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Literature summary for 2.7.7.27 extracted from

  • Haedrich, N.; Hendriks, J.H.; Koetting, O.; Arrivault, S.; Feil, R.; Zeeman, S.C.; Gibon, Y.; Schulze, W.X.; Stitt, M.; Lunn, J.E.
    Mutagenesis of cysteine 81 prevents dimerization of the APS1 subunit of ADP-glucose pyrophosphorylase and alters diurnal starch turnover in Arabidopsis thaliana leaves (2012), Plant J., 70, 231-242.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
C81S mutation in small subunit APS1. Substitution of Cys81 by serine prevents small subunit APS1 dimerization. Cys81 is both necessary and sufficient for dimerization of APS1. Compared to control plants, the C81S lines have higher levels of ADP-glucose and maltose, and either increased rates of starch synthesis or a starch-excess phenotype, depending on the daylength. APS1 protein levels are five- to tenfold lower than in control plants Arabidopsis thaliana
additional information complementation of an aps1 null mutant with a series of constructs containing a full-length APS1 gene encoding either the wild-type APS1 protein or mutated forms in which one of the five cysteine residues is replaced by serine. Substitution of Cys81 by serine prevents small subunit APS1 dimerization, whereas mutation of the other cysteines had no effect Arabidopsis thaliana

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana P55228 small subunit
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Source Tissue

Source Tissue Comment Organism Textmining
leaf
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Arabidopsis thaliana
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Synonyms

Synonyms Comment Organism
APS1
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Arabidopsis thaliana