Jack Preiss: Papers

Papers Published or in Press

In refereed journals

l.Preiss, J., and P. Handler. Enzymatic synthesis of NMN. J.Biol. Chem. 225, 759, (l957).

2.Preiss, J., and P. Handler. Synthesis in Diphosphopyridine Nucleotide from Nicotinic acid by human erythrocytes in vitro. J. American Chem. Soc. 79, l5l4 (l957).

3.Preiss, J., and P. Handler. Intermediates in the synthesis of Diphosphopyridine Nucleotide from nicotinic acid. J. American Chem.Soc. 79, 4246 (l957).

4.Preiss, J., and P. Handler. Biosynthesis of DPN. I. Identification of intermediates. J. Biol. Chem. 233, 488 (l958)

5.Preiss, J., and P. Handler. Biosynthesis of DPN. II. Enzymatic aspects. J.Biol. Chem. 233, 493 (l958).

6.Preiss, J., P. Berg, J. Ofengand, F.H., Bergmann, and M. Dieckmann. The chemical nature of the RNA-amino acid compound formed by amino acid-activating enzymes. Proc. Nat. Acad. Sci. 45, 319 (l959).

7.Preiss, J., M. Dieckmann, and P. Berg. The enzymatic synthesis of amino acyl derivative of ribonucleic acid. IV. The formation of the 3'-hydroxyl terminal trinucleotide sequence of amino acceptor ribonucleic acid. The Journal of Biological Chemistry 236, l748 (l96l).

8. Preiss, J., and G. Ashwell. Alginic acid metabolism in bacteria.I.Enzymatic formation of unsaturated oligosaccharides and 4-deoxy-L-erythro-5-hexoseulose uronic acid. J. Biol. Chem. 237, 309 (l962).

9.Preiss, J., and G. Ashwell. Aliginic acid metabolism in bacteria. II. Enzymatic reduction of 4-deoxy-L-erythro-5-hexoseulose uronic acid to 2-keto-3-deoxy-D-gluconic acid. J. Biol. Chem. 237, 317 (l962).

l0.Preiss, J., and G. Ashwell. 3-deoxy-D-glycero-2,5-hexodiulosonic acid, a new intermediate in the metabolism of polygalacturonate. Biochem. Biophys. Res. Commun. 8, 357 (l962).

ll Preiss, J. Oxidation of GDP-mannose to GDP-mannuronate. Biochem. Biophys. Res. Commun. 9, 235 (l962).

l2.Preiss, J., and G. Ashwell. Polygalacturonic acid metabolism in bacteria. I. Enzymatic formation of 4-deoxy-L-threo-5-hexoseulose uronic acid. J. Biol. Chem. 238, l57l (l962).

l3.Preiss, J., and G. Ashwell. Polygalacturonic acid metabolism in bacteria. II. Formation and metabolism of 3-deoxy-D-glycero-2,5-hexodiulosonic acid. J. Biol. Chem. 238, l577 (l962).

l4.Shen, L., and J. Preiss. The activation and inhibition of bacterial adenosine-diphosphoglucose pyrophosphorylase. Biochem. and Biophys. Res. Commun. 17, 424 (l964).

l5.Shen, L., H.P. Ghosh, E. Greenberg, and J. Preiss. Adenosine diphosphate glucose-glycogen transglucosylase in Arthrobacter sp. NRRL B l973. Biochim. Biophys. Acta 89, 370 (l964).

l6.Preiss, J., and E. Wood. Sugar nucleotide reactions in Arthrobacter. I. Guanosine diphosphate mannose pyrophosphorylase: Purification and properties. J. Biol. Chem. 139, 3119 (l964).

l7.Preiss, J. Sugar nucleotide reactions in Arthrobacter. II. Biosynthesis of guanosine diphosphomannuronate. The Journal of Biological Chemistry 239, 3127 (l964).

l8.Preiss,J.,L.Shen,andM.Partridge.The activation of Escherichicia coli ADP-glucose pyrophosphorylase. Biochem. Biophys. Res. Commun. l8, l80 (l965).

l9.Greenberg, E., and J. Preiss. The occurrence of adenosine diphosphate glucose: Glycogen transglucosylase in bacteria. J. Biol. Chem. 239, 43l4 (l964).

20.Ghosh, H.P., and J. Preiss. The biosynthesis of starch in spinach chloroplasts. J. Biol. Chem. 240, 96l (l965).

2l.Shen, L. and Preiss,J. Biosynthesis of bacterial glycogen.I.Purification and properties of the adenosine diphosphoglucose pyrophosphorylase of Arthrobacter species NRRL B l973. J.Biol. Chem. 240, 2334 (l965).

22.Greenberg, E., and J. Preiss. Biosynthesis of bacterial glycogen. II. Purification and properties of the adenosine diphosphoglucose: Glycogen transglucosylase of Arthrobacter species NRRL B l973. J. Biol. Chem. 240, 234l (l965).

23.H.P. Ghosh and Preiss, J. Biosynthesis of starch in spinach chloroplasts. Biochem. 4, l354 (l965).

24.H.P. Ghosh and Preiss, J. The isolation and characterization of glycogen from Arthrobacter species NRRL B l973. Biochim. Biophys. Acta l04, 274 (l965).

25.Preiss, J., and E. Greenberg. Biosynthesis of bacterial glycogen. III. The adenosine diphosphate glucose: a-4-glucosyl transferase of Escherichia coli B. Biochem. 4, 2328 (l965).

26.Preiss, J., L. Shen, E. Greenberg, and N. Gentner. Biosynthesis of bacterial glycogen. IV. Activation and inhibition of the adenosine diphosphate glucose pyrophosphorylase of Escherichia coli B. Biochem. 5, 1833 (l966).

27.Ghosh, H.P., and J. Preiss. Adenosine diphosphate glucose pyrophosphorylase. A regulatory enzyme in the biosynthesis of starch in spinach chloroplasts. J. Biol. Chem. 241, 4491-4505 (l966).

28.Shen, L., and J. Preiss. Biosynthesis of bacterial glycogen. V. The activation and inhibition of the adenosine diphosphate glucose pyrophosphorylase of Arthrobacter viscosus NRRL B l973. Arch. Biochem. Biophys. ll6, 375 (l966).

29.R.L. Spencer and Preiss, J. Biosynthesis of diphosphyridine nucleotide. The purification and the properties of diphosphopyridine nucleotide synthetase from Escherichia coli B. J. Biol. Chem. 242, 385 (l967).

30.Preiss, J., and E. Greenberg. Enzymic synthesis of GDP-mannose-14C from mannose-14C. Anal. Biochem. l8, 464 (l967).

3l.N. Gentner and Preiss, J. Activator-inhibitor interactions in the adenosine diphosphate glucose pyrophosphorylase of Escherichia coli B. Biochem. Biophys. Res. Commun. 27, 417 (l967).

32.Preiss, J., and E. Greenberg. Biosynthesis of starch in Chlorella pyrenoidosa. I. Purification and properties of the adenosine diphosphoglucose: a-l,4-glucan, a-4-glucosyl transferase from Chlorella. Arch. Biochem. Biophys. ll8, 702 (l967).

33.G.G. Sanwal and Preiss, J. Biosynthesis of starch in Chlorella pyrenoidosa. II. Regulation of ATP: a -D-glucose-l-phosphate adenyl transferase (ADP-glucose pyrophosphorylase) by inorganic phosphate and 3-phosphoglycerate. Arch. Biochem. Biophys. ll9, 454 (l967).

34.Preiss, J., M. Biggs, and E. Greenberg. The effect of magnesium ion concentration on the pH optimum of the spinach leaf alkaline fructose diphosphatase. J. Biol. Chem. 242, 2202 (l967).

