6 Catalytic Strategies in Enzymic Carboxylation and Decarboxylation

[1]  J. Peliska,et al.  Synthesis and study of (Z)-3-chlorophosphoenolpyruvate. , 1990, Archives of biochemistry and biophysics.

[2]  S. Kuby.  A Study of enzymes , 1990 .

[3]  J. Robertus,et al.  Site-directed alteration of Glu197 and Glu66 in a pyruvoyl-dependent histidine decarboxylase. , 1989, Protein engineering.

[4]  M. Hackert,et al.  Pyruvoyl-dependent histidine decarboxylase. Active site structure and mechanistic analysis. , 1989, The Journal of biological chemistry.

[5]  W. Cleland,et al.  Steady-state kinetic studies of the metal ion-dependent decarboxylation of oxalacetate catalyzed by pyruvate kinase. , 1989, Archives of biochemistry and biophysics.

[6]  G. Schneider,et al.  Crystal structure of the active site of ribulose-bisphosphate carboxylase , 1989, Nature.

[7]  G. Lorimer,et al.  Carbonyl sulfide: an alternate substrate for but not an activator of ribulose-1,5-bisphosphate carboxylase. , 1989, The Journal of biological chemistry.

[8]  D. Gonzalez,et al.  The use of substrate analogues to study the active-site structure and mechanism of PEP carboxylase , 1989 .

[9]  V. Kansal.  Biophosphates and their analogues: Synthesis, structure, metabolism and activity: edited by K.S. Bruzik and W.J. Stec. Vol. 3, pp. 598, 1987. Elsevier, Amsterdam, US$ 155.50, Dft. 350.00 , 1989 .

[10]  M. O'Leary.  Multiple isotope effects on enzyme-catalyzed reactions. , 1989, Annual review of biochemistry.

[11]  J. Knowles.  The mechanism of biotin-dependent enzymes. , 1989, Annual review of biochemistry.

[12]  J. Knowles,et al.  On the intermediacy of carboxyphosphate in biotin-dependent carboxylations. , 1988, Biochemistry.

[13]  L. Abell,et al.  Isotope effect studies of the pyridoxal 5'-phosphate dependent histidine decarboxylase from Morganella morganii. , 1988, Biochemistry.

[14]  L. Abell,et al.  Isotope effect studies of the pyruvate-dependent histidine decarboxylase from Lactobacillus 30a. , 1988, Biochemistry.

[15]  W. Jencks,et al.  Thiazolium C(2)-proton exchange: structure-reactivity correlations and the pKa of thiamin C(2)-H revisited. , 1988, Biochemistry.

[16]  M S Chapman,et al.  Tertiary structure of plant RuBisCO: domains and their contacts. , 1988, Science.

[17]  G. H. Reed,et al.  Coordination of manganous ion at the active site of pyruvate, phosphate dikinase: the complex of oxalate with the phosphorylated enzyme. , 1988, Biochemistry.

[18]  F. C. Hartman,et al.  Evidence supporting lysine 166 of Rhodospirillum rubrum ribulosebisphosphate carboxylase as the essential base which initiates catalysis. , 1988, The Journal of biological chemistry.

[19]  W. Cleland,et al.  Isotope effect studies of the chemical mechanism of pig heart NADP isocitrate dehydrogenase. , 1988, Biochemistry.

[20]  M. O'Leary,et al.  Reaction of phosphoenolpyruvate carboxylase with (Z)-3-bromophosphoenolpyruvate and (Z)-3-fluorophosphoenolpyruvate , 1988 .

[21]  D. Gonzalez,et al.  Identification of 2-enolbutyrate as the product of the reaction of maize leaf phosphoenolpyruvate carboxylase with (Z)- and (E)-2-phosphoenolbutyrate: evidence from NMR and kinetic measurements , 1988 .

[22]  S. Benner,et al.  The stereospecificity of oxaloacetate decarboxylase: a stereochemical imperative? , 1987 .

[23]  R. Kluger,et al.  Thiamin diphosphate: a mechanistic update on enzymic and nonenzymic catalysis of decarboxylation , 1987 .

[24]  P. Christen,et al.  The stereospecific labilization of the C-4' pro-S hydrogen of pyridoxamine 5'-phosphate is abolished in (Lys258----Ala) aspartate aminotransferase. , 1987, The Journal of biological chemistry.

[25]  C. Perrin,et al.  Proton exchange in biotin: a reinvestigation, with implications for the mechanism of carbon dioxide transfer , 1987 .

