Starch degradation

Annual Review of Plant Biology

Volumn 56, Issue , 2005, Pages 73-96

  Smith, Alison M ^a   Zeeman, Samuel C ^b   Smith, Steven M ^c,d  

^a JOHN INNES CENTRE   (United Kingdom)

^b UNIVERSITY OF BERN   (Switzerland)

^c UNIVERSITY OF EDINBURGH   (United Kingdom)

^d UNIVERSITY OF WESTERN AUSTRALIA   (Australia)

Author keywords

Amylase; Arabidopsis; Cereal endosperm; Chloroplast; Maltose

Indexed keywords

BETA AMYLASE; STARCH;

ARABIDOPSIS; BIOREMEDIATION; ENZYMOLOGY; METABOLISM; PLANT LEAF; REVIEW; SPECIES DIFFERENCE;

ARABIDOPSIS; BETA-AMYLASE; BIODEGRADATION, ENVIRONMENTAL; PLANT LEAVES; SPECIES SPECIFICITY; STARCH;

ARABIDOPSIS;

EID: 20444405023     PISSN: 15435008     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.arplant.56.032604.144257     Document Type: Review

References (128)

1. ap Rees T, Wright BW, Fuller WA. 1977. Measurements of starch breakdown as estimates of glycolysis during thermogenesis by the spadix of Arum maculatum. Planta 134:53-56
2. Balmer Y, Koller A, del Val G, Manieri W, Schürmann P, Buchanan BB. 2003. Proteomics gives insights into the regulatory function of chloroplast thioredoxins. Proc. Natl. Acad. Sci. USA 100:370-75
3. Banks W, Muir DD. 1980. Structure and chemistry of the starch granule. In The Biochemistry of Plants, ed. J Preiss, 3:321-69. New York: Academic
4. Beck E, Ziegler P. 1989. Biosynthesis and degradation of starch in higher plants. Annu. Rev. Plant Physiol. Plant Mol. Biol. 40:95-117
5. Blennow A, Engelsen SB, Munck L, Møller BL. 2000. Starch molecular structure and phosphorylation investigated by a combined chromatographic and chemometric approach. Carbohydr. Polymers 41:163-74
6. Blennow A, Engelsen SB, Nielsen TH, Baunsgaard L, Mikkelsen R. 2002. Starch phosphorylation: a new front line in starch research. Trends Plant Sci. 7:445-50
7. Boos W, Schuman H. 1998. Maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulation. Microbiol. Mol. Biol. Rev. 62:204-29
8. Briggs DE. 1973. Hormones and carbohydrate metabolism in germinating cereal grains. In Biosynthesis and its Control in Plants, ed. BV Milborrow, pp. 219-77. London: Academic
9. Bulpin PV, ap Rees T. 1978. Starch breakdown in the spadix of Arum maculatum. Phytochem. 17:391-96
10. Burton R, Jenner H, Carrangis L, Fahy B, Fincher G, et al. 2002. Starch granule initiation and growth are altered in barley mutants that lack isoamylase activity. Plant J. 31:97-112
11. Burton RA, Zhang XQ, Hrmova M, Fincher GB. 1999. A single limit dextrinase gene is expressed both in the developing endosperm and in germinated grains of barley. Plant Physiol. 119:859-71
12. Bustos R, Fahy B, Hylton CM, Seale R, Nebane NM, et al. 2004. Starch granule initiation is controlled by a heteromultimeric isoamylase in potato tubers. Proc. Natl. Acad. Sci. USA 101:2215-20
13. Caspar T, Lin TP, Kakefuda G, Benbow L, Preiss J, Somerville C. 1991. Mutants of Arabidopsis with altered regulation of starch degradation. Plant Physiol. 95:1181-88
14. Chia T, Thorneycroft D, Chapple A, Messerli G, Chen J, et al. 2004. A cytosolic glucosyltransferase is required for conversion of starch to sucrose in Arabidopsis leaves at night. Plant J. 37:853-63
15. Critchley JH, Zeeman SC, Takaha T, Smith AM, Smith SM. 2001. A critical role for disproportionating enzyme in starch breakdown is revealed by a knock-out mutant in Arabidopsis. Plant J. 26:89-100
16. Dale JE. 1969. Gibberellins and early growth in seedlings of Phaseolus vulgaris. Planta 89:155-64
17. Daussant J, Zbaszyniak B, Sadowski J, Wiatroszak I. 1981. Cereal β-amylase: immunochemical study on two enzyme-deficient inbred lines of rye. Planta 151:176-79