35.Dahmen, W., B. Webb, and J. Preiss. The deamido-diphosphopyridine nucleotide and diphosphopyridine nucleotide pyrophosphorylase of Escherichia coli and yeast. Arch. Biochem. Biophys. 120, 440 (l967).

36.Sanwal, G., E. Greenberg, J. Hardie, E. Cameron, and J. Preiss. Regulation of starch biosynthesis in plant leaves: Activation and inhibition of ADP-glucose pyrophosphorylase. Plant Physiol. 43, 417 (l968).

37.Gentner, N., and J. Preiss. Biosynthesis of bacterial glycogen. VI. Differences in the kinetic properties of the Escherichia coli B adenosine diphosphate glucose pyrophosphorylase depending on whether Mg++ or Mn++ serves as divalent cation. J. Biol. Chem. 243, 5882 (l968).

38.Govons, S., R. Vinopal, J. Ingraham, and J. Preiss. Isolation of mutants of Escherichia coli B altered in their ability to synthesize glycogen. J. Bacteriol. 97, 970-972 (l969).

39.Dickinson, D., and J. Preiss. ADP glucose pyrophosphorylase from maize endosperm. Arch. Biochem. Biophys. 130, ll9-l28 (l969).

40.Sanwal, G., and J. Preiss. Sugar nucleotides and nucleotide-peptide complexes of Chlorella pyrenoidosa: Isolation and characterization. Phytochem. 8, 707-723 (l969).

41.Furlong, C.E., and J. Preiss. Biosynthesis of bacterial glycogen. VII. Purification and properties of adenosine diphosphoglucose pyrophosphorylase of Rhodospirillum rubrum: J.Biol. Chem. 244, 2539-2548 (l969).

42.Preiss, J., and E. Greenberg. Allosteric regulation of uridine diphosphoglucose:D-fructose-6-phosphate-2-glucosyl transferase (E.C.2.4.l.l4). Biochem. Biophys. Res. Commun. 36,289-295 (l969).

43.Gentner, N., E. Greenberg, and J. Preiss. TPNH and pyridoxal-5'-phosphate: Activators of ADP-glucose pyrophosphorylase of Escherichia coli B. Biochem. Biophys. Res. Commun. 36, 373-380 (l969).

44.Dickinson, D., and J. Preiss. Presence of ADP-glucose pyrophosphorylase in shrunken-2 and brittle-2 mutants of maize endosperm. Plant Physiol. 44, No. 7, l058-l062 (l969).

45.Eidels, L., and J. Preiss. Citrate synthetase: A regulatory enzyme from Rhodopseudomonas capsulata. J. Biol. Chem. 245, 2937-2945 (l970).

46.Eidels, L., P.L. Edelman, and J. Preiss. Biosynthesis of bacterial glycogen. VIII. Activation and inhibition of the adenosine diphosphoglucose pyrophosphorylase of Rhodopseudomonas capsulata and of Agrobacterium tumefaciens. Arch. Biochem. & Biophys. l40, 60-74 (l970).

47.Eidels, L., and J. Preiss. Carbohydrate metabolism in Rhodopseudomonas capsulata: Enzyme titers, glucose metabolism, and polyglucose polymer synthesis. Arch. Biochem. Biophys. l40, 75-89 (l970).

48.Preiss, J., A. Sabraw, and E. Greenberg. An ADP-glucose pyrophosphorylase with lower affinities for substrate and effector molecules in an Escherichia coli B mutant deficient in glycogen synthesis. Biochem. Biophys. Res. Commun. 42, l80-l86 (l97l).

49.Preiss, J., C. Lammel, and A. Sabraw. A unique adenosine diphosphoglucose pyrophosphorylase associated with maize embryo tissue. Plant Physiol. 47, l04-l08 (l97l).

50.Ozbun, J.L., J.S. Hawker and J. Preiss. Multiple forms of a-l,4 glucan synthetase from spinach leaves. Biochem. Biophys. Res. Commun. 43, 63l-636 (l97l).

5l.Ribereau-Gayon, G., A. Sabraw, C. Lammel, and J. Preiss. Biosynthesis of bacterial glycogen IX: Regulatory properties of the adenosine diphosphate glucose pyrophosphorylases of the Enterobacteriaceae. Arch. Biochem. Biophys. l42, 675-692 (l97l).

52.Paule, M.R., and J. Preiss. Biosynthesis of bacterial glycogen X. The kinetic mechanism of adenosine diphosphoglucose pyrophosphorylase from Rhodospirillum rubrum. J. Biol. Chem. 246, 4602-4609 (l97l).

53.Ozbun, J.L., J.S. Hawker, and J. Preiss. Adenosine diphosphoglucose-starch glucosyltransferases from developing kernels of waxy maize. Plant Physiol. 48, 765-769 (l97l).

54.Paule, M.R. (J. Preiss). The effects of temperature on the kinetics of adenosine diphosphoglucose pyrophosphorylase from Rhodospirillum rubrum. Biochem. l0, 4509-4517 (l97l).

55. Ozbun,J.L.,J.S.Hawker,andJ.Preiss.Soluble adenosinediphosphateglucose-a-l,4glucan a- 4-glucosyltransferases from spinach leaves. Biochem. J. l26, 953-963 (l972).

56.Ozbun, J.L., J.S. Hawker, and J. Preiss. Unprimed starch synthesis by soluble ADP glucose-starch glucosyltransferase from potato tubers. Phytochem. ll, l287-l293 (l972).

57.Crawford, I.P., and J. Preiss. Distribution of closely linked markers following intragenic recombination in Escherichia coli. J. Mol. Biol. 7l, 7l7 (l972).

58.Ozbun, J.L., J.S. Hawker, E. Greenberg, C. Lammel, J. Preiss, and E.Y.C. Lee. Starch synthetase, phosporylase, ADP glucose pyrophosphorylase and UDP-glucose pyrophosphorylase in developing maize kernels. Plant Physiol. 5l, l-5 (l973).

59.Fox, J., and L.D. Kennedy, J.S., Hawker, J.L. Ozbun, E. Greenberg, C. Lammel, and J. Preiss. De novo synthesis of bacterial glycogen and plant starch by ADP: a-glucan 4-glucosyl transferase. Ann. N. Y. Acad. Sci. 2l0, 90-l03 (l973).

60.Preiss, J., J.L. Ozbun, J.S. Hawker, and E. Greenberg.ADPG synthetase and ADPG-a-glucan 4-a glucosyl transferase: Enzymes involved in bacterial glycogen and plant starch synthesis. Ann. N. Y. Acad. Sci. 2l0, 265-278 (l973).

6l.Govons, S., N. Gentner, E. Greenberg, and J. Preiss. Biosynthesis of bacterial glycogen. XI. Kinetic characterization of an altered ADP-glucose synthase from a "glycogen excess" mutant of Escherichia coli B. J. Biol. Chem. 248, l73l-l740 (l973).

62.Preiss, J. Studies on the function of a regulatory site using mutants. Intrascience Chemistry Reports 6, l3-22 (l972).

63.Hawker, J.S., J.L. Ozbun, H. Ozaki, E. Greenberg, and J. Preiss. Interaction of spinach leaf adenosine diphosphate glucose a-l, 4-glucan a-4-glucosyl transferase and a-l, 4-glucan, a-l, 4-glucan-6-glycosyl transferase in synthesis of branched a-glucan. Archiv. Biochem. Biophys. l60, 530-55l (l974).

64..Haugen, T., A. Ishaque, A.K. Chatterjee, and J. Preiss. Purification of Escherichia coli ADP-glucose pyrophosphorylase by affinity chromatography. FEBS Letters 42, 205-208 (l974).

