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discounted EARLY registration ends Dec 31, 2014
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discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Pathway: starch degradation I

Enzyme View:

This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Synonyms: starch mobilization from cereal endosperm, starch degradation from cereal endosperm

Superclasses: Biosynthesis Carbohydrates Biosynthesis Sugars Biosynthesis
Degradation/Utilization/Assimilation Carbohydrates Degradation Polysaccharides Degradation Starch Degradation
Degradation/Utilization/Assimilation Polymeric Compounds Degradation Polysaccharides Degradation Starch Degradation

Some taxa known to possess this pathway include ? : Hordeum vulgare , Oryza sativa , Zea mays

Expected Taxonomic Range: Poaceae

Summary:
General Background

Plants accumulate and mobilize starch in both photosynthetic tissue (leaves) and non-photosynthetic storage tissues (such as tuber and seed endosperm). In leaves, starch is synthesized during the light period and is degraded during the dark period. In storage tissues, starch is degraded during tuber sprouting and seed germinating. Except for seed endosperm where starch degradation occurs in an acellular tissue, starch degradation generally occurs in the plastids (chloroplast of leaves and amyloplast of tubers) where starch accumulates. Isoforms of the starch degradation enzymes are also found and in many cases abundant in extra-plastidic subcellular locations in leaves and tubers. Their physiological functions are not well understood [Zeeman10].

About This Pathway

This pathway represents the starch degradation route present in the endosperm of cereal crops. Many details of the pathway as well as the relative importance of the four types of enzymes that contribute to this process, namely α-amylases, β-amylases, limit dextran debranching enzymes, and α-glucosidases, are still the subject of investigation and debate [Zeeman10, Stanley11].

Citations: [Kossmann00, Finnie11, Sun91, Rejzek11, Wu02c]

Variants: starch degradation II , starch degradation III , starch degradation IV , starch degradation V

Unification Links: PlantCyc:PWY-842

Credits:
Created 16-Feb-2011 by Zhang P , TAIR , PMN
Revised 07-Mar-2013 by Dreher KA , PMN


References

Finnie11: Finnie C, Andersen B, Shahpiri A, Svensson B (2011). "Proteomes of the barley aleurone layer: A model system for plant signalling and protein secretion." Proteomics 11(9);1595-605. PMID: 21433287

Kossmann00: Kossmann J, Lloyd J (2000). "Understanding and influencing starch biochemistry." Crit Rev Biochem Mol Biol 2000;35(3);141-96. PMID: 10907795

Mu01: Mu HH, Yu Y, Wasserman BP, Carman GM (2001). "Purification and characterization of the maize amyloplast stromal 112-kDa starch phosphorylase." Arch Biochem Biophys 388(1);155-64. PMID: 11361132

Rejzek11: Rejzek M, Stevenson CE, Southard AM, Stanley D, Denyer K, Smith AM, Naldrett MJ, Lawson DM, Field RA (2011). "Chemical genetics and cereal starch metabolism: structural basis of the non-covalent and covalent inhibition of barley β-amylase." Mol Biosyst 7(3);718-30. PMID: 21085740

Sogaard90: Sogaard M, Svensson B (1990). "Expression of cDNAs encoding barley alpha-amylase 1 and 2 in yeast and characterization of the secreted proteins." Gene 1990;94(2);173-9. PMID: 2258050

Stanley11: Stanley D, Rejzek M, Naested H, Smedley M, Otero S, Fahy B, Thorpe F, Nash RJ, Harwood W, Svensson B, Denyer K, Field RA, Smith AM (2011). "The role of alpha-glucosidase in germinating barley grains." Plant Physiol 155(2);932-43. PMID: 21098673

Sun91: Sun ZT, Henson CA (1991). "A quantitative assessment of the importance of barley seed alpha-amylase, beta-amylase, debranching enzyme, and alpha-glucosidase in starch degradation." Arch Biochem Biophys 284(2);298-305. PMID: 1824915

Wu02c: Wu C, Colleoni C, Myers AM, James MG (2002). "Enzymatic properties and regulation of ZPU1, the maize pullulanase-type starch debranching enzyme." Arch Biochem Biophys 406(1);21-32. PMID: 12234486