18. Davies HV, Ross HA. 1984. The pattern of starch and protein degradation in tubers. Potato Res. 27:373-81
19. Davies HV, Ross HA. 1986. Hydrolytic and phosphorolytic enzyme activity and reserve mobilisation in sprouting tubers of potato (Solanum tuberosum L.). J. Plant Physiol. 126:379-86
20. Davies HV. 1990. Carbohydrate metabolism during sprouting. Amer. Potato J. 67:815-27
21. Deiting U, Zrenner R, Stitt M. 1998. Similar temperature requirement for sugar accumulation and for the induction of new forms of sucrose phosphate synthase and amylase in cold-stored potato tubers. Plant Cell Env. 21:127-38
22. Dinges JR, Colleoni C, James MG, Myers A. 2003. Mutational analysis of the pullulanase-type debranching enzyme of maize indicates multiple functions in starch metabolism. Plant Cell 15:666-80
23. Dronzek BL, Hwang P, Bushuk W. 1972. Scanning electron microscopy of starch from sprouted wheat. Cereal Chem. 49:232-39
24. Dunn G. 1974. A model for starch breakdown in higher plants. Phytochem. 13:1341-46
25. Duwenig E, Steup M, Willmitzer L, Kossmann J. 1997. Antisense inhibition of cytosolic phosphorylase in potato plants (Solanum tuberosum L.) affects tuber sprouting and flower formation with only little impact on carbohydrate metabolism. Plant J. 12:323-33
26. Echeverria E, Boyer CD. 1986. Localization of starch biosynthetic and degradative enzymes in maize leaves. Amer. J. Bot. 73:167-71
27. Fannon JE, Hauber RJ, BeMiller JN. 1992. Surface pores of starch granules. Cereal Chem. 69:284-88
28. Fettke J, Eckermann N, Poeste S, Pauly M, Steup M. 2004. The glycan substrate of the cytosolic (Pho 2) phosphorylase isozyme from Pisum sativum L.: identification, linkage analysis, and subcellular localisation. Plant J. 39:933-46
29. Fincher GB. 1989. Molecular and cellular biology associated with endosperm mobilization in germinating cereal grains. Annu. Rev. Plant Physiol. Plant Mol. Biol. 40:305-46
30. Flügge UI. 1999. Phosphate translocators in plastids. Annu. Rev. Plant Physiol. Plant Mol. Biol. 50:27-54
31. Fondy BR, Geiger DR, Servaites JC. 1989. Photosynthesis, carbohydrate metabolism, and export in Beta vulgaris L. and Phaseolus vulgaris L. during square and sinusoidal light regimes. Plant Physiol. 89:396-402
32. Fuwa H, Nakajima M, Hamada A, Glover DV. 1977. Comparative susceptibility to amylases of starches from different plant species and several single endosperm mutants and their double-mutant combinations with opaque-2 inbred Oh43 maize. Cereal Chem. 54:230-37
33. Gallant D, Mercier C, Guilbot A. 1972. Electron microscopy of starch granules modified by bacterial α-amylase. Cereal Chem. 49:354-65
34. Gibon Y, Bläsing OE, Palacios-Rojas N, Pankovic D, Hendriks JHM, et al. 2004. Adjustment of diurnal starch turnover to short days: depletion of sugar during the night leads to a temporary inhibition of carbohydrate utilization, accumulation of sugars and post-translational activation of ADP-glucose pyrophosphorylase in the following light period. Plant J. 39:847-62
35. Hammond JBW, Preiss J. 1983. Spinach leaf intra and extra chloroplast phosphorylase activities during growth. Plant Physiol. 73:709-12
36. Harmer SL, Hogenesch JB, Straume M, Chang HS, Han B, et al. 2000. Orchestrated transcription of key pathways in Arabidopsis by the circadian clock. Science 290:2110-13
37. Harris N. 1976. Starch grain breakdown in cotyledon cells of germinating mung bean seeds. Planta 129:271-72
38. Häusler RE, Schlieben NH, Schulz B, Flügge UI. 1998. Compensation of decreased triose phosphate/phosphate translocator activity by accelerated starch turnover and glucose transport in transgenic tobacco. Planta 204:366-76
