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Literature summary extracted from

  • Martins, R.F.; Hatti-Kaul, R.
    Bacillus agaradhaerens LS-3C cyclodextrin glycosyltransferase: activity and stability features (2003), Enzyme Microb. Technol., 33, 819-827.
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.4.1.19 PEG 3000 10% w/v, increases cyclodextrin production Salipaludibacillus agaradhaerens
2.4.1.19 sorbitol 1 mM, increases cyclodextrin production Salipaludibacillus agaradhaerens

General Stability

EC Number General Stability Organism
2.4.1.19 enzyme stability is greatly enhanced with sorbitol Salipaludibacillus agaradhaerens

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.19 beta-cyclodextrin inhibits cyclization Salipaludibacillus agaradhaerens
2.4.1.19 maltose inhibits cyclization Salipaludibacillus agaradhaerens

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.19 Salipaludibacillus agaradhaerens
-
 LS-3C
-
2.4.1.19 Salipaludibacillus agaradhaerens LS-3C
-
 LS-3C
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.19 maltodextrin + glycosyl acceptor displays unusually high amylolytic activity in relation to the cyclization activity. Disproportionation activity of the CGTase is optimal with maltose as the acceptor substrate. Cyclization reaction and beta-cyclodextrin formation are significantly promoted in the presence of CaCl2. The salt allows the cyclization reaction to be performed at higher temperature Salipaludibacillus agaradhaerens beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin the product of cyclization reaction is predominantly beta-cyclodextrin along with alpha-cyclodextrin as a minor product. The CDs profile is influenced by the reaction conditions. At pH 10, alpha-cyclodextrin is replaced by gamma-cyclodextrin formation ?
2.4.1.19 maltodextrin + glycosyl acceptor displays unusually high amylolytic activity in relation to the cyclization activity. Disproportionation activity of the CGTase is optimal with maltose as the acceptor substrate. Cyclization reaction and beta-cyclodextrin formation are significantly promoted in the presence of CaCl2. The salt allows the cyclization reaction to be performed at higher temperature Salipaludibacillus agaradhaerens LS-3C beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin the product of cyclization reaction is predominantly beta-cyclodextrin along with alpha-cyclodextrin as a minor product. The CDs profile is influenced by the reaction conditions. At pH 10, alpha-cyclodextrin is replaced by gamma-cyclodextrin formation ?