Journal article
Subunit interactions specify the allosteric regulatory properties of the potato tuber ADP-glucose pyrophosphorylase
Biochemical and biophysical research communications, Vol.362(2), pp.301-306
2007
Handle:
https://hdl.handle.net/2376/117928
PMID: 17707339
Abstract
ADP-glucose pyrophosphorylase (AGPase) catalyzes the first committed step of starch synthesis in plants. The potato tuber enzyme contains a pair of catalytic small subunits (SSs) and a pair of non-catalytic large subunits (LSs). We have previously identified a LS mutant containing a P52L replacement, which rendered the enzyme with down-regulatory properties. To investigate the structure–function relationships between the two subunits with regard to allosteric regulation, putative SS mutants that could reverse the down-regulatory condition of LS
P52L were identified by their ability to restore glycogen accumulation in an AGPase-deficient
Escherichia coli glgC-strain. Two distinct LS-dependent classes, bona fide SS suppressors dependent on LS
P52L but not LS
WT and SS up-regulating allosteric mutants, were evident by kinetic analysis. These results indicate that both LS and SS have a regulatory function in controlling allosteric properties through enhancing cooperative subunit interactions.
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Details
- Title
- Subunit interactions specify the allosteric regulatory properties of the potato tuber ADP-glucose pyrophosphorylase
- Creators
- Dongwook KimSeon-Kap HwangThomas W Okita
- Publication Details
- Biochemical and biophysical research communications, Vol.362(2), pp.301-306
- Academic Unit
- Biological Chemistry, Institute of
- Publisher
- Elsevier Inc
- Identifiers
- 99900548052101842
- Language
- English
- Resource Type
- Journal article