65.Preiss, J., A. Sabraw, and E. Greenberg. Biosynthesis of bacterial glycogen: Kinetic studies of a glucose-l-P adenylyl transferase (E.C. 2.7.7.27) from a glycogen deficient mutant of Escherichia coli B. J. Biol. Chem. 250, 763l-7638 (l975).

66.Fox, J., K.K. Kawaguchi, E. Greenberg, and J. Preiss. Biosynthesis of bacterial glycogen: Purification and properties of the Escherichia coli B ADP glucose a-l, 4-glucan a-4 glucosyl transferase. Biochem. l5, 849-856 (l976).

67.Haugen, T., A. Ishaque, and J. Preiss. ADP-glucose pyrophosphorylase: Evidence for a lysine residue at the activator site of the Escherichia coli B enzyme. Biochem. Biophys. Res. Commun. 69, 346-353 (l976).

68.Preiss, J., C. Lammel, and E. Greenberg. Biosynthesis of bacterial glycogen. XIV. Kinetic studies of a glucose-l-P denylyl transferase (E.C. 2.7.7.27) from a glycogen excess mutant of Escherichia coli B. Archiv. Biochem. Biophys. l74, l05-ll9 (l976).

69.Preiss, J., K. Crawford, J. Downey, C. Lammel, and E. Greenberg. Biosynthesis of bacterial glycogen. The kinetic properties of Serratia marcescens ADP-glucose pyrophosphorylase. J. Bacteriol. l27, 193-203 (l976).

70.Haugen, T., A. Ishaque, and J. Preiss. Biosynthesis of bacterial glycogen. Characterization of the subunit structure of Escherichia coli B glucose-l-P adenylyltransferase (E.C. 2.7.7.27). J. Biol. Chem. 25l, 7880-7885 (l976).

7l.Levi, C., and J. Preiss. The regulatory properties of the ADP-glucose pyrophosphorylase of the blue-green bacterium, Synechococcus 630l. Plant Physiol. 58, 753-756 (l976).

72.Carlson, C.A., T.F. Parsons, and J. Preiss. Biosynthesis of bacterial glycogen. Activator induced oligomerization of a mutant Escherichia coli ADP-glucose synthase. J. Biol. Chem. 25l, 7886-7892 (l976).

73.Steiner, K.E., and J. Preiss. Biosynthesis of bacterial glycogen Genetic and allosteric regulation of glycogen biosynthesis in Salmonella typhimurium LT.2. J. Bacteriol. l29, 246-253 (l977).

74.Boyer, C.D., and J. Preiss. Biosynthesis of bacterial glycogen: Purification and properties of the Escherichia coli B. a-l, 4-glucan, a-l,4-glucan-6-glucosyl transferase. Biochem. l6, 2963-3699 (l977).

75.Boyer, C.D., and J. Preiss. Multiple forms of starch branching enzymes of maize: Evidence for independent genetic control. Biochem. Biophys. Res. Commun. 80, l69-l75 (l978).

76.Levi, C., and J. Preiss. Amylopectin degradation in pea chloroplast extracts. Plant Physiol. 6l, 2l8-220 (l978).

77.Su, J-C., and J. Preiss. Purification and properties of sucrose synthase from maize kernels. Plant Physiol. 6l, 389-393 (l978).

78.Boyer, C.D., and J. Preiss. Multiple forms of a-l,4-glucan, a-l,4-glucan-6-glycosyl transferase from develoing Zea mays L. kernels. Carbohyd. Res. 6l, 32l-332 (l978).

79.Parsons, T.F., and J. Preiss. Biosynthesis of bacterial glycogen. Incorporation of pyridoxal phosphate into the allosteric activator site and an ADP-glucose-protected pyridoxal phosphate binding site of Escherichia coli B ADP-glucose synthase. J. Biol. Chem. 253, 6l97-6202 (l978).

80.Kawaguchi, K., J. Fox, E. Holmes, C. Boyer, and J. Preiss. "De novo" synthesis of Escherichia coli glycogen is due to primer associated with glycogen synthase and activation by branching enzyme. Arch. Biochem. Biophys. l90, 385-397 (l978).

8l.Parsons, T.F., and J. Preiss. Biosynthesis of bacterial glycogen. Isolation and characterization of the pyridoxal-P allosteric activator site and the ADP-glucose protected pyridoxal-P binding site of Escherichia coli B ADP-glucose synthase. J. Biol. Chem. 253, 7638-7645 (l978).

82.Haugen, T., and J. Preiss. Biosynthesis of bacterial glycogen. The nature of the binding of substrates and effectors to ADP-glucose synthases. J. Biol. Chem. 254, 127-136 (l979).

83.Okita, T., E. Greenberg, D. Kuhn, and J. Preiss. Subcellular localization of the starch degradative and biosynthetic enzymes of spinach leaves. Plant Physiol. 64, l87-l92 (l979).

84.Holmes, E., and J. Preiss. Characterization of Escherichia coli B glycogen synthase enzymatic reactions and products. Arch. Biochem. Biophys. l96, 436-448 (l979).

85.Boyer, C., and J. Preiss. Properties of citrate stimulated starch synthesis catalyzed by starch synthase I of developing maize kernels. Plant Physiol. 64, l039-l042 (l979).

86.Preiss, J., E. Greenberg, T.F. Parsons and J. Downey. Regulatory properties of the ADP-glucose pyrophosphorylase from Rhodopseudomonas sphaeroides and from Rhodopseudomonas gelatinosa. Arch. Microbiol. l26, 2l-3l (l980).

87.Lehmann, M., and J. Preiss. Biosynthesis of bacterial glycogen: Purification and properties of Salmonella typhimurium LT-2 adenosine diphosphate glucose pyrophosphorylase. J. Bacteriol. l43, l20-l27 (l980).

88.Pollock, C., and J. Preiss. The citrate-stimulated starch synthase of starchy maize kernels: Purification and properties. Arch. Biochem. Biophys. 204, 578-588 (l980).

89.Preiss, J., T.W. Okita, and E. Greenberg. Characterization of the spinach leaf phosphorylases. Plant Physiol. 66, 864-869 (l980).

90.Okita, T. W., and J. Preiss. Starch degradation in spinach leaves. Isolation and characterization of the amylases and R-enzyme of spinach leaves. Plant Physiol. 66, 870-876 (l980).

9l.Boyer, C.D., and J. Preiss. Evidence for independent genetic control of the multiple forms of maize endosperm branching enzymes and starch synthases. Plant Physiol. 67, ll4l-ll45 (l98l).

92.Kappel, W.K. and J. Preiss. Biosynthesis of bacterial glycogen. Purification and characterization of ADP-glucose pyrophosphorylase with modified regulatory properties from Escherichia coli B mutant CLll36-504 . Arch. Biochem. Biophys. 209, l5-28 (l98l).

93.Okita, T.W., R.L. Rodriguez, and J. Preiss. Cloning of the Glycogen Biosynthetic enzyme structural genes of Escherichia coli. J. Biol. Chem. 256, 6944-6952 (l98l).

94.Yung, S-G., and J. Preiss. Biosynthesis of bacterial glycogen: Purification and structural properties of Rhodospirillum tenue ADP-glucose synthetase. J. Bacteriol. l47, l0l-l09 (l98l).

95.Preiss, J. and E. Greenberg. Biosynthesis of bacterial glycogen: The activator specificity of the ADP-glucose pyrophosphorylases from the genus Rhodospirillum. J. Bacteriol, l47, 7ll-7l9 (l98l).

96.Copeland, L., and J. Preiss. Purification of spinach leaf ADP-glucose pyrophosphorylase. Plant Physiol. 68, 966-l00l (l98l).

97.Carlson, C., and J. Preiss. Alteration of the regulatory and molecular properties of E. coli B ADP-glucose synthase upon selective modification by trinitrobenzenesulfonate. Biochem, 20, 75l9-7527 (l98l).

