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Literature summary extracted from

  • Wayllace, N.Z.; Valdez, H.A.; Ugalde, R.A.; Busi, M.V.; Gomez-Casati, D.F.
    The starch-binding capacity of the noncatalytic SBD2 region and the interaction between the N- and C-terminal domains are involved in the modulation of the activity of starch synthase III from Arabidopsis thaliana (2010), FEBS J., 277, 428-440.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.21 W366A mutation in starch-binding domains, 3fold decrease in affinity to starch Arabidopsis thaliana
2.4.1.21 W366A/Y394A mutation in starch-binding domains, significant decrease in affinity to starch Arabidopsis thaliana
2.4.1.21 Y394A mutation in starch-binding domains, 2fold decrease in affinity to starch Arabidopsis thaliana

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.21 0.28
-
 ADP-glucose catalytic domain Arabidopsis thaliana
2.4.1.21 0.59
-
 ADP-glucose catalytic domain co-expressed with starch-binding domain 3 and large part of starch-binding domain 2 Arabidopsis thaliana
2.4.1.21 0.62
-
 ADP-glucose catalytic domain co-expressed with starch-binding domains 23 Arabidopsis thaliana
2.4.1.21 0.81
-
 ADP-glucose catalytic domain co-expressed with starch-binding domain 2 and part of starch-binding domain 3 Arabidopsis thaliana
2.4.1.21 0.95
-
 ADP-glucose catalytic domain co-expressed with starch-binding domains 123 Arabidopsis thaliana
2.4.1.21 1.68
-
 ADP-glucose truncated protein lacking starch binding domain 1 and large part of starch binding domain 2 Arabidopsis thaliana
2.4.1.21 1.74
-
 ADP-glucose truncated protein lacking starch-binding domains 12 Arabidopsis thaliana
2.4.1.21 1.77
-
 ADP-glucose truncated protein lacking starch binding domain 1 and medium part of starch binding domain 2 Arabidopsis thaliana
2.4.1.21 2.39
-
 ADP-glucose truncated protein lacking starch binding domain 1 and small part of starch binding domain 2 Arabidopsis thaliana
2.4.1.21 2.56
-
 ADP-glucose truncated protein lacking starch-binding domain 1 Arabidopsis thaliana
2.4.1.21 4.08
-
 ADP-glucose wild-type Arabidopsis thaliana

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.21 Arabidopsis thaliana
-
 starch synthase III
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.21 ADP-glucose + glycogen
-
 Arabidopsis thaliana ADP + ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.1.21 More enzyme contains an N-terminal region, including three in-tandem starch-binding domains, followed by a C-terminal catalytic domain. The D(316-344) and D(495-535) regions in the D2 and D3 domains, respectively, but not the individual starch-binding domains, are involved in the interaction with the catalytic domain. Residues W366 and Y394 in the D2 domain are important in starch binding. Residue W366 is key to the apparent affinity for the polysaccharide substrate of starch synthase III Arabidopsis thaliana