39. Heineke D, Kruse A, Flügge UI, Frommer WB, Riesmeier JW, et al. 1994. Effect of antisense repression of the chloroplast triose-phosphate translocator on photosynthetic metabolism in transgenic potato plants. Planta 193:174-80
40. Hendricks JHM, Kolbe A, Gibon Y, Stitt M, Geigenberger P. 2003. ADP-glucose pyrophosphorylase is activated by post-translational redox-modification on response to light and sugars in leaves of Arabidopsis and other plant species. Plant Physiol. 133:838-49
41. Herold A, Leegood RC, McNeil PH, Robinson SP. 1981. Accumulation of maltose during photosynthesis in spinach protoplasts treated with mannose. Plant Physiol. 67:85-88
42. Huber KC, BeMiller JN. 1997. Visualization of channels and cavities of corn and sorghum starch granules. Cereal Chem. 74:537-41
43. Huber KC, BeMiller JN. 2000. Channels of maize and sorghum starch granules. Carbohydr. Polymers 41:269-76
44. Humphreys TE. 1975. Maltose uptake in the Zea mays scutellum. Phytochem. 14:333-40
45. Hussain H, Mant A, Seale R, Zeeman S, Hinchliffe E, et al. 2003. Three isoforms of isoamylase contribute different catalytic properties for the debranching of potato glucans. Plant Cell 15:133-49
46. Isherwood FA. 1973. Starch-sucrose interconversion in Solanum tuberosum. Phytochem. 12:2579-91
47. Isherwood FA. 1976. Mechanism of starch-sucrose interconversion in Solanum tuberosum. Phytochem. 15:33-41
48. James MG, Robertson DS, Myers AM. 1995. Characterization of the maize gene sugary1, a determinant of starch composition of kernels. Plant Cell 7:417-29
49. Juliano BO, Varner JE. 1969. Enzymic degradation of starch granules in the cotyledons of germinating peas. Plant Physiol. 44:886-92
50. Kakefuda G, Preiss J. 1997. Partial purification and characterization of a diurnally fluctuating novel endoamylase from Arabidopsis thaliana leaves. Plant Physiol. 35:907-13
51. Kaplan F, Guy CL. 2004. β-amylase induction and the protective role of maltose during temperature shock. Plant Physiol. 135:1674-84
52. Kruger NJ, ap Rees T. 1993. Maltose metabolism by pea chloroplasts. Planta 158:271-73
53. Kubo A, Fujita N, Harada K, Matsuda T, Satoh H, Nakamura Y. 1999. The starch-debranching enzymes isoamylase and pullulanase are both involved in amylopectin biosynthesis in rice endosperm. Plant Physiol. 121:399-409
54. Lao NT, Schoneveld O, Mould RM, Hibberd JM, Gray JC, Kavanagh TA. 1999. An Arabidopsis gene encoding a chloroplast-targeted β-amylase. Plant J. 20:519-27
55. Leach HW, Schoch TJ. 1961. Structure of the starch granule. II. Action of various amylases on granular starch. Cereal Chem. 38:34-46
56. Li B, Servaites JC, Geiger DR. 1992. Characterization and subcellular localization of debranching enzyme and endoamylase from leaves of sugar beet. Plant Physiol. 98:1277-84
57. Lin TP, Caspar T, Somerville C, Preiss J. 1988. A starch deficient mutant of Arabidopsis thaliana with low ADP glucose pyrophosphorylase activity lacks one of the two subunits of the enzyme. Plant Physiol. 88:1175-81
58. Lin TP, Spilatro SR, Preiss J. 1988. Subcellular localization and characterization of amylases in Arabidopsis leaf. Plant Physiol. 86:251-59
59. Lizotte PA, Henson CA, Duke SH. 1990. Purification and characterization of pea epicotyl β-amylase. Plant Physiol. 92:615-21
60. Lloyd JR, Blennow A, Burhenne K, Kossmann J. 2004. Repression of a novel isoform of disproportionating enzyme (stDPE2) in potato leads to inhibition of starch degradation in leaves but not tubers stored at low temperature. Plant Physiol. 134:1347-54
61. Lorberth R, Ritte G, Willmitzer L, Kossmann J. 1998. Inhibition of a starch-granule-bound protein leads to modified starch and repression of cold-induced sweetening. Nature Biotech. 16:473-77
