Abstract:
:ADP-glucose pyrophosphorylase (AGPase) is a key regulatory enzyme in starch biosynthesis. However, plant AGPases differ in several parameters, including spatial and temporal expression, allosteric regulation, and heat stability. AGPases of cereal endosperms are heat labile, while those in other tissues, such as the potato (Solanum tuberosum) tuber, are heat stable. Sequence comparisons of heat-stable and heat-labile AGPases identified an N-terminal motif unique to heat-stable enzymes. Insertion of this motif into recombinant maize (Zea mays) endosperm AGPase increased the half-life at 58 degrees C more than 70-fold. Km values for physiological substrates were unaffected, although Kcat was doubled. A cysteine within the inserted motif gives rise to small subunit homodimers not found in the wild-type maize enzyme. Placement of this N-terminal motif into a mosaic small subunit containing the N terminus from maize endosperm and the C terminus from potato tuber AGPase increases heat stability more than 300-fold.
journal_name
Plant Physioljournal_title
Plant physiologyauthors
Linebarger CR,Boehlein SK,Sewell AK,Shaw J,Hannah LCdoi
10.1104/pp.105.067637subject
Has Abstractpub_date
2005-12-01 00:00:00pages
1625-34issue
4eissn
0032-0889issn
1532-2548pii
pp.105.067637journal_volume
139pub_type
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