erythrocytes and choleragen, a toxin from Vibrio cholerae. , 1985, Biochemistry.
[53] R. Collier,et al. Diphtheria toxin. Effect of substituting aspartic acid for glutamic acid 148 on ADP-ribosyltransferase activity. , 1985, The Journal of biological chemistry.
[54] S. Benner,et al. A stereochemical imperative in dehydrogenases: new data and criteria for evaluating function-based theories in bioorganic chemistry , 1985 .
[55] D. J. Raber,et al. Conformational properties of oxidation-reduction cofactors , 1985 .
[56] W. Ray,et al. On the origin of the lactate dehydrogenase induced rate effect. , 1984, Biochemistry.
[57] J. Verhoeven,et al. Diastereo-differentiating hydride transfer at bridged NAD(H) models , 1984 .
[58] R. Collier,et al. NAD binding site of diphtheria toxin: identification of a residue within the nicotinamide subsite by photochemical modification with NAD. , 1984, Proceedings of the National Academy of Sciences of the United States of America.
[59] H. Bourne,et al. Amino acid sequence of retinal transducin at the site ADP-ribosylated by cholera toxin. , 1984, The Journal of biological chemistry.
[60] H. Jörnvall,et al. Extended superfamily of short alcohol‐polyol‐sugar dehydrogenases: structural similarities between glucose and ribitol dehydrogenases , 1984, FEBS letters.
[61] E. Cedergren-Zeppezauer. Crystal-structure determination of reduced nicotinamide adenine dinucleotide complex with horse liver alcohol dehydrogenase maintained in its apo conformation by zinc-bound imidazole. , 1983, Biochemistry.
[62] J. Chin. Perfect enzymes: is the equilibrium constant between the enzyme's bound species unity? , 1983 .
[63] S. Benner,et al. A mechanistic basis for the stereoselectivity of enzymic transfer of hydrogen from nicotinamide cofactors , 1983 .
[64] D. A. Yost,et al. Adenosine diphosphoribose transfer reactions catalyzed by Bungarus fasciatus venom NAD glycohydrolase. , 1983, The Journal of biological chemistry.
[65] L. Banaszak,et al. The presence of a histidine-aspartic acid pair in the active site of 2-hydroxyacid dehydrogenases. X-ray refinement of cytoplasmic malate dehydrogenase. , 1983, The Journal of biological chemistry.
[66] H. Eklund,et al. Binding of substrate in a ternary complex of horse liver alcohol dehydrogenase. , 1982, The Journal of biological chemistry.
[67] J. Bolin,et al. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. II. Environment of bound NADPH and implications for catalysis. , 1982, The Journal of biological chemistry.
[68] N. Oppenheimer,et al. Diphtheria toxin. Site and configuration of ADP-ribosylation of diphthamide in elongation factor 2. , 1981, The Journal of biological chemistry.
[69] H. Jörnvall,et al. Alcohol and polyol dehydrogenases are both divided into two protein types, and structural properties cross-relate the different enzyme activities within each type. , 1981, Proceedings of the National Academy of Sciences of the United States of America.
[70] N. Oppenheimer,et al. Secondary deuterium and nitrogen-15 isotope effects in enzyme-catalyzed reactions. Chemical mechanism of liver alcohol dehydrogenase. , 1981, Biochemistry.
[71] T. A. Jones,et al. Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 A resolution. , 1981, Journal of molecular biology.
[72] Dahlquist Fw,et al. Determination of the equilibrium distibution between alcohol and aldehyde substrates when bound to horse liver alcohol dehydrogenase using magnetic resonance. , 1980 .
[73] J. Howard,et al. ADP-ribosylation of elongation factor 2 by diphtheria toxin. Isolation and properties of the novel ribosyl-amino acid and its hydrolysis products. , 1980, The Journal of biological chemistry.
[74] W. Jencks,et al. Mechanism of reactions of N-(methoxymethyl)-N,N-dimethylanilinium ions with nucleophilic reagents , 1980 .
[75] Carl Frieden,et al. Anomalous equilibrium and kinetic .alpha.-deuterium secondary isotope effects accompanying hydride transfer from reduced nicotinamide adenine dinucleotide , 1980 .
[76] William P. Jencks,et al. When is an intermediate not an intermediate? Enforced mechanisms of general acid-base, catalyzed, carbocation, carbanion, and ligand exchange reaction , 1980 .