62. Lu Y, Sharkey T. 2004. The role of amylomaltase in maltose metabolism in the cytosol of photosynthetic cells. Planta 218:466-73
63. MacGregor EA. 2004. The proteinaceous inhibitor of limit dextrinase in barley and malt. Biochim. Biophys. Acta 1696:165-70
64. Matheson NK, Richardson RH. 1976. Starch phosphorylase enzymes in developing and germinating pea seeds. Phytochem. 15:887-92
65. Matheson NK, Wheatley JM. 1962. Starch changes in developing and senescing tobacco leaves. Austr. J. Biol. Sci. 15:445-58
66. Matheson NK, Wheatley JM. 1963. Diurnal-nocturnal changes in the starch of tobacco leaves. Austr. J. Biol. Sci. 16:70-76
67. Mikkelsen R, Baunsgaard L, Blennow A. 2004. Functional characterisation of α-glucan, water dikinase, the starch phosphorylating enzyme. Biochem. J. 377:525-32
68. Nakamura Y. 1996. Some properties of starch debranching enzymes and their possible role in amylopectin biosynthesis. Plant Sci. 121:1-18
69. Nielsen TH, Deiting U, Stitt M. 1997. A β-amylase in potato tubers is induced by storage at low temperature. Plant Physiol. 113:503-10
70. Nielsen TH, Wischmann B, Enevoldsen K, Møller BL. 1994. Starch phosphorylation in potato tubers proceeds concurrently with de novo biosynthesis of starch. Plant Physiol. 105:111-17
71. Niittylä T, Messerli G, Trevisan M, Chen J, Smith AM, Zeeman SC. 2004. A previously unknown maltose transporter essential for starch degradation in leaves. Science 303:87-89
72. Ohad I, Friedberg I, Ne'eman Z, Schramm M. 1971. Biogenesis and degradation of starch. I. The fate of the amyloplast membranes during maturation and storage of potato tubers. Plant Physiol. 47:465-77
73. Okita TW, Greenberg E, Kuhn DN, Preiss J. 1979. Subcellular localization of the starch degradative and biosynthetic enzymes of spinach leaves. Plant Physiol. 64:187-92
74. Okita TW, Preiss J. 1980. Starch degradation in spinach leaves. Isolation and characterization of the amylases and R-enzyme of spinach leaves. Plant Physiol. 66:870-76
75. Peavey DG, Steup M, Gibbs M. 1977. Characterization of starch breakdown in the intact spinach chloroplast. Plant Physiol. 60:305-08
76. Ritchie S, Swanson SJ, Gilroy S. 2000. Physiology of the aleurone layer and starchy endosperm during grain development and early seedling growth: new insights from cell and molecular biology. Seed Sci. Res. 10:193-212
77. Ritte G, Eckermann N, Häbel S, Lorberth R, Steup M. 2002. Compartmentation of the starch-related R1 protein in higher plants. Starch 52:179-85
78. Ritte G, Lloyd JR, Eckermann N, Rottmann A, Kossmann J, Steup M. 2002. The starch-related R1 protein is an α-glucan, water dikinase. Proc. Natl. Acad. Sci. USA 99:7166-71
79. Ritte G, Lorberth R, Steup M. 2002. Reversible binding of the starch-related R1 protein to the surface of transitory starch granules. Plant J. 21:387-91
80. Ritte G, Scharf A, Eckermann N, Häbel S, Steup M. 2004. Phosphorylation of transitory starch is increased during degradation. Plant Physiol. 135:2068-77
81. Rost S, Frank C, Beck E. 1996. The chloroplast envelope is permeable for maltose, but not for maltodextrins. Biochim. Biophys. Acta 1291:221-27
82. Scheidig A, Frölich A, Schulze S, Lloyd JR, Kossmann J. 2002. Down-regulation of a chloroplast-targeted β-amylase leads to a starch-excess phenotype in leaves. Plant J. 30:581-91
83. Schleucher J, Vanderveer PJ, Sharkey TD. 1998. Export of carbon from chloroplasts at night. Plant Physiol. 118:1439-45
84. Schroder SW, MacGregor AW. 1998. Synthesis of limit dextrinase in germinated barley kernels and aleurone tissues. J. Am. Soc. Brew. Chem. 56:32-37
85. Schulze W, Stitt M, Schulze ED, Neuhaus HE, Fichtner K. 1991. A quantification of the significance of assimilatory starch for growth of Arabidopsis thaliana L. Heynh. Plant Physiol. 95:890-95
