Evolution of the development of how starch is biosynthesized

Starch/Staerke

Volumn 65, Issue 1-2, 2013, Pages 8-21

  Robyt, John F ^a   Mukerjea, Rupendra ^a  

^a IOWA STATE UNIVERSITY   (United States)

Author keywords

ADPGlc; Pulse and chase; Putative primers; Starch granules; Starch synthase

Indexed keywords

ADP-GLC; PULSE AND CHASE; PUTATIVE PRIMERS; STARCH GRANULES; STARCH-SYNTHASE;

GLUCOSE; GRANULATION; PHOSPHORYLATION; SYNTHESIS (CHEMICAL);

STARCH;

SOLANUM TUBEROSUM;

EID: 84873572149     PISSN: 00389056     EISSN: 1521379X     Source Type: Journal    
DOI: 10.1002/star.201200157     Document Type: Review

References (53)

1. Hanes, C. S., The reversible formation of starch from glucose-1-posphate catalyzed by potato phosphorylase. Proc. Royal Soc. London B 1940, 129, 174-208.
2. Trevelyan, W. E., Mann, P. F. E., Harrison, J. S., The phosphorylase reaction. I. Equilibrium constant: Principles and preliminary survey. Arch. Biochem. Biophys. 1952, 39, 419-427.
3. Ewart, M. H., Siminovitch, D., Briggs, D. R., Studies of the chemistry of the living bark of the black locust in relation to its frost hardiness. VIII. Possible enzymatic processes involved in starch-sucrose interconversion. Plant Physiol. 1954, 29, 407-413.
4. Liu, T.-T., Shannon, J. C., A nonaqueous procedure for isolating starch granules with associated metabolites from maize (Zea mays L.) endosperm. Plant Physiol. 1981, 67, 525-533.
5. Green, D. E., Stumpf, P. K., Starch phosphorylase from potato. J. Biol. Chem. 1942, 142, 355-366.
6. French, D., Wild, G. M., Primer specificity of potato phosphorylase. J. Am. Chem. Soc. 1953, 75, 4490-4492.
7. Bailey, J. M., Whelan, W. J., Physical properties of starch: Relationship between iodine stain and chain length. J. Biol. Chem. 1961, 236, 969-973.
8. Swanson, M. A., Cori, C. F., Studies on the structure of polysaccharides III. Relation of structure to activation of phosphorylases. J. Biol. Chem. 1948, 172, 815-829.
9. Baba, T., Noro, M., Hiroto, M., Arai, Y., Properties of primer dependent starch synthesis catalyzed by starch synthase from potato tubers. Phytochemistry 1990, 29, 719-723.
10. De Fekete, M. A. G., Leloir, L. F., Cardini, C. E., Mechanism of starch biosynthesis. Nature 1960, 10, 918-919.
11. Recondo, E., Leloir, L. F., Adenosine diphosphate glucose and starch biosynthesis. Biochem. Biophys. Res. Commun. 1961, 6, 85-88.
12. Leloir, L. F., De Fekete, M. A. R., Cardini, C. E., Starch and oligosaccharide synthesis from uridine diphosphate glucose. J. Biol. Chem. 1961, 236, 636-641.
13. Frydman, R. B., Cardini, C. E., Studies on the biosynthesis of starch. II. Some properties of the adenosine diphosphate glucose: starch glucosyltransferase. J. Biol. Chem. 1967, 242, 312-317.
14. Mukerjea, Ru., Robyt, J. F., Starch biosynthesis: The primer nonreducing-end mechanism versus the nonprimer reducing-end two-site insertion mechanism. Carbohydr. Res. 2005, 340, 245-255.
15. Denyer, K., Clarke, B., Hylton, C., Tatge, H., Smith, A. M., The elongation of amylose and amylopectin chains in isolated starch granules. Plant J. 1996, 10, 1135-1143.
16. III-α-maltosyl- maltohexaose comprising the branch point of amylopectin. Eur. J. Biochem. 2001, 268, 4878-4884.