[26]  J. Hermes,et al.  Determination of substrate specificity of carboxylases by nuclear magnetic resonance. , 1987, Analytical biochemistry.

[27]  F. C. Hartman,et al.  Function of Lys-166 of Rhodospirillum rubrum ribulosebisphosphate carboxylase/oxygenase as examined by site-directed mutagenesis. , 1987, The Journal of biological chemistry.

[28]  A. Iglesias,et al.  Higher plant phosphoenolpyruvate carboxylase , 1987 .

[29]  J. Holtum,et al.  CO2 is the inorganic carbon substrate of NADP malic enzymes from Zea mays and from wheat germ. , 1987, European journal of biochemistry.

[30]  M. S. Chapman,et al.  Sliding-layer conformational change limited by the quaternary structure of plant RuBisCO , 1987, Nature.

[31]  G. Schneider,et al.  Three‐dimensional structure of ribulose‐1,5‐bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum at 2.9 Å resolution , 1986, The EMBO journal.

[32]  J. Knowles,et al.  Biotin-dependent carboxylation catalyzed by transcarboxylase is a stepwise process. , 1986, Biochemistry.

[33]  W. Cleland,et al.  Carbon isotope effects on the metal ion catalyzed decarboxylation of oxalacetate , 1986 .

[34]  J. Schloss,et al.  Deuterium isotope effects in the carboxylase reaction of ribulose-1,5-bisphosphate carboxylase/oxygenase , 1986 .

[35]  G. Lorimer,et al.  Reaction intermediate partitioning by ribulose-bisphosphate carboxylases with differing substrate specificities. , 1986, The Journal of biological chemistry.

[36]  M. O'Leary,et al.  Solvent dependence of the carbon kinetic isotope effect on the decarboxylation of 4-pyridylacetic acid. A model for enzymatic decarboxylations , 1986 .

[37]  G. S. Reddy,et al.  Kinetic mechanism of ribulosebisphosphate carboxylase: evidence for an ordered, sequential reaction , 1986 .

[38]  G. S. Reddy,et al.  The sites for catalysis and activation of ribulosebisphosphate carboxylase share a common domain. , 1986, Archives of biochemistry and biophysics.

[39]  J. Knowles,et al.  Enzymatic biotin-mediated carboxylation is not a concerted process , 1986 .

[40]  F. Wedler,et al.  Manganese in metabolism and enzyme function , 1986 .

[41]  J. Kirsch,et al.  Site-directed mutagenesis of aspartate aminotransferase from E. coli. , 1985, Biochemical and biophysical research communications.

[42]  B. Miller,et al.  Influence of Acetate Buffers and Metal Ions on Ketonization Rates of Enolpyruvate: A Further Test of the Marcus Function. , 1985 .

[43]  S. Tanase,et al.  Purification and properties of a pyridoxal 5'-phosphate-dependent histidine decarboxylase from Morganella morganii AM-15. , 1985, The Journal of biological chemistry.

[44]  N. Xuong,et al.  Structure determination of histidine decarboxylase from Lactobacillus 30a at 3.0 A resolution. , 1985, Journal of molecular biology.

[45]  M. O'Leary,et al.  Carbon isotope effect on carboxylation of ribulose bisphosphate catalyzed by ribulosebisphosphate carboxylase from Rhodospirillum rubrum. , 1985, Biochemistry.

[46]  W. Cleland,et al.  Use of intermediate partitioning to calculate intrinsic isotope effects for the reaction catalyzed by malic enzyme. , 1985, Biochemistry.

[47]  J. Morrison,et al.  Mechanisms of enzymatic and acid-catalyzed decarboxylations of prephenate. , 1984, Biochemistry.

[48]  W. Cleland,et al.  Use of multiple isotope effects to study the mechanism of 6-phosphogluconate dehydrogenase. , 1984, Biochemistry.

[49]  M. O'Leary,et al.  Carbon isotope effects on enzyme-catalyzed carboxylation of ribulose bisphosphate , 1984 .

[50]  W. Cleland,et al.  Variation of transition-state structure as a function of the nucleotide in reactions catalyzed by dehydrogenases. 2. Formate dehydrogenase. , 1984, Biochemistry.

[51]  S. Benner,et al.  Stereochemical imperative in enzymic decarboxylations. Stereochemical course of the decarboxylation catalyzed by acetoacetate decarboxylase , 1984 .

[52]  D. Leussing,et al.  Application of Marcus theory to metal ion catalyzed group transfer reactions , 1984 .

[53]  G. Eichele,et al.  Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure. , 1984, Journal of molecular biology.