Zeeman10: Zeeman SC, Kossmann J, Smith AM (2010). "Starch: its metabolism, evolution, and biotechnological modification in plants." Annu Rev Plant Biol 61;209-34. PMID: 20192737

Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

Dinges03: Dinges JR, Colleoni C, James MG, Myers AM (2003). "Mutational analysis of the pullulanase-type debranching enzyme of maize indicates multiple functions in starch metabolism." Plant Cell 2003;15(3);666-80. PMID: 12615940

Dong97: Dong G, Vieille C, Zeikus JG (1997). "Cloning, sequencing, and expression of the gene encoding amylopullulanase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme." Appl Environ Microbiol 63(9);3577-84. PMID: 9293009

Frandsen00: Frandsen TP, Lok F, Mirgorodskaya E, Roepstorff P, Svensson B (2000). "Purification, enzymatic characterization, and nucleotide sequence of a high-isoelectric-point alpha-glucosidase from barley malt." Plant Physiol 123(1);275-86. PMID: 10806244

Fulton08: Fulton DC, Stettler M, Mettler T, Vaughan CK, Li J, Francisco P, Gil M, Reinhold H, Eicke S, Messerli G, Dorken G, Halliday K, Smith AM, Smith SM, Zeeman SC (2008). "Beta-AMYLASE4, a noncatalytic protein required for starch breakdown, acts upstream of three active beta-amylases in Arabidopsis chloroplasts." Plant Cell 20(4);1040-58. PMID: 18390594

Kang05a: Kang S, Vieille C, Zeikus JG (2005). "Identification of Pyrococcus furiosus amylopullulanase catalytic residues." Appl Microbiol Biotechnol 66(4);408-13. PMID: 15599521

Lao99: Lao NT, Schoneveld O, Mould RM, Hibberd JM, Gray JC, Kavanagh TA (1999). "An Arabidopsis gene encoding a chloroplast-targeted beta-amylase." Plant J 1999;20(5);519-27. PMID: 10652124

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Naested06: Naested H, Kramhoft B, Lok F, Bojsen K, Yu S, Svensson B (2006). "Production of enzymatically active recombinant full-length barley high pI alpha-glucosidase of glycoside family 31 by high cell-density fermentation of Pichia pastoris and affinity purification." Protein Expr Purif 46(1);56-63. PMID: 16343940

Sjakste04: Sjakste T, Roder M (2004). "Distribution and inheritance of beta-amylase alleles in north European barley varieties." Hereditas 141(1);39-45. PMID: 15383070

Stryer88: Stryer L "Biochemistry." WH Freeman and Co., 3rd edition, New York, 1988.

Vinje10: Vinje MA, Duke SH, Henson CA (2010). "Utilization of Different Bmy1 Intron III Alleles for Predicting β-Amylase Activity and Thermostability in Wild and Cultivated Barley." Plant Molecular Biology Reporter 28(3);491-501.

Vinje11: Vinje MA, Willis DK, Duke SH, Henson CA (2011). "Differential RNA expression of Bmy1 during barley seed development and the association with β-amylase accumulation, activity, and total protein." Plant Physiol Biochem 49(1);39-45. PMID: 20974538

Vinje11a: Vinje MA, Willis DK, Duke SH, Henson CA (2011). "Differential expression of two β-amylase genes (Bmy1 and Bmy2) in developing and mature barley grain." Planta 233(5);1001-10. PMID: 21279650

Yoshigi94: Yoshigi N, Okada Y, Sahara H, Koshino S (1994). "PCR cloning and sequencing of the beta-amylase cDNA from barley." J Biochem 115(1);47-51. PMID: 8188635

Yoshigi94a: Yoshigi N, Okada Y, Sahara H, Koshino S (1994). "Expression in Escherichia coli of cDNA encoding barley beta-amylase and properties of recombinant beta-amylase." Biosci Biotechnol Biochem 58(6);1080-6. PMID: 7765034


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Thu Dec 18, 2014, BIOCYC13A.