1989
DOI: 10.1021/bk-1989-0389.ch006
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Regulation of Starch Synthesis

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Cited by 10 publications
(4 citation statements)
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“…These conclusions were drawn from studies on a irreversible binding of labelled pyridoxal-P (ana log of PGA) and 8-azido-ADP-glucose (analog of ADP-glucose) to the purified spinach enzyme [13,14,27], and from the comparison of conserved re gions of AGP from several species [17,28,29], Based on studies with spinach AGP, the activatorbinding site was postulated to be located both on the small and large subunit [13,27], while the substrate-binding site is present almost exclusively on the large subunit [27]. However, an Arabidopsis m utant entirely lacking the large subunit o f AGP and having only about 4% of the small subunit protein has been reported [5] to have about 5% of the AGP activity, when compared to wild type plants, suggesting that the small subunit o f A G P in this species does contain the substrate-binding do main.…”
Section: Subunit Structurementioning
confidence: 99%
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“…These conclusions were drawn from studies on a irreversible binding of labelled pyridoxal-P (ana log of PGA) and 8-azido-ADP-glucose (analog of ADP-glucose) to the purified spinach enzyme [13,14,27], and from the comparison of conserved re gions of AGP from several species [17,28,29], Based on studies with spinach AGP, the activatorbinding site was postulated to be located both on the small and large subunit [13,27], while the substrate-binding site is present almost exclusively on the large subunit [27]. However, an Arabidopsis m utant entirely lacking the large subunit o f AGP and having only about 4% of the small subunit protein has been reported [5] to have about 5% of the AGP activity, when compared to wild type plants, suggesting that the small subunit o f A G P in this species does contain the substrate-binding do main.…”
Section: Subunit Structurementioning
confidence: 99%
“…Unfortunately, the state of oligomerization of the small subunits of native A G P in this Arabi dopsis m utant is unknown at present. The hom o tetrameric AGP from E. coli differs from plant A G P in the structure of the activator-binding site, but not the substrate-binding dom ain [14,[27][28][29], probably reflecting the distinct nature of activa tors of the bacterial and plant AGP.…”
Section: Subunit Structurementioning
confidence: 99%
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