[54]  N. Fujita,et al.  Reaction mechanism of phosphoenolpyruvate carboxylase. Bicarbonate-dependent dephosphorylation of phosphoenol-alpha-ketobutyrate. , 1984, Biochemistry.

[55]  H. Miziorko,et al.  Electron spin resonance studies of ribulosebisphosphate carboxylase: identification of activator cation ligands. , 1984, Biochemistry.

[56]  D. Jordan,et al.  Species variation in kinetic properties of ribulose 1,5-bisphosphate carboxylase/oxygenase. , 1983, Archives of biochemistry and biophysics.

[57]  G. Lorimer,et al.  Ribulose-1,5-bisphosphate carboxylase-oxygenase. , 1983, Annual review of biochemistry.

[58]  J. Knowles,et al.  The stereochemical course at phosphorus of the reaction catalyzed by phosphoenolpyruvate carboxylase. , 1982, The Journal of biological chemistry.

[59]  J. Knowles,et al.  Ribulose-1,5-bisphosphate carboxylase: primary deuterium kinetic isotope effect using [3-2H]ribulose 1,5-bisphosphate. , 1982, Biochemistry.

[60]  W. Cleland,et al.  Use of multiple isotope effects to determine enzyme mechanisms and intrinsic isotope effects. Malic enzyme and glucose-6-phosphate dehydrogenase. , 1982, Biochemistry.

[61]  M. O'Leary.  Phosphoenolpyruvate Carboxylase: An Enzymologist's View , 1982 .

[62]  T. Nowak,et al.  Phosphoenolpyruvate carboxykinase. Mn2+ and Mn2+ substrate complexes. , 1982, The Journal of biological chemistry.

[63]  J. Rétey,et al.  Stereospecificity in organic chemistry and enzymology , 1982 .

[64]  J. N. Butler,et al.  Carbon Dioxide Equilibria and their Applications , 1982 .

[65]  M. O'Leary,et al.  Kinetic and isotope effect studies of maize phosphoenolpyruvate carboxylase. , 1981, Biochemistry.

[66]  D. Jordan,et al.  Species variation in the specificity of ribulose biphosphate carboxylase/oxygenase , 1981, Nature.

[67]  M. O'Leary,et al.  Medium effects in enzyme-catalyzed decarboxylations. , 1981, Biochemistry.

[68]  井上 祥平,et al.  Organic and bio-organic chemistry of carbon dioxide , 1981 .

[69]  J. Vederas,et al.  Stereochemistry of pyridoxal phosphate catalyzed enzyme reactions , 1980 .

[70]  G. Eichele,et al.  Three-dimensional structure of a pyridoxal-phosphate-dependent enzyme, mitochondrial aspartate aminotransferase. , 1980, Proceedings of the National Academy of Sciences of the United States of America.

[71]  J. Staunton,et al.  Studies of enzyme-mediated reactions. Part 13. Stereochemical course of the formation of histamine by decarboxylation of (2S)-histidine with enzymes from Clostridium welchii and Lactobacillus 30a. , 1980, Journal of the Chemical Society. Perkin transactions 1.

[72]  J. Vederas,et al.  Stereospecificity of sodium borohydride reduction of tyrosine decarboxylase from Streptococcus faecalis. , 1979, The Journal of biological chemistry.

[73]  I. A. Rose,et al.  Evidence that carboxyphosphate is a kinetically competent intermediate in the carbamyl phosphate synthetase reaction. , 1979, The Journal of biological chemistry.

[74]  F. Jordan,et al.  Carbon-13 kinetic isotope effects on pyruvate decarboxylation. II. Solvent effects in model systems , 1978 .

[75]  V. Schramm,et al.  Kinetic mechanism of phosphoenolpyruvate carboxykinase (GTP) from rat liver cytosol. Product inhibition, isotope exchange at equilibrium, and partial reactions. , 1978, The Journal of biological chemistry.

[76]  F. Jordan,et al.  Carbon Kinetic Isotope Effects on Pyruvate Decarboxylation Catalyzed by Yeast Pyruvate Decarboxylase and Models , 1978 .

[77]  H. Yamada,et al.  Stereochemistry of reactions catalyzed by glutamate decarboxylase. , 1978, Biochemistry.

[78]  M. O'Leary,et al.  Specificity in enzymatic decarboxylation. , 1978, Journal of the American Chemical Society.

[79]  R. Schowen,et al.  Transition States of Biochemical Processes , 1978, Springer US.

[80]  M. J. Deniro,et al.  Mechanism of carbon isotope fractionation associated with lipid synthesis. , 1977, Science.

