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Literature summary for 2.4.1.19 extracted from

  • Li, C.; Ban, X.; Gu, Z.; Li, Z.
    Calcium ion contribution to thermostability of cyclodextrin glycosyltransferase is closely related to calcium-binding site CaIII (2013), J. Agric. Food Chem., 61, 8836-8841.
    View publication on PubMed
Search for more literature for 2.4.1.19

Protein Variants

Protein Variants Comment Organism
A315D the mutation significantly changes the contribution of Ca2+ to the enzyme's thermostability Niallia circulans
D577K the mutation significantly changes the contribution of Ca2+ to the enzyme's thermostability Niallia circulans

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ the enzyme has three Ca2+ binding sites. Ca2+ has a small contribution to the enzyme's thermostability Niallia circulans
Ca2+ the enzyme has two Ca2+ binding sites. Ca2+ has a small contribution to the enzyme's thermostability Paenibacillus macerans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
starch + glycosyl acceptor Paenibacillus macerans
-
 alpha-cyclodextrin
-
 ?
starch + glycosyl acceptor Niallia circulans
-
 beta-cyclodextrin
-
 ?

Organism

Organism UniProt Comment Textmining
Niallia circulans
-
-
-
Paenibacillus macerans
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
starch + glycosyl acceptor
-
 Paenibacillus macerans alpha-cyclodextrin
-
 ?
starch + glycosyl acceptor
-
 Niallia circulans beta-cyclodextrin
-
 ?

Synonyms

Synonyms Comment Organism
alpha-CGTase
-
 Paenibacillus macerans
alpha-cyclodextrin glycosyltransferase
-
