From bacterial glycogen to starch: understanding the biogenesis of the plant starch granule

Plants, green algae, and cyanobacteria synthesize storage polysaccharides by a similar ADPglucose-based pathway. Plant starch metabolism can be distinguished from that of bacterial glycogen by the presence of multiple forms of enzyme activities for each step of the pathway. This multiplicity does no...

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Bibliographic Details
Published in:Annual review of plant biology 2003-01, Vol.54 (1), p.207-233
Main Authors: Ball, Steven G, Morell, Matthew K
Format: Article
Language:English
Subjects:
Adenosine Diphosphate Glucose - metabolism
Algae
Amylose - biosynthesis
Aquatic plants
Bacteria
Bacteria - metabolism
Biochemistry
Biochemistry, Molecular Biology
Biosynthesis
Carbohydrates
E coli
Enzymatic activity
Enzymes
Flowers & plants
Glycogen - biosynthesis
Glycogen - metabolism
Life Sciences
Metabolism
Plants - metabolism
Plants - microbiology
Saccharides
Starch
Starch - biosynthesis
Starch - metabolism
Starch Synthase - metabolism
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Summary:Plants, green algae, and cyanobacteria synthesize storage polysaccharides by a similar ADPglucose-based pathway. Plant starch metabolism can be distinguished from that of bacterial glycogen by the presence of multiple forms of enzyme activities for each step of the pathway. This multiplicity does not coincide with any functional redundancy, as each form has seemingly acquired a distinctive and conserved role in starch metabolism. Comparisons of phenotypes generated by debranching enzyme-defective mutants in Escherichia coli and plants suggest that enzymes previously thought to be involved in polysaccharide degradation have been recruited during evolution to serve a particular purpose in starch biosynthesis. Speculations have been made that link this recruitment to the appearance of semicrystalline starch in photosynthetic eukaryotes. Besides the common core pathway, other enzymes of malto-oligosaccharide metabolism are required for normal starch metabolism. However, according to the genetic and physiological system under study, these enzymes may have acquired distinctive roles.
ISSN:1543-5008
1040-2519
1545-2123
DOI:10.1146/annurev.arplant.54.031902.134927