Literature summary extracted from
Busi, M.V.; Palopoli, N.; Valdez, H.A.; Fornasari, M.S.; Wayllace, N.Z.; Gomez-Casati, D.F.; Parisi, G.; Ugalde, R.A.
Functional and structural characterization of the catalytic domain of the starch synthase III from Arabidopsis thaliana (2008), Proteins, 70, 31-40.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.4.1.21 |
the catalytic C-terminal domain (SSIII-CD) of is cloned and expressed in Escherichia coli. SSIII-CD fully complements the production of glycogen by an Agrobacterium tumefaciens glycogen synthase null mutant, suggesting that this truncated isoform restores in vivo de novo synthesis of bacterial glycogen |
Arabidopsis thaliana |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.4.1.21 |
Arabidopsis thaliana |
F4IAG2 |
var. Columbia Col-0 |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.4.1.21 |
recombinantly expressed catalytic C-terminal domain (SSIII-CD) |
Arabidopsis thaliana |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.4.1.21 |
ADP-glucose + (1,4-alpha-D-glucosyl)n |
recombinant SSIII-CD uses with more efficiency rabbit muscle glycogen than amylopectin as primer and displays a high apparent affinity for ADP-Glc |
Arabidopsis thaliana |
ADP + (1,4-alpha-D-glucosyl)n+1 |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.4.1.21 |
SSIII |
- |
Arabidopsis thaliana |
2.4.1.21 |
starch synthase III |
- |
Arabidopsis thaliana |