98.Carlson, C.A. and J. Preiss. Involvement of arginine residues in the allosteric activation of Escherichia coli ADP-glucose synthetase. Biochem. 2l, l929 (l982).

99.Amir, J., and J. Preiss. Kinetic characterization of spinach leaf sucrose-phosphate synthase. Plant Physiology 69, l027-l030 (l982).

l00.Preiss, J. Regulation of the biosynthesis and degradation of starch. Annual Review of Plant Physiology 54, 43l-454 (l982).

l0l.Sowokinos, J.R., and J. Preiss. Pyrophosphorylases in Solanum tuberosum. III. Purification, structural and catalytic properties of potato tuber ADP-glucose pyrophosphorylase. Plant Physiol. 69, l459-l466 (l982).

l02.Holmes, E., and J. Preiss. Detection of two essential sulfhydryl residues in Escherichia coli B glycogen synthase. Archives of Biochem. Biophys. 2l6, 736-740 (l982).

l03.Yung, S-G., and J. Preiss. Biosynthesis of bacterial glycogen: Purification and structural and immunological properties of Rhodopseudomonas sphaeroides ADP glucose synthetase. J. Bacteriol. l5l, No. 2, 742-749 (l982).

l04.Preiss, J., J. Huebner, and E. Greenberg. Purification and structural properties of Rhodopospirillum rubrum ADP glucose pyrophosphorylase. Current Microbiol. 7, 257-262 (l982).

l05.Holmes, E., C. Boyer, and J. Preiss. Immunological characterization of Escherichia coli B glycogen synthase and branching enzyme and comparison with enzymes from other bacteria. J. Bacteriol. l5l, No. 3, l444-l453 (l982).

l06.Preiss, J., M. Mazelis, and E. Greenberg. Cloning of the asparate-b-semialdehyde dehydrogenase structural gene from Escherichia coli Kl2. Current Microbiol. 7, 263-268 (l982).

l07.Greenberg, E., J.E. Preiss, M. VanBoldrick, and J. Preiss. Biosynthesis of bacterial glycogen: Activator specificity of the ADP glucose pyrophosphorylase of Rhodopseudomonads. Arch. Biochem. Biophys. 220, 594-604 (l983).

l08.Urbanowski, J., P. Leung, H. Weissbach, and J. Preiss. The in vitro expression of the gene for Escherichia coli ADP glucose pyrophosphorylase is stimulated by cyclic-AMP and cyclic-AMP receptor protein. J. Biol. Chem. 258, 2782-2784 (l983).

l09.Baecker, P.A., C.E. Furlong, and J. Preiss. Biosynthesis of bacterial glycogen: Primary structure of Escherichia coli ADP-glucose synthetase as deduced from the nucleotide sequence of the glg C gene. J. Biol. Chem. 258, 5084-5088 (l983).

ll0.MacDonald, F.D., and J. Preiss. Solubilization of the starch-granule-bound starch synthase of normal maize kernels. Plant Physiol. 73, l75-l78 (l983).

lll.Preiss, J., and E. Greenberg. Pyrophosphate may be involved in regulation of bacterial glycogen synthesis. Biochem. Biophys. Res. Commun. ll5, 820-826 (l983).

ll2.Preiss, J., S.G. Yung, and P.A. Baecker. Regulation of bacterial glycogen synthesis. J. Mol. Cell. Biochem. 57, 6l-80 (l983).

ll3.Hammond, J.B.W., and J. Preiss. Spinach leaf intra and extra chloroplast phosphorylase activities during growth. Plant Physiol. 73, 709-712 (l983).

ll4.Robinson, N.L., E. Zeiger, and J. Preiss. Regulation of ADPglucose synthesis in guard cells of Commelina communis. Plant Physiol. 73, 862-864 (l983).

ll5.Hammond, J.B.W., and J. Preiss. ATP dependent proteolytic activity from spinach leaves. Plant Physiol. 73, 902-905 (l983).

ll6.Preiss, J. Starch, sucrose biosynthesis and partition of carbon in plants are regulated by orthophosphate and triose-phosphate. Trends in Biochem. Sci. 9, No. l, 24-27 (l984).

ll7.Singh, B.K., E. Greenberg, and J. Preiss. ADPglucose pyrophosphorylase from the CAM, plants, Hoya carnosa and Xerosicyos danguyi. Plant Physiol. 74, 7ll-7l6 (l984).

ll8.Yung, S.G., M. Paule, R. Beggs, E. Greenberg, and J. Preiss. Biosynthesis of bacterial glycogen: Characterization of adenosine diphosphate glucose synthetase from Enterobacter hafniae and Aeromonas hydrophila. Arch. Microbiol. l38, l-8 (l984).

ll9.Preiss, J. Bacterial glycogen synthesis and its regulation. Annual Reviews of Microbiology 38, 4l9-458 (l984).

l20.Robinson, N. and Preiss, J. Biochemical phenomena associated stomatal function. Physiol. Plant. 64, l4l-l46 (l985).

l2l.Macdonald, F.D. and Preiss, J. Partial purification and characterization of granule-bound starch synthases from normal and waxy maize. Plant Physiol. 79, 34-40 (l985).

l22.Singh, B.K. and Preiss, J. Starch branching enzymes from maize: Immunological characterization using polyclonal and monoclonal antibodies. Plant Physiol. 78, 849-852 (l985).

l23.Lee, Y.M. and Preiss, J. Covalent modification of substrate binding sites of E. coli ADPglucose synthetase: Isolation and structural characterization of 8-azido ADPglucose incorporated peptides. J. Biol. Chem. 26l, l058-l064 (l986).

l24.Lee, Y.M., Mukerhjee, S., and Preiss, J. Covalent modification of E. coli ADPglucose synthetase with 8-azido substrate analogues. Arch. Biochem. Biophys. 244, 585-595 (l986).

l25.Macdonald, F.D. and Preiss, J. The subcellular location and characteristics of pyrophosphate-fructose-6-phosphate l-phosphotransferase from suspension cultured cells of soybean. Planta l67, 240-245 (l986).

l26.Baecker, P.A., Greenberg, E., and Preiss, J. Biosynthesis of bacterial glycogen: Primary structure of Escherichia coli a-l,4-glucan: a-l,4-glucan 6-glycosyltransferase as deduced from the nucleotide sequence of the glgB gene. J. Biol. Chem 26l, 8738-8743 (l986).

l27.Leung, P., Lee, Y.M., Greenberg, E., Esch, K., Boylan, S., and Preiss, J. Cloning and expression of the Escherichia coli glgC gene from a mutant containing an ADPglucose pyrophosphorylase with altered allosteric properties. J. Bacteriol. l67, 82-88 (l986).

l28.Larsen, C.E. and Preiss, J. Covalent modification of the inhibitor binding site(s) of E. coli ADPglucose synthetase: Specific incorporation of the photoaffinity analog 8-azido AMP. Biochem. 25, 437l-4376 (l986).

l29.Larsen, C.E., Lee, Y.M., and Preiss, J. Covalent modification of the inhibitor binding site(s) of E. coli. ADP glucose synthetase isolation and structural characterization of 8-azido AMP incorporated peptides. J. Biol. Chem. 26l, l5402-l5409 (l986).

l30.Kumar, A., Larsen, C.E., and Preiss, J. Biosynthesis of bacterial glycogen: Primary structure of Escherichia coli ADPglucose: a-l,4-glucan, a-4-glucosyl transferase as deduced from the nucleotide sequence of the glgA gene. J. Biol. Chem. 26l, l6256-l6259 (l986).