[81]  M. O'Leary.  Carbon isotope effect of the enzymatic decarboxylation of pyruvic acid. , 1976, Biochemical and biophysical research communications.

[82]  A. Mildvan,et al.  Mechanism of malic enzyme from pigeon liver. Magnetic resonance and kinetic studies of the role of Mn2+. , 1976, The Journal of biological chemistry.

[83]  H. G. Wood,et al.  Transcarboxylase: role of biotin, metals, and subunits in the reaction and its quaternary structure. , 1976, CRC critical reviews in biochemistry.

[84]  I. A. Rose,et al.  Oxalacetate decarboxylase activity in muscle is due to pyruvate kinase. , 1976, The Journal of biological chemistry.

[85]  W. Cleland,et al.  Equilibrium perturbation by isotope substitution. , 1975, Biochemistry.

[86]  D. Kemp,et al.  Physical organic chemistry of benzisoxazoles. III. Mechanism and the effects of solvents on rates of decarboxylation of benzisoxazole-3-carboxylic acids , 1975 .

[87]  F. Dallocchio,et al.  A multiple role for the coenzyme in the mechanism of action of 6-phosphogluconate dehydrogenase. The oxidative decarbosylation of 2-deoxy-6-phosphogluconate. , 1973, The Journal of biological chemistry.

[88]  K. Dalziel,et al.  Studies of 6-phosphogluconate dehydrogenase from sheep liver. 2. Kinetics of the oxidative-decarboxylation reaction, coenzyme binding and analyses for metals. , 1972, European journal of biochemistry.

[89]  M. O'Leary,et al.  Acetoacetate decarboxylase. Identification of the rate-determining step in the primary amine catalyzed reaction and in the enzymic reaction. , 1972, Journal of the American Chemical Society.

[90]  A. Braunstein,et al.  The stereochemistry of the abortive transmination shown by glutamate decarboxylase , 1971, FEBS letters.

[91]  Schmidt De,et al.  PK of the lysine amino group at the active site of acetoacetate decarboxylase. , 1971 .

[92]  G. Lienhard,et al.  Mechanisms of thiamine-catalyzed reactions. Decarboxylation of 2-(1-carboxy-1-hydroxyethyl)-3,4-dimethylthiazolium chloride. , 1970, Journal of the American Chemical Society.

[93]  F. C. Størmer,et al.  Acetolactate Decarboxylase from Aerobacter aerogenes , 1970 .

[94]  R. Laursen,et al.  The active site of cetoacetate decarboxylase. , 1966, Journal of the American Chemical Society.

[95]  M. Lane,et al.  The enzymatic carboxylation of phosphoenolpyruvate. I. Purification and properties of phosphoenolpyruvate carboxylase. , 1966, The Journal of biological chemistry.

[96]  H. Dunathan.  Conformation and reaction specificity in pyridoxal phosphate enzymes. , 1966, Proceedings of the National Academy of Sciences of the United States of America.

[97]  F. Westheimer,et al.  Acetoacetate decarboxylase. Identification of lysine at the active site. , 1966, Biochemistry.

[98]  D. Feingold,et al.  Biosynthesis of uridine diphosphate D-xylose. II. Uridine diphosphate D-glucuronate carboxy-lyase of Cryptococcus laurentii. , 1966, Biochemistry.

[99]  D. Feingold,et al.  Biosynthesis of Uridine Diphosphate D-Xylose. I. Uridine Diphosphate Glucuronate Carboxy-lyase of Wheat Germ* , 1965 .

[100]  E. Snell,et al.  Pyridoxal-catalyzed decarboxylation of amino acids. , 1962, Biochemistry.

[101]  L. F. Hass,et al.  Mechanism of the propionyl carboxylase reaction. II. Isotopic exchange and tracer experiments. , 1962, The Journal of biological chemistry.

[102]  F. Westheimer,et al.  ON THE MECHANISM OF THE ENZYMATIC DECARBOXYLATION OF ACETOACETATE1 , 1959 .

[103]  P. Bartlett,et al.  CONTROLLED FORMATION OF cis- AND trans- DECALIN-9-CARBOXYLIC ACIDS BY CARBONYLATION , 1959 .

[104]  Ronald Breslow,et al.  On the Mechanism of Thiamine Action. IV.1 Evidence from Studies on Model Systems , 1958 .

[105]  M. Calvin.  The photosynthetic carbon cycle , 1956 .

[106]  F. Loewus,et al.  The mechanism of enzymatic carbon dioxide fixation into oxal-acetate. , 1954, The Journal of biological chemistry.