[77] N. Oppenheimer,et al. Substrate specificity and partial purification of a stereospecific NAD- and guanidine-dependent ADP-ribosyltransferase from avian erythrocytes. , 1979, The Journal of biological chemistry.
[78] A. L. Powell,et al. Mechanism of the Cannizzaro reaction , 1979 .
[79] A. L. Powell,et al. Reduction of benzaldehyde by methoxide ion in aqueous methanol , 1979 .
[80] G. Chang,et al. Oxidized NADP as a potential active-site-directed reagent of pigeon liver malic enzyme. , 1979, Biochemical and biophysical research communications.
[81] N. Oppenheimer. The stereospecificity of pig brain NAD‐glycohydrolase‐catalyzed methanolysis of NAD+ , 1978, FEBS letters.
[82] N. Kaplan,et al. Enzyme stereospecificities for nicotinamide nucleotides , 1978 .
[83] N. Oppenheimer. Structural determination and stereospecificity of the choleragen-catalyzed reaction of NAD+ with guanidines. , 1978, The Journal of biological chemistry.
[84] H. Bull,et al. Concerning the mechanism of the enzymatic and nonenzymatic hydrolysis of nicotinamide nucleotide coenzymes. , 1978, The Journal of biological chemistry.
[85] N. Oppenheimer,et al. Stereospecificity of the intramolecular association of reduced pyridine coenzymes. , 1978, Biochemistry.
[86] N. Oppenheimer,et al. Structure of a poly (adenosine diphosphoribose) monomer: 2'-(5"-hosphoribosyl)-5'-adenosine monophosphate. , 1978, Proceedings of the National Academy of Sciences of the United States of America.
[87] M. Sinnott,et al. SN1 hydrolyses of glycosyl pyridinium salts, and quantification of the main source of catalytic power of E. coli(lacZ)-β-galactosidase , 1977 .
[88] M G Rossmann,et al. Studies of asymmetry in the three-dimensional structure of lobster D-glyceraldehyde-3-phosphate dehydrogenase. , 1977, The Journal of biological chemistry.
[89] D. Kabat,et al. Mechanism of action of Pseudomonas aeruginosa exotoxin Aiadenosine diphosphate-ribosylation of mammalian elongation factor 2 in vitro and in vivo , 1977, Infection and immunity.
[90] J. Knowles,et al. Evolution of enzyme function and the development of catalytic efficiency. , 1976, Biochemistry.
[91] W. Trommer,et al. A transition state analogue for two pyruvate metabolizing enzymes, lactate dehydrogenase and alanine dehydrogenase. , 1976, Biochemistry.
[92] F. Schuber,et al. Calf-Spleen Nicotinamide-Adenine Dinucleotide Glycohydrolase Kinetic Mechanism , 1976 .
[93] F. Schuber,et al. The stereochemistry of calf spleen NAD‐glycohydrolase‐catalyzed NAD methanolysis , 1976, FEBS letters.
[94] J. Klinman. Isotope effects and structure-reactivity correlations in the yeast alcohol dehydrogenase reaction. A study of the enzyme-catalyzed oxidation of aromatic alcohols. , 1976, Biochemistry.
[95] F. Schuber,et al. Calf-spleen nicotinamide--adenine dinucleotide glycohydrolase. Solubilization purification and properties of the enzyme. , 1976, European journal of biochemistry.
[96] R. A. Neal,et al. An examination of octanol and octanal metabolism to octanoic acid by horse liver alcohol dehydrogenase. , 1975, Biochimica et biophysica acta.
[97] S. Forsén,et al. The solution conformation of nicotinamide mononucleotide: a quantitative application of the nuclear Overhauser effect. , 1975, Biochemistry.
[98] N. Oppenheimer,et al. The alpha beta epimerization of reduced nicotinamide adenine dinucleotide. , 1975, Archives of biochemistry and biophysics.
[99] S. Taylor,et al. Structure-function relationships in lactate dehydrogenase. , 1973, Proceedings of the National Academy of Sciences of the United States of America.
[100] M. Sinnott,et al. The effect of methanol and dioxan on the rates of the beta-galactosidase-catalysed hydrolyses of some beta-D-galactrophyranosides: rate-limiting degalactosylation. The ph-dependence of galactosylation and degalactosylation. , 1973, The Biochemical journal.
[101] M. Wilchek,et al. Covalent coupling of nucleotides to agarose for affinity chromatography. , 1973, Biochimica et biophysica acta.
