Literature summary for 2.4.1.19 extracted from

Leemhuis, H.; Kragh, K.M.; Dijkstra, B.W.; Dijkhuizen, L.
Engineering cyclodextrin glycosyltransferase into a starch hydrolase with a high exo-specificity (2003), J. Biotechnol., 103, 203-212.

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Protein Variants

Protein Variants	Comment	Organism
additional information	engineering cyclodextrin glycosyltransferase into a starch hydrolase with a high exospecificity. the cyclodextrin product specificity can be changed into linear product specificity, by introducing a five-residue insertion mutation at the donor substrate binding subsites. The CGTase mutants remain clearly different from the maltogenic alpha-amylase, as they have much lower hydrolytic activities, they form linear products of variable sizes and they retain a low cyclodextrin forming activity, whereas maltogenic alpha-amylases produce primarily maltose. The five-residue insertion, concomitantly, strongly enhances the exo-specificity of CGTase	Thermoanaerobacterium thermosulfurigenes

Organism

Organism	UniProt	Comment	Textmining
Thermoanaerobacterium thermosulfurigenes	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
starch + glycosyl acceptor	the cyclodextrin product specificity can be changed into linear product specificity, by introducing a five-residue insertion mutation at the donor substrate binding subsites. The CGTase mutants remain clearly different from the maltogenic alpha-amylase, as they have much lower hydrolytic activities, they form linear products of variable sizes and they retain a low cyclodextrin forming activity, whereas maltogenic alpha-amylases produce primarily maltose. The five-residue insertion, concomitantly, strongly enhances the exo-specificity of CGTase	Thermoanaerobacterium thermosulfurigenes	cyclodextrin	-	?

Synonyms

Synonyms	Comment	Organism
CGTase	-	Thermoanaerobacterium thermosulfurigenes

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Release 2023.1 (January 2023)