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Literature summary extracted from

  • Zehentgruber, D.; Lundemo, P.; Svensson, D.; Adlercreutz, P.
    Substrate complexation and aggregation influence the cyclodextrin glycosyltransferase (CGTase) catalyzed synthesis of alkyl glycosides (2011), J. Biotechnol., 155, 232-235.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.25 additional information
-
 additional information at 25 mM alpha-cyclodextrin, the reaction rate decreases with increasing dodecyl-beta-maltoside concentration, and when the alpha-cyclodextrin concentration is varied at fixed dodecyl-beta-maltoside concentration, an S shaped curve is obtained Paenibacillus macerans
2.4.1.25 18
-
 dodecyl-beta-maltoside pH 5.2, 60°C, 300 mM alpha-cyclodextrin Paenibacillus macerans

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.25 Paenibacillus macerans
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.25 dodecyl-beta-maltoside + alpha-cyclodextrin
-
 Paenibacillus macerans dodecyl-beta-maltooctaoside + ?
-
 ?
2.4.1.25 dodecyl-beta-maltoside + starch when starch is used as glycosyl donor in the CGTase catalyzed alkyl glycoside elongation reaction, it is important to choose reaction conditions under which the cyclization of starch to alpha-cyclodextrin is efficient, since alpha-cyclodextrin may form low reactivity complexes with dodecyl-beta-maltoside Paenibacillus macerans dodecyl-beta-maltooctaoside + ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.25 CGTase
-
 Paenibacillus macerans