[102] R. Sarma,et al. Conformation of pyridine nucleotides studied by phosphorus-31 and hydrogen-1 fast Fourier transform nuclear magnetic resonance spectroscopy. I. Oxidized and reduced mononucleotides. , 1973, Journal of the American Chemical Society.
[103] J. H. Yuan,et al. Bull semen nicotinamide adenine dinucleotide nucleosidase. V. Kinetic studies. , 1973, The Journal of biological chemistry.
[104] R. A. Neal,et al. An examination of the oxidation of aldehydes by horse liver alcohol dehydrogenase. , 1972, The Journal of biological chemistry.
[105] G. Lienhard,et al. A transition state analog for lysozyme. , 1972, The Journal of biological chemistry.
[106] N. Oppenheimer,et al. A structure of pyridine nucleotides in solution. , 1971, Proceedings of the National Academy of Sciences of the United States of America.
[107] N. Gupta. A study of formaldehyde dismutation by liver alcohol dehydrogenase with NAD plus-analogs. , 1970, Archives of biochemistry and biophysics.
[108] L. Kohn,et al. The structural properties of spinach leaf glyoxylic acid reductase. , 1970, The Journal of biological chemistry.
[109] W. Warren. Catalysis of both oxidation and reduction of glyoxylate by pig heart lactate dehydrogenase isozyme 1. , 1970, The Journal of biological chemistry.
[110] K. Tipton,et al. The oxidation and reductn of glyoxylate by lactic dehydrogenase. , 1969, European journal of biochemistry.
[111] C. Woenckhaus,et al. Die intramolekulare Wechselwirkung in Coenzymen, III. Nicotinamid‐pentamethylen‐adenosin‐pyrophosphat , 1966 .
[112] I. Karle. The crystal structure of N‐benzyl‐l,4‐dihydronicotinamide , 1961 .
[113] R. Abeles,et al. The dismutation of formaldehyde by liver alcohol dehydrogenase. , 1960, The Journal of biological chemistry.
[114] H. Levy,et al. The stereospecificity of enzymatic hydrogen transfer from diphosphopyridine nucleotide. , 1957, The Journal of biological chemistry.
[115] N. Kaplan,et al. Reaction of pyridine nucleotide analogues with dehydrogenases. , 1956, The Journal of biological chemistry.
[116] H. F. Fisher,et al. The enzymatic transfer of hydrogen. I. The reaction catalyzed by alcohol dehydrogenase. , 1953, The Journal of biological chemistry.
[117] A. N. Ramanathan,et al. Liver alcohol dehydrogenase and ester formation. , 1952, The Biochemical journal.
[118] E. Racker,et al. The mechanism of oxidation of aldehydes by glyceralde-hyde-3-phosphate dehydrogenase. , 1952, The Journal of biological chemistry.
[119] Dilip K. Kondepudi,et al. The Handedness of the Universe. , 1990 .
[120] S. Benner,et al. Interpreting the behavior of enzymes: purpose or pedigree? , 1988, CRC critical reviews in biochemistry.
[121] G Pettersson,et al. Liver alcohol dehydrogenase. , 1987, CRC critical reviews in biochemistry.
[122] N. Oppenheimer,et al. Stereospecificity for nicotinamide nucleotides in enzymatic and chemical hydride transfer reactions. , 1985, CRC critical reviews in biochemistry.
[123] M. Gamasa,et al. Evidence supporting a single electron transfer pathway in the cannizzaro reaction , 1983 .
[124] E. C. Ashby,et al. Evidence supporting a single electron transfer pathway in the reduction of aromatic ketones by metal alkoxides. Lithium isopropoxide, an excellent reducing agent for aromatic ketones. , 1982 .
[125] J. Klinman,et al. Probes of mechanism and transition-state structure in the alcohol dehydrogenase reaction. , 1981, CRC critical reviews in biochemistry.
[126] J. Moss,et al. Activation of adenylate cyclase by choleragen. , 1979, Annual review of biochemistry.
[127] F. Schuber,et al. ADP‐ribonolactone: A potential activated intermediate analogue of NAD‐glycohydrolase , 1977, FEBS letters.
[128] H. Gutfreund. Kinetic analysis of the properties and reactions of enzymes. , 1975, Progress in biophysics and molecular biology.
[129] N. Gupta,et al. Coupled oxidation-reduction activity of liver alcohol dehydrogenase. , 1966, Biochimica et biophysica acta.
[130] George S. Hammond,et al. A Correlation of Reaction Rates , 1955 .