l3l.Plaxton, W.C. and Preiss, J. Purification and properties of non-proteolytic degraded ADPglucose pyrophosphorylase from maize endosperm. Plant Physiol. 83, l07-ll2 (l987).

l32.Preiss, J. Fructose 2,6-biosphosphate: Present status and future prospects. Physiol. Plant. 69, 373-376 (l987).

l33.Spilatro, S.R. and Preiss, J. Regulation of starch synthesis in the bundle sheath and mesophyll of Zea mays L. Intracellular compartmentalization of enzymes of starch metabolism and the properties of the ADPglucose pyrophosphorylases. Plant Physiol. 69, 62l-627 (l987).

l34.Leung, P. and Preiss, J. (l987) Cloning of the ADPglucose pyrophosphorylase (glgC) and glycogen synthase (glgA) structural genes Salmonella typhimurium LT2. J. Bacteriol. l69, 4349-4354.

l35.Leung, P. and Preiss, J. (l987) Biosynthesis of bacterial glycogen. Primary structure of Salmonella typhimurium ADPglucose synthetase as deduced from the nucleotide sequence of the glgC gene. J. Bacteriol. l69, 4355-4360.

l36.Morell, M.K., Bloom, M., Knowles, V. and Preiss, J. (l987) Subunit structure of spinach leaf ADPglucose pyrophosphorylase. Plant Physiol. 85, l82-l87.

l37.Robinson, N.L. and Preiss, J. (l987) Localization of carbohydrate metabolizing enzymes in guard cells of Commelina communis. Plant Physiol. 85, 360-364.

l38.Lee, Y.M., Kumar, A. and Preiss, J. (l987) Amino acid sequence of an Escherichia Coli ADPglucose synthetase allosteric mutant as deduced from the DNA sequence of the glgC gene. For the Record; Nucleic Acids Res. l5, l0603.

l39.Morell, M., Bloom, M., and Preiss, J. (l988) Affinity labeling of the allosteric activator site(s) of spinach leaf ADPglucose pyrophosphorylase. J. Biol. Chem, 263, 633-637.

l40.Lin, T.P., Spilatro, S. and Preiss, J. (l988) Subcellular localization and characterization of amylases in Arabidopsis leaf. Plant Physiol. 86, 25l-259.

l4l.Lin, T.P. and Preiss, J. (l988) Characterization of the D-enzyme (4-a-glucanotransferase) in Arabidopsis leaf. Plant Physiol. 86, 260-265.

l42.Lin, T.P., Caspar, T., Somerville, C. and Preiss, J. (l988) Isolation and characterization of a starchless mutant of Arabidopsis thaliana (L) Henyh lacking ADPglucose pyrophosphoylase activity. Plant Physiol. 86, ll3l-ll35.

l43.Kumar, A., Tanaka, T., Lee, Y.M. and Preiss, J. (l988) Biosynthesis of bacterial glycogen: Use of site-directed mutagenesis to probe the role of Tyrosine ll4 in the catalytic mechanism of ADPglucose synthetase from Escherichia coli. J. Biol. Chem. 263, l4634-l4639.

l44.Romeo, T., Kumar, A. and Preiss, J. (l988) Analysis of the Escherichia coli glycogen gene cluster suggests that catabolic enzymes are encoded among the biosynthetic genes. Gene 70, 363-376.

l45.Lin, T-P., Caspar, T., Somerville, C.R. and Preiss, J. (l988) A starch deficient mutant of Arabidopsis thaliana with low ADPglucose pyrophosphorylase activity lacks one of the two subunits of the enzyme. Plant Physiol. 88, ll75-ll8l.

l46.Mulichak, A.M., Skrzypczak-Jankum, E., Rydel, T.J., Tulinsky, A. and Preiss, J. (l988) Crystallization and Preliminary Disfraction Data of Escherichia coli ADPglucose pyrophosphorylase. J. Biol. Chem. 263, l7237-l7238.

l47.Romeo, T. and Preiss, J. (l989) Genetic regulation of glycogen biosynthesis in Escherichia coli: In vitro effects of cAMP and ppGpp and analysis of in vivo transcripts. J. Bacteriol. l7l, 2773-2782.

l48.Kumar, A., Ghosh, P., Lee, Y.M., Hill, M.A. and Preiss, J. (l989) Biosynthesis of bacterial glycogen: determination of the amino acid changes that alter the regulatory properties of a mutant Escherichia coli ADPglucose synthetase. J. Biol. Chem. 264, l0464-l047l

l49.Anderson, J.M., Hnilo, J., Larson, R. Okita, T.W., Morell, M. and Preiss, J. (l989) The encoded primary sequence of a rice seed ADPglucose pyrophosphorylase subunit and its homology to the bacterial enzyme. J. Biol. Chem. 264, l2238-l2242.

l50.Caspar, T., Lin, T.P., Monroe, J., Bernhard, W., Spilatro, S., Preiss, J. and Somerville, C. (l989) Altered regulation of ß-amylase activity in mutants of Arabidopsis with lesions in starch metabolism. Proc. Nati, Acad. Sci. USA, 86, 5830-5833.

l5l.Kim, W.T., Francheschi, V.R., Okita, T.W., Robinson, N.L., Morell, M. and Preiss, J. (l989) Immunocytochemical localization of ADPglucose pyrophosphorylase in developing potato tuber cells. Plant Physiol. 91, 2l7-220.

l52.Furakawa, K., Tagaya, M., Inouye, M., Preiss, J. and Fukui, T. (l990) Identification of Lys l5 at the Active Site in Escherichia coli Glycogen Synthase. Conservation of a Lys-X-Gly-Gly sequence in the Bacterial and Mammalian Enzymes. J. Biol. Chem. 265, 2086-2090.

l53.Preiss, J., Danner, S., Summers, P.S., Morell, M., Barton, C.R., Yang, L. and Neider, M. (l989) Molecular Characterization of the Brittle-2 gene effect on maize endosperm ADPglucose pyrophosphorylase subunits. Plant Physiol. 92, 881-885.

l54.Okita, T.W., Nakata, P.A., Anderson, J.M., Sowokinos, J., Morell, M. and Preiss, J. (l990) The Subunit Structure of Potato Tuber ADPglucose Pyrophosphorylase. Plant Physiol. 93, 785-790.

l55.Gardiol, A. and Preiss, J. (1990) Escherichia coli E-39 ADPglucose Synthetase has Different Activation Kinetics from the Wild Type Allosteric Enzyme. Arch. Biochem. Biophys. 280, 175-180.

l56.Romeo, T., Black, J. and Preiss, J. (1990) Genetic Regulation of Glycogen Synthesis in Escherichia coli: In vivo Effects of the Catabolite Repression and Stringent Response Systems in glg Gene Expression. Current Microbiol. 21, 131-137.

157. Monroe, J. and Preiss, J. (1990) Purification of a b-amylase that accumulates in Arabidopsis thaliana mutants defective in starch metabolism. Plant Physiol. 94, 1033- 1039.

158. Preiss, J., Ball, K. Hutney, J. Smith-White, B., Li, L. and T.W. Okita. (1991) Regulatory Mechanisms involved in the biosynthesis of starch. Pure and Applied Chem. 63 535-544.

159. Anderson, J.M., Larsen, R., Laudencia, D., Kim, W.T., Morrow, Okita,T.W. and Preiss, J. (1991). Molecular characterization of the gene encoding a rice endosperm-specific ADPglucose Pyrophosphorylase subunit and its developmental pattern of transcription. Gene 97, 199-205.

160. Caspar, T., Lin, T.P., Kakefuda, G., Benbow, L., Preiss, J. and Somerville, C. (1991) Mutants of Arabidopsis deficient in starch degradation Plant Physiol. 95, 1181-1188.

161. Hill, M.A., Kaufmann, K., Otero, J. and Preiss, J. (1991) Biosynthesis of Bacterial Glycogen: Mutagenesis of a catalytic site residue of ADPglucose pyrophosphorylase from Escherichia coli. J. Biol. Chem. 266, 12455-12460.

162. Preiss, J., Ball, K., Smith-White, B., Iglesias, A., Kakefuda, G. and Li, L. (1991) Starch biosynthesis and its Regulation. Biochem. Soc. Trans. 19, 539-547.

163. Iglesias, A.A., Kakefuda, G. and Preiss, J. (1991) Regulatory and Structural Properties of the cyanobacterial ADPglucose Pyrophosphorylases. Plant Physiol. 97, 1187-1195.

164. Nakata, P.A., Greene, T.W., Anderson, J.M., Smith-White, B.J., Okita, T.W. and Preiss, J. (1991) Comparison of the primary sequence of the two potato tuber ADPglucose pyrophosphorylase subunits. Plant Mol. Biol. 17, 1089-1093.

165. Monroe, J.D., Salminen, M.D. and Preiss, J. (1991) Nucleotide sequence of a cDNA clone encoding a b-amylase from Arabidopsis thaliana . Plant physiol. 97, 1599-1601

166. Li, L. and Preiss J. (1992) Characterization of ADPglucose pyrophosphorylase from a starch deficient mutant of Arabidopsis thaliana . Carbohydr. Res. 227: 227-239.

167. Kakefuda, G., Charng, Y.-Y., Iglesias,A.A., McIntosh, L. and Preiss,J. (1992) Molecular cloning and sequencing of ADP-glucose pyrophosphorylase from Synechocystis PCC6803. Plant Physiol. 99: 344-347.

168. Smith-White, B.J. and Preiss, J. (1992) Comparison of Proteins of ADP-Glucose Pyrophosphorylase from diverse sources. J. Mol. Evolution, 34: 449-464.

169. Ghosh, P., Meyer, C., Remy, E., Peterson, D. and Preiss, J. (1992) Biosynthesis of Bacterial Glycogen: Cloning, Expression and Nucleotide Sequence of glg C Gene from an Allosteric Mutant of Escherichia coli B. Arch. Biochem. Biophys. 296: 122-128.

170. Iglesias, A.A., Kakefuda, G. and Preiss, J. (1992) Involvement of Arginine Residues in the Allosteric Activation and Inhibition of Synochecystis PCC 6803 ADPglucose Pyrophosphorylase. J. Protein Chem. 11, 119-128.

171. Ball, K.L. and Preiss, J. (1992) Evidence for an arginine residue at the allosteric sites of spinach leaf ADPglucose pyrophosphorylase. J. Protein Chem. 11, 231-237.

172. Meyer, C.R., Ghosh, P., Remy, E. and Preiss, J. (1992) Cloning, Expression and Nucleotide Sequence of a Mutant glg C Gene from Escherichia coli B; Substitution of a Proline to Serine at Position 295 results in altered Allosteric Properties of ADPGlc Synthetase. J. Bacteriol.,174: 4509-4512.

173. Charng, Y.-Y., Kakefuda, G., Iglesisas, A.A., Buikema, W.J. and Preiss, J. (1992) Molecular cloning and Expression of the Gene encoding ADP-Glucose Pyrophosphorylase from Cyanobacterium Anabaena sp. Strain PCC 7120. Plant Mol. Biol. 20: 37-47.

174. Stark, D.M.,Timmerman, K.P., Barry, G.F., Preiss, J. and Kishore, G.M. (1992) Role of ADPglucose Pyrophosphorylase in regulating starch levels in plant tissues.Science 258: 287-292.

175. García-González, M., Sivak, M.N., Guerrero, M.G., Preiss, J. and Lara, C. (1992) Depression of carbon flow to the glycogen pool induced by nitrogen assimilation in intact cells of Anacystis nidulans . Physiol. Plant. 86: 360-364.

176. Iglesias, A.A. and Preiss, J. (1992) Bacterial Glycogen and Plant Starch Synthesis. Biochem. Education. 20: 196-203.

177. Iglesias, A.A., Barry, G.F., Meyer, C., Bloksberg, L., Nakata, P.A., Greene, T., Laughlin, M.J., Okita, T.W., Kishore, G.M. and Preiss, J. (1993) Expression of the potato tuber ADP-glucose pyrophosphorylase in Escherichia coli. J. Biol. Chem. 268: 1081-1086.

178. Kleczkowski, L.A., Villand, P., Lüthi, E., Olsen O.-A. and Preiss, J. (1993) Insensitivity of barley endosperm ADP-glucose pyrophosphorylase to the 3-phosphoglycerate and orthophosphate regulation. Plant Physiol. 101: 179-186.

179. Takeda, Y., Guan, H.P. and Preiss, J. (1993) Branching of Amylose by the branching isoenzymes of maize endosperm. Carbohydr. Res. 240: 253-263.

180. Takeda, Y. and Preiss, J. (1993) Structures of B90 (Sugary ) and W64A (normal) maize starches. Carbohydr. Res. 240: 265-275.

181. Kleczkowski, L.A., Villand, P., Lüthi, E., Preiss, J. and Olsen O.-A. (1993) Kinetic mechanism and regulation of ADP-glucose pyrophosphorylase from barley (Hordeum vulgare) leaves. J. Biol. Chem. 268: 6228-6233.

182. Meyer, C.R., Ghosh, P., Nadler, S. and Preiss, J. (1993) Cloning, Expression and Sequence of an allosteric mutant ADPglucose pyrophosphorylase from E. coli B. Arch. Biochem. Biophys. 302: 64-71

183. Preiss, J. (1993) Biosynthesis of Starch. ADPglucose pyrophosphorylase, the regulatory enzyme of starch: structure-function relationships Denpun Kagagku 40: 117-131.

184. Guan, H.P. and Preiss, J. (1993) Differentiation of the properties of the branching isozymes from maize. Plant Physiol. 102: 1269-1273.

185. Iglesias, A.A., Charng, Y.-y. and Preiss, J. (1993) On the interaction of pyridoxal-5'- phosphate with cyanobacterial ADP-glucose pyrophosphorylase. An. Asoc. Quim. Arg. 81: 213-223.

186. Ardila, F., Sivak, M.N. and Preiss, J. (1993) Chemical modification of glycogen synthase from Escherichia coli B. using the substrate analogue 8-azido ADPglucose, a photoaffinity labeling agent. An. Asoc. Quim. Arg. 81: 301-309.

187. Sivak, M.N., Wagner, M. and Preiss, J. (1993) Biochemical Evidence for the role of theWaxy Protein from pea (Pisum sativum L.) as a granule-bound starch synthase. Plant Physiol. 103: 1355-1359.

188. Russell, D.A. DeBoer, D.L., Stark, D.M., Preiss, J. and Fromm, M. (1993) Plastid targeting of E.coli b-glucuronidase and ADP-glucose pyrophosphorylase in maize (Zea mays L.) cells. Plant Cell Rpts. 13: 24-27.

189. Iglesias, A.A., Charng, Y.-y., Ball, S. and Preiss, J. (1994) Characterization of the Kinetic, Regulatory and Structural properties of the ADP-glucose Pyrophosphorylase from Chlamydomonas reinhardtii . Plant Physiol. 104: 1287-1294.

190. Guan, H.P., Baba, T. and Preiss, J. (1994) Expression of Branching Enzyme I of Maize Endosperm in Escherichia coli. Plant Physiol. 104: 1449-1453.

191. Guan, H.P., Baba, T. and Preiss, J. (1994) Expression of Branching Enzyme II of Maize Endosperm in Escherichia coli. Cellular & Molec. Biol. 40: 981-987.

192. Charng, Y.-y., Iglesias, A.A. and Preiss, J. (1994) Structure-Function Relationships of cyanobacterial ADP-glucose pyrophosphorylase: site-directed mutagenesis and chemical modification of the activator-binding sites of ADP-glucose pyrophosphorylase from Anabaena PCC 7120. J. Biol. Chem. 269: 24107-24113.

193. Ball, K.L. and Preiss, J. (1994) Allosteric sites of the large subunit of the spinach leaf adenosine diphosphate glucose pyrophosphorylase. J. Biol. Chem. 269: 24706-24711.

194. Alonso, M.D., Lomako, J., Lomako, W.M., Whelan, W.J. and Preiss, J. (1994) Properties of carbohydrate-free recombinant glycogenin expressed in an Escherichia coli mutant lacking UDP-glucose pyrophosphorylase activity. FEBS Lett. 352: 222-226.

195. Guan, H.P., Kuriki, T., Sivak, M.N. and Preiss, J. (1995) Maize branching enzyme catalyzes the synthesis of glycogen-like polysaccharide in glgB deficient Escherichia coli. Proc. Nat'l. Acad. Sci. USA. 92: 964-967.

196. Roberts, M.W., Preiss, J. and Okita, T.W. (1995) A capillary zone electrophoresis assay for the nucleoside transfer enzyme Adenosine diphosphate-glucose pyrophosphorylase. Anal. Biochem. 225: 121-126.

197. Charng, Y.-y., Sheng, J. and Preiss, J. (1995) Mutagenesis of an amino acid residue in the activator-binding site of ADP-glucose pyrophosphorylase causes alteration in activator specificity. Arch. Biochem. Biophys.318: 476-480.

198. M. Giroux, B. Smith-White V. Gilmore, L.C. Hannah and J. Preiss (1995) The large subunit of the embryo isoform of ADPlucose pyrophosphorylase from Zea mays. Plant Physiol. 108: 1333-1334.

199. Sivak, M.N. and Preiss, J. (1995) Progress in the Genetic manipulation of crops aimed at changing starch structure and increasing starch accumulation. J. Environment. Degradation, 3: 145-152.

200. Ballicora, M.A., Laughlin, M.J., Fu, Y., Okita, T.W., Barry, G.F. and Preiss, J. (1995) ADPglucose from potato tuber. Significance of the N-terminal of the small subunit for catalytic properties and heat stability. Plant Physiol. 109: 245-251.

201. Rahman, S., Kosarhashemi, B., Samuel, M.S., Hill, A., Abbott, D.C., Skerritt, J. H., Preiss, J., Appels, R. and Morell, M. (1995) The major proteins of wheat endosperm starch granules. Austral. J. Plant Physiol. 22: 793-805.

202. Greene, T.W. Chantler, S.E., Kahn, M.L., Barry, G.F., Preiss, J. and Okita, T.W. (1995) Mutagenesis of the potato ADPglucose pyrophosphorylase and characterization of an allosteric mutant defective in 3-phosphoglycerate activation. Proc. Natl. Acad. Sci. 93:1509-1513.

203. Sheng, J., Charng, Y.-y. and Preiss, J. (1996) Site-directed mutagenesis of Lysine382, the activator binding site, of ADP-glucose pyrophosphorylase from Anabaena PCC 7120. Biochem. 35: 3115-3121.

204. Cao, H. and Preiss, J. (1996) Evidence for essential arginine residues at the active sites of maize branching enzymes. J. Prot. Chem.15: 291-304.

205. Kuriki, T., Guan, H., Sivak, M. and Preiss, J. (1996) Analysis of the active center of branching enzyme II from maize endosperm. J. Prot. Chem. 15: 305-313.

206. Van den Koornhuyse, N., Libessart, N., Delrue, B., Zabawinski, C., Decq, A., Iglesias, A., Preiss, J. and Ball, S. (1996) Control of starch composition and structure through substrate supply in the monocellular Alga Chlamydomonas reinhardtii. J. Biol. Chem. 271:16281-16287.

207. Ball, S. Guan, H.-P., James, M., Myers, A., Keeling, P., Mouille, G., Buléon, Colonna and Preiss, J. (1996) From Glycogen to Amylopectin: A model for the biogenesis of the plant starch granule. Cell 86: 349-352.

208. Preiss,J. (1996) Starch Biosynthesis: Specific functions for the starch biosynthetic enzymes. Carbohydrates in Europe 15: 11-14.

209. Guan, H. Li, P., Imparl-Radosevich, J., Preiss, J. and Keeling, P. (1997) Comparing the properties of Escherichia coli branching enzyme and maize branching enzyme. Arch. Biochem. Biophys. Arch. Biochem. Biophys. 342: 92-98.

210. Sheng, J. and Preiss, J. (1997) Arginine294 is essential for the inhibition of Anabaena PCC 7120 ADP-glucose pyrophosphorylase by phosphate. Biochem. 36: 13077-13084.

211. Kuriki, T., Stewart, D.C. and Preiss, J. (1997) Construction of chimeric enzymes out of maize endosperm branching enzymes I and II: activity and properties. J. Biol. Chem. 272: 28999-29004.

212. Kakefuda G. and Preiss, J. (1997) Partial purification and characterization of a diurnally fluctuating novel endoamylase from Arabidopsis thaliana leaves. Plant Physiol. & Biochem. 35: 907-913.

213. Hill, M.A. and Preiss, J. (1998) Functional Analysis of Conserved Histidines in ADP Glucose Pyrophosphorylase From Escherichia coli . Biochem. Biophys. Res. Commun. 244: 573-577.

214. Meyer, C.R.,Yirsa, J., Gott, B. and Preiss, J. (1998) A kinetic study of site-directed mutants of Escherichia coli ADP-glucose pyrophosphorylase: the role of residue 295 in allosteric regulation. Arch. Biochem. Biophys. 352: 247-254.

215. Meyer, C.R., Bork, J.A., Nadler, S., Yirsa, J. and Preiss, J. (1998) Site-directed mutagenesis of a regulatory site of Escherichia coli ADP-glucose pyrophosphorylase: the role of residue 336 in allosteric behavior. Arch. Biochem. Biophys. 353: 152-159.

216. Binderup K. and Preiss, J. (1998) Glutamine-459 is Important for Escherichia coli Branching Enzyme Activity. Biochemistry 37: 9033-9037.

217. Fu, Y., Ballicora, M.A. and Preiss, J. (1998) Mutagenesis of the Glucose-1-phosphate Binding Site of Potato Tuber ADP-Glucose Pyrophosphorylase. Plant Physiol. 117: 989 -996.

218. Uttaro, A.D., Ugalde, R.A., Preiss, J. and Iglesias, A.A. (1998) Cloning and Expression of the glg C gene from Agrobacterium tumefaciens. Purification and Characterization of the ADPglucose Synthetase. Arch. Biochem. Biophys. 357: 13-21.

219 Ballicora, M.A., Fu, Y., Nesbitt, N.M. and Preiss, J. (1998) ADP-Glucose Pyrophosphorylase from Potato Tuber. Site-Directed Mutagenesis Studies of the Regulatory Sites. Plant Physiol. 118: 265-274.

220. Funane, K. Libessart, N., Stewart, D., Michishita, T. and Preiss, J. (1998) Analysis of essential histidine residues of maize branching enzymes by chemical modification and site directed mutagenesis. J. Protein Chem. 17: 579-590.

221. Fu, Y., Ballicora, M.A., Leykam, J.F. and Preiss, J. (1998) Mechanism of Reductive Activation of Potato Tuber ADP-glucose Pyrophosphorylase. J.Biol. Chem. 273: 25045 -2502.