86. Servaites JC, Geiger DR. 2002. Kinetic characteristics of chloroplast glucose transport. J. Exp. Bot. 53:1581-91
87. Sharkey TD, Savitch LV, Vanderveer PJ, Micallef BJ. 1992. Carbon partitioning in a Flaveria linearis mutant with reduced cytosolic fructose bisphosphatase. Plant Physiol. 100:210-15
88. Sissons MJ, MacGregor AW. 1994. Hydrolysis of barley starch granules by alpha-glucosidases from malt. J. Cereal Sci. 19:161-69
89. Smith AM, Martin C. 1993. Starch biosynthesis and the potential for its manipulation. In Biosynthesis and Manipulation of Plant Products, ed. D Grierson, pp. 1-54. London: Blackie
90. Smith SM, Fulton DC, Chia T, Thorneycroft D, Chapple A, et al. 2004. Diurnal changes in the transcriptome encoding enzymes of starch metabolism provide evidence for both transcriptional and post-transcriptional regulation. Plant Physiol. 135:2687-99
91. Sonnewald U, Basner A, Greve B, Steup M. 1995. Asecond L-type isozyme of potato glucan phosphorylase: cloning, antisense inhibition and expression analysis. Plant Mol. Biol. 27:567-76
92. Sowokinos JR, Lulai EC, Knoper JA. 1985. Translucent tissue defects in Solanum tuberosum L. I. Alterations in amyloplast membrane integrity, enzyme activities, sugars, and starch content. Plant Physiol. 78:489-94
93. Stahl Y, Coates S, Bryce JH, Morris PC. 2004. Antisense downregulation of the barley limit dextrinase inhibitor modulates starch granule size distribution, starch composition and amylopectin structure. Plant J. 36:616-28
94. Stanley D, Fitzgerald AM, Farnden KJF, MacRae EA. 2002. Characterisation of putative α-amylases from apple (Malus domestica) and Arabidopsis thaliana. Biologia 57:137-48
95. Steup M, Robenek H, Melkonian M. 1983. In-vitro degradation of starch granules isolated from spinach chloroplasts. Planta 158:428-36
96. Stitt M, ap Rees T. 1980. Carbohydrate breakdown by the chloroplasts of Pisum sativum. Biochim. Biophys. Acta 627:131-43
97. Stitt M, Bulpin PV, ap Rees T. 1978. Pathway of starch breakdown in photosynthetic tissues of Pisum sativum. Biochim. Biophys. Acta 544:200-14
98. Stitt M, Heldt HW. 1981. Simultaneous synthesis and degradation of starch in spinach chloroplasts in the light. Biochim. Biophys. Acta 638:1-11
99. Stitt M, Heldt HW. 1981. Physiological rates of starch breakdown in isolated intact spinach chloroplasts. Plant Physiol. 68:755-61
100. Stitt M, Wirtz W, Gerhardt R, Heldt HW, Spencer C, et al. 1985. A comparative study of metabolite levels in plant leaf material in the dark. Planta 166:354-64
101. Sun Z, Duke SH, Henson CA. 1995. The role of pea chloroplast α-glucosidase in transitory starch degradation. Plant Physiol. 108:211-17
102. Sun Z, Henson CA. 1990. Degradation of native starch granules by barley α-glucosidases. Plant Physiol 94:320-27
103. Sun Z, Henson CA. 1991. A quantitative assessment of the importance of barley seed α-amylase, β-amylase, debranching enzyme, and α-glucosidase in starch degradation. Arch. Biochem. Biophys. 234:298-305
104. Takaha T, Critchley J, Okada S, Smith SM. 1998. Normal starch content and composition in tubers of antisense potato plants lacking D-enzyme (4-α-glucanotransferase). Planta 205:445-51
105. Tarrágo JF, Nicolás G. 1976. Starch degradation in the cotyledons of germinating lentils. Plant Physiol. 58:618-21
106. Thimm O, Bläsing OE, Gibon Y, Nagel A, Meyer S, et al. 2004. Map-man: a user-driven tool to display genomics datasets onto diagrams of metabolic pathways and other biological processes. Plant J. 37:914-99
107. Tsugeki R, Fedoroff NV. 1999. Genetic ablation of root cap cells in Arabidopsis. Proc. Natl. Acad. Sci. USA 96:12941-46
