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Literature summary for 2.4.1.21 extracted from

  • Denyer, K.; Waite, D.; Edwards, A.; Martin, C.; Smith, A.M.
    Interaction with amylopectin influences the ability of granule-bound starch synthase I to elongate malto-oligosaccharides (1999), Biochem. J., 342, 647-653.
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
expression of granule-bound starch synthase I in Escherichia coli Pisum sativum
expression of granule-bound starch synthase in Escherichia coli Solanum tuberosum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Solanum tuberosum
additional information
-
additional information recombinant starch synthase II, amylopectin: 4.6 mg/ml Pisum sativum
15.3
-
maltotriose recombinant granule-bound starch synthase I Solanum tuberosum

Organism

Organism UniProt Comment Textmining
Pisum sativum
-
starch synthase II
-
Solanum tuberosum
-
granule-bound starch synthase I
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP-glucose + maltotriose
-
Pisum sativum ADP + maltotetraose
-
?
ADP-glucose + maltotriose 6.4fold activation of maltotriose elongation by granule-bound starch synthase I by amylopectin promoting a processive mode of maltotriose elongation Solanum tuberosum ADP + maltotetraose
-
?