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Literature summary extracted from

  • Brust, H.; Lehmann, T.; DHulst, C.; Fettke, J.
    Analysis of the functional interaction of Arabidopsis starch synthase and branching enzyme isoforms reveals that the cooperative action of SSI and BEs results in glucans with polymodal chain length distribution similar to amylopectin (2014), PLoS ONE, 9, e102364.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.18 recombinant expression of His-tagged isozymes rBE2 and rBE3 in Escherichia coli strain BL21(DE3) and in strain DELTAglgCAP with BL21(DE3) background Arabidopsis thaliana
2.4.1.21 expressed in Escherichia coli BL21(DE3) cells Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.21 ADP-alpha-D-glucose + [(1->4)-alpha-D-glucosyl]n Arabidopsis thaliana
-
 ADP + [(1->4)-alpha-D-glucosyl]n+1
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.18 Arabidopsis thaliana
-
-
-
2.4.1.21 Arabidopsis thaliana
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.18 recombinant His-tagged isozymes rBE2 and rBE3 from Escherichia coli strains by nickel affinity chromatography Arabidopsis thaliana

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.1.18 leaf
-
 Arabidopsis thaliana
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.18 additional information Starch synthase I activity in native PAGE without addition of glucans is dependent on at least one of the two branching enzyme isoforms active in Arabidopsis leaves. This interaction is most likely not based on a physical association of the enzymes. Chain length distribution patterns of the formed glucans are irrespective of enzyme isoforms origin and still independent of assay conditions. All starch synthase isoforms I-IV are able to interact with branching enzymes and form branched glucans, product analysis, overview Arabidopsis thaliana ?
-
 ?
2.4.1.21 ADP-alpha-D-glucose + maltodextrin
-
 Arabidopsis thaliana ADP + ?
-
 ?
2.4.1.21 ADP-alpha-D-glucose + soluble starch
-
 Arabidopsis thaliana ADP + ?
-
 ?
2.4.1.21 ADP-alpha-D-glucose + [(1->4)-alpha-D-glucosyl]n
-
 Arabidopsis thaliana ADP + [(1->4)-alpha-D-glucosyl]n+1
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.18 SBE
-
 Arabidopsis thaliana
2.4.1.18 starch branching enzyme
-
 Arabidopsis thaliana
2.4.1.21 SSI isoform Arabidopsis thaliana
2.4.1.21 SSIII isoform Arabidopsis thaliana
2.4.1.21 starch synthase
-
 Arabidopsis thaliana

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.18 8
-
 assay at Arabidopsis thaliana

General Information

EC Number General Information Comment Organism
2.4.1.18 metabolism starch synthase and branching enzyme establish the two glycosidic linkages existing in starch. Both enzymes exist as several isoforms. Starch synthase I activity in native PAGE without addition of glucans is dependent on at least one of the two branching enzyme isoforms active in Arabidopsis leaves. This interaction is most likely not based on a physical association of the enzymes. All starch synthase isoforms I-IV are able to interact with branching enzymes and form branched glucans Arabidopsis thaliana