108. van Berkel J, Conrads-Strauch J, Steup M. 1991. Glucan-phosphorylase forms in cotyledons of Pisum sativum L.: localization, developmental change, in-vitro translation, and processing. Planta 185:432-39
109. Weber A, Servaites JC, Geiger DR, Kofler H, Hille D, et al. 2000. Identification, purification, and molecular cloning of a putative plastidic glucose transporter. Plant Cell 12:787-801
110. Weber APM. 2004. Solute transporters as connecting elements between cytosol and plastid stroma. Curr. Opinion Plant Biol. 7:247-53
111. Weise S, Weber APM, Sharkey TD. 2004. Maltose is the major form of carbon exported from the chloroplast at night. Planta 218:474-82
112. Wischmann B, Nielsen TH, Møller BL. 1999. In vitro biosynthesis of phosphorylated starch in intact potato amyloplasts. Plant Physiol. 119:1-8
113. Witt W, Sauter JJ. 1996. Purification and properties of the starch granule-degrading α-amylase from potato tubers. J. Exp. Bot. 47:1789-95
114. Yang Y, Steup M. 1990. Polysaccharide fraction from higher plants which strongly interacts with the cytosolic phosphorylase isozyme. Plant Physiol. 94:960-69
115. Yomo H, Varner JE. 1973. Control of the formation of amylases and proteases in the cotyledons of germinating peas. Plant Physiol. 51:708-13
116. Yu TS, Kofler H, Häusler RE, Hille D, Flügge UI, et al. 2001. The Arabidopsis sex1 mutant is defective in the R1 protein, a general regulator of starch degradation in plants, and not in the chloroplast hexose transporter. Plant Cell 13:1907-18
117. Zeeman SC, ap Rees T. 1999. Changes in carbohydrate metabolism and assimilate export in starch-excess mutants of Arabidopsis. Plant Cell Env. 22:1445-53
118. Zeeman SC, Northrop F, Smith AM, ap Rees T. 1998. A starch-accumulating mutant of Arabidopsis thaliana deficient in a chloroplastic starch hydrolyzing enzyme. Plant J. 15:357-65
119. Zeeman SC, Pilling E, Tiessen A, Kato L, Donald AM, Smith AM. 2002. Starch synthesis in Arabidopsis. Granule synthesis, composition, and structure. Plant Physiol. 129:516-29
120. Zeeman SC, Smith SM, Smith AM. 2004. The breakdown of starch in leaves. N. Phytol. 163:247-61
121. Zeeman SC, Thorneycroft D, Schupp N, Chapple A, Weck M, et al. 2004. Plastidial α-glucan phosphorylase is not required for starch degradation in Arabidopsis leaves but has a role in the tolerance of abiotic stress. Plant Physiol. 135:849-58
122. Zeeman SC, Umemoto T, Lue WL, Au-Yeung P, Martin C, et al. 1998. A mutant of Arabidopsis lacking a chloroplastic isoamylase accumulates both starch and phytoglycogen. Plant Cell 10:1699-711
123. Zeigler P. 1988. Partial purification and characterization of the major endoamylase of developing pea leaves. Plant Physiol. 86:659-66
124. Zhu ZP, Hylton CM, Rössner U, Smith AM. 1998. Characterization of starch-debranching enzymes in pea embryos. Plant Physiol. 118:581-90
125. Zrenner R, Krause KP, Apel P, Sonnewald U. 1996. Reduction of the cytosolic fructose -1,6-bisphosphatase in transgenic potato plants limits photosynthetic sucrose biosynthesis with no impact on plant growth and tuber yield. Plant J. 9:671-81
126. Baunsgaard L, Lütken H, Mikkelsen R, Glaring MA, Pham TT, Blennow A. 2005. A novel isoform of glucan, water dikinase phosphorylates pre-phosphorylated alpha-glucans and is involved in starch degradation in Arabidopsis. Plant J. 41:595-605
127. Kötting O, Pusch K, Tiessen A, Geigenberger P, Steup M, Ritte G. 2005. Identification of a novel enzyme required for starch metabolism in Arabidopsis leaves. The phosphoglucan, water dikinase. Plant Physiol. 137:242-52
128. Yu TS, Zeeman SC, Thorneycroft D, Fulton DC, Dunstan H, et al. 2005. alpha-amylase is not required for breakdown of transitory starch in Arabidopsis leaves. J. Biol. Chem. In press