17. Damager, I., Olsen, C. E., Blennow, A., Denyer, K. et al., Chemical synthesis of methyl 6'-α-maltosyl-a-maltotrioside and its use for the investigation of the action of starch synthase II. Carbohydr. Res. 2003, 338, 189-197.
18. Van De Wal, M., D'Hulst, C., Vincken, J.-P., Buléon, A. et al., Amylose is synthesized in vitro by estension of and cleavage from amylopectin. J. Biol. Chem. 1998, 273, 22232-22240.
19. Ball, S. G., Van De Wal, M. H. B. J., Visser, R. G. F., Progress in understanding the biosynthesis of amylose. Trends Plant Sci. 1998, 3, 462-467.
20. Denyer, K., Waite, D., Motawia, S., Møller, B. L., Smith, A. M., Biochem. J. 1999, 340, 183-191.
21. Bray, D., Robbins, P. W., The Direction of chain growth in Salmonella anatum O-antigen biosynthesis. Biochem. Biophys. Res. Commun. 1967, 3, 334-339.
22. Robbins, P. W., Bray, D., Dankert, M., Wright, A., Direction of chain growth in polysaccharide synthesis. Science 1967, 158, 1536-1542.
23. Ward, J. B., Perkins, H. R., The direction of glycan synthesis in a bacterial peptidoglycan. Biochem. J. 1973, 135, 721-728.
24. Robyt, J. F., Kimble, B. K., Walseth, T. F., The mechanism of dextransucrase action: I. Direction of dextran biosynthesis. Arch. Biochem. Biophys. 1974, 165, 634-644.
25. Robyt, J. F., Yoon, S.-H., Mukerjea, Ru., Dextransucrase and the mechanism for dextran biosynthesis. Carbohydr. Res. 2008, 343, 1015-1022.
26. Robyt, J. F., Martin, P. J., Mechanism of synthesis of glucans by glucosyltransferases from Streptococcus mutans 6715. Carbohydr. Res. 1983, 113, 301-315.
27. Ielpi, L., Couso, R. O., Dankert, M. A., Sequential assembly and polymerization of the polyphenol-linked pentasaccharide repeating unit of the xanthan polysaccharide formed by Xanthomonas campestris. J. Bacteriol. 1993, 175, 2490-2500.
28. Han, N. S., Robyt, J. F., The mechanism of Acetobacter xylinum cellulose biosynthesis: Direction of chain elongation and the role of lipid pyrophosphate intermediates in the cell membrane. Carbohydr. Res. 1998, 313, 125-133.
29. Mukerjea, Ru., Yu, L., Robyt, J. F., Starch biosynthesis: Mechanism for the elongation of starch chains. Carbohydr. Res. 2002, 337, 1015-1022.
30. Mukerjea, Ru., Robyt, J. F., Starch biosynthesis: Further evidence against the primer nonreducing-end elongation and evidence for the reducing-end two-site insertion mechanism. Carbohydr. Res. 2005, 340, 2206-2211.
31. Mukerjea, Ru., Falconer, D. J., Yoon, S.-H., Robyt, J. F., Large-scale isolation, fractionation, and purification of soluble starch-synthesizing enzymes: Starch-synthase and branching-enzyme from potato tubers. Carbohydr. Res. 2010, 345, 1555-1563.
32. Mukerjea, Ru., Robyt, J. F., De novo biosynthesis of starch chains without a primer and the mechanism for its biosynthesis by potato starch-synthase. Carbohydr. Res. 2012, 352, 137-142.
33. Mukerjea, Ru., McIntyre, A. P., Robyt, J. F., Potent inhibition of starch-synthase by Tris-type buffers is responsible for the perpetuation of the primer myth for starch biosynthesis. Carbohydr. Res. 2012, 355, 28-34.
34. Frydman, R. B., Cardini, C. E., Soluble enzymes related to starch synthesis. Biochem. Biophys. Res. Commun. 1964, 17, 407-411.