222. Wu, M.-X. and Preiss, J. (1998) The N-Terminal Region is Important for the Allosteric Activation and Inhibition of the Escherichia coli ADP-glucose Pyrophosphorylase. Arch. Biochem. Biophys. 358: 182-188.

223. Libessart, N. and Preiss, J. (1998) High-Level Expression of Branching Enzyme II from Maize Endosperm in Escherichia coli . Protein Express. Purif. 14: 1-7.

224. Libessart, N. and Preiss, J. (1998) Arginine residue 384 at the catalytic center is important for Branching Enzyme II from Maize endosperm. Arch. Biochem. Biophys 360: 135-141.

225. Ballicora, M.A., Fu, Y., Frueauf, J.B. and Preiss, J. (1999) Heat Stability of the Potato Tuber ADP-Glucose Pyrophosphorylase. Role of Cys Residue 12 in the Small Subunit. Biochem. Biophys. Res. Commun. 257: 782-786.

226. Ballicora, M.A., Freuauf, J.B., Fu, Y., Schürmann, P. and Preiss, J. (2000) Activation of the potato tuber ADP-glucose Pyrophosphorylase by thioredoxin . J. Biol. Chem. 275: 1315 1320

227. Binderup, K., Libessart, N. And Preiss, J. (2000) Slow-binding inhibition of branching enzyme by the pseudo-oligosaccharide BAY e4609. Arch. Biochem. Biophys. I374: 73 -78.

228. Binderup, K., Watanabe, L., Polikarpov, I., Preiss, J. and Arni, R.K. (2000) Crystallization and preliminary X-ray Diffraction analysis of the catalytic subunit of ADP-glucose pyrophosphorylase from potato tuber. Acta Crystallographica D56: 192-194.

229. Binderup, K., Mikkelsen. R. and Preiss, J. (2000) Limited Proteolysis of Branching Enzyme from Escherichia coli . Arch. Biochem. Biophys. 377: 366-371.

230. Hong, S,and Preiss, J. (2000) Localization of C-terminal domains required for the maximal activity or for the determination of substrate presence of maize branching enzymes. Arch. Biochem. Biophys. 378: 349-355.

231. Gómez-Casatí, D.F., Preiss,J. And Iglesias, A.A. (2000) Studies on the effect of temperature on the activity and stability of cyanobacterial ADP-glucose pyrophosphorylase. Arch. Biochem. Biophys. 384: 319-326.

232. Mikkelsen, R. Binderup, K. and Preiss, J. (2001) Tyrosine Residue 300 is Important for Activity and Stability of Branching Enzyme from Escherichia coli. Arch. Biochem. Biophys. 385: 372-377.

233. Zabawinski, C., Van den Koornhuyse, N., D'Hulst, C., Schlichting, R., Giersch, C., Delrue, B., Lacroix, J.-M., Preiss, J. and Ball, S. (2001) Starchless mutants of Chlamydomonas reinhardtii Lack the Small subunit of a heterotetrameric ADP-glucose Pyrophosphorylase. J. Bacteriol. 183: 1069-1077.

234. Hong, S., Mikkelsen, R. and Preiss, J. (2001) Analysis of Maize Branching Enzyme II by PCR Random Mutagenesis. Arch. Biochem. Biophys. 386: 62-68.

235. Wu, M.-X. and Preiss, J. (2001) Abridged Forms of the Recombinant Escherichia coli ADP-glucose Pyrophosphorylase : The Importance of the N-Terminal Region for Allosteric Activation and Inhibition. Arch. Biochem. Biophys. 389, 159-165.

236. Frueauf, J.B., Ballicora, A.M. And Preiss, J. (2001) Aspartate residue 142 is important for catalysis by ADPGlc pyrophosphorylase from Escherichia coli. J. Biol. Chem. 276: 46319-46325.

237. Binderup, K., Mikkelsen, R. And Preiss, J. (2001) Truncation of the Amino-Terminus of Branching Enzyme changes in Branching Pattern. Arch. Biochem. Biophys. 397: 279-285..

238. Abad, M.C., Binderup, K., Preiss, J. and Geiger, J. H. (2002) Crystallization and preliminary X-ray diffraction studies of Escherichia coli Branching Enzyme. Acta Crystallographica D series. D58 359-361..

239. Frueauf, J.B., Ballicora, A.M. And Preiss, J. (2002) Alteration of inhibitor specificity by site-directed mutagenesis of Arg294 in the ADP-glucose pyrophosphorylase from anabaena PCC 7120. Arch. Biochem. Biophys. 400: 208-214..

240. Ballicora, M.A., Sesma, J.I., Iglesias, A.A. And Preiss, J. (2002) Characterization of Chimeric ADPglucose Pyrophosphorylases of Escherichia coli and Agrobacterium tumefaciens. Importance of the C-terminal Domain on the Selectivity for Allosteric Regulators. Biochemistry, 41: 9431-9437.

241. Abad, M.C., Binderup, K., Rios-Steiner, Jorge, Preiss, J. and Geiger, J. H. (2002) The X-ray Crystallographic structure of Escherichia coli Branching Enzyme. J. Biol. Chem. 277: 42164-42170.

242. Freuauf, J.B. , Ballicora, M.A. And Preiss, J. (2003) ADPglucose Pyrophosphorylase from potato tuber. Site-Directed Mutagenesis of Homologous Aspartic Acid Residues in the Small and Large Subunits. Plant J. 33: 503-511.

243. Crevillén, P., Ballicora, M.A., Mérida, Á. Preiss, J. And Romero, J. (2003) The different large subunit isoforms of Arabidopsis thaliana ADP-glucose pyrophosphorylase confer distinct kinetic and regulatory properties to the heterotetrameric enzyme. J. Biol. Chem. 278: 28508-2515. .

244. Devillers, C.H., Piper, M.E., Ballicora, M.A. And Preiss, J. (2003) Characterization of the branching patterns of glycogen branching enzyme truncated on the N-terminus. Arch. Biochem. Biophys. 418: 34-38

245. Yep, A., Bejar, C.M., Ballicora, M.A., Dubay, J., Iglesias, A.A. And Preiss, J. (2004) An assay for the ADP-glucose Pyrophosphorylase that measures the synthesis of radioactive ADP-glucose with glycogen synthase. Analytical Biochemistry. 324: 52-59.

246. Yep, A., Ballicora, M. A. Sivak, M. N. and Preiss J. (2004) Identification and Characterization of a Critical Region in the Glycogen Synthase from Escherichia coli.J. Biol. Chem. 279: 8359-8367.

247. Yep, A., Ballicora, M. A. Sivak, M. N. and Preiss J. (2004) The active site of the Escherichia coli Glycogen Synthase is similar to the active site of retaining GT-B Glycosyltransferases. (2004) Biochem. Biophys. Res. Commun. 316: 960-966.

248. Bejar, C.M., Ballicora, M.A., , Gomez-Casati, D.F., Iglesias, A.A. And Preiss, J. (2004) The ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domains. FEBS letters, 573: 99-104.

249. Sakulsinghharoj, C., Choi, S.-B., Hwang, S.-K., Edwards, G.E., Bork, J., Meyer, C.R., Preiss, J. And Okita, T.W. (2004) Engineering starch biosynthesis for increasing rice seed weight: the role of the cytoplasmic ADP-glucose pyrophosphorylase. Plant Science 167: 1323-1333.

250. Jin, X., Ballicora, M.A., Preiss, J. and Geiger, James H.(2005) Crystal structure of potato tuber ADP-glucose pyrophosphorylase. Embo J. In Press.

251. Ballicora, Miguel A., Dubay, J.R., Devillers, C.H. And Preiss, J. (2005) Resurrecting the ancestral enzymatic role of a modulatory subunit. J. Biol. Chem. In Press.

Last updated 1/12/05