35. Hawker, J. S., Ozbun, J. L., Preiss, J., Unprimed starch synthesis by soluble ADP-Glucose-starch glucosyltransferase from potato tubers. Phytochemistry 1972, 11, 1287-1293.
36. Pollock, C., Preiss, J., The citrate-stimulated starch synthase of starchy maize kernels: Purification and properties. Arch. Biochem. Biophys. 1980, 204, 578-588.
37. McDonald, F. D., Preiss, J., Partial purification and characterization of granule-bound starch synthase of normal maize kernels. Plant Physiol. 1983, 73, 175-178.
38. McDonald, F. D., Preiss, J., Partial purification and characterization of granule-bound starch synthase from normal and waxy maize. Plant Physiol. 1985, 78, 849-852.
39. Schiefer, S., Lee, E. Y. C., Whelan, W. J., The requirement for a primer in the in vitro synthesis of polysaccharides by sweetcorn (1, 4)-a-D-glucan synthase. Carbohydr. Res. 1978, 61, 239-252.
40. Mukerjea, Ru., Robyt, J. F., Starch biosynthesis: Sucrose as a substrate for the synthesis of a highly branched component found in 12 varieties of starches. Carbohydr. Res. 2003, 338, 1811-1822.
41. Mukerjea, Ru., Robyt, J. F., Isolation, structure, and characterization of the putative soluble amyloses from potato, wheat, and rice starches. Carbohydr. Res. 2010, 345, 449-451.
42. Pilling, E., Smith, A. M., Growth ring formation in the starch granules of potato tubers. Plant Physiol. 2003, 132, 365-371.
43. Pérez, S., Bertoft, E., The molecular structures of starch components and their contribution to the architecture of starch granules: A comprehensive review. Starch/Stä rke 2010, 62, 389-420.
44. Mukerjea, Ro., Mukerjea, Ru., Robyt, J. F., Controlled peeling of the surfaces of starch granules by gelatinization in aqueous dimethyl sulfoxide at selected temperatures. Carbohydr. Res. 2006, 341, 757-765.
45. Mukerjea, Ro., Mukerjea, Ru., Robyt, J. F., Starch biosynthesis: Experiments on how starch granules grow in vivo. Carbohydr. Res. 2009, 344, 67-73.
46. Badenhuizen, N. P., Dutton, W., 14C-labeled starch granules in potato tubers as revealed by radioautographs. Protoplasma 1956, 47, 156-163.
47. Yoshida, M., Fujii, M., Nikuni, Z., Maruo, B., Appositive growth of starch granules in beans as revealed by autoradiography. Bull. Agric. Chem. Soc. Jpn. 1958, 21, 127.
48. Mukerjea, Ro., Mukerjea, Ru., Robyt, J. F., Activities of the sucrose-starch synthase in the various layers of starch granules (Unpublished work).
49. Borovsky, D., Smith, E. E., Whelan, W. J., Temperaturedependence of the action of Q-enzyme and the nature of the substrate for Q-enzyme. FEBS Lett. 1975, 54, 201-205.
50. Borovsky, D., Smith, E. E., Whelan, W. J., On the mechanism of amylose branching by potato Q-enzyme. Eur. J. Biochem. 1976, 62, 307-312.
51. Borovsky, D., Smith, E. E., Whelan, W. J., French, D., Kikumoto, S., The mechanism of Q-enzyme action and its influence on the structure of amylopectin. Arch. Biochem. Biophys. 1979, 198, 627-631.
52. French, D., Fine structure of starch and its relationship to the organization of starch granules. J. Jpn. Soc. Starch Sci. 1972, 19, 8-25.
53. Jane, J.-L., Kasemsuwan, T., Leas, S., Zobel, H., Robyt, J. F., Anthology of starch granule morphology by scanning electron microscopy. Starch/Stä rke 1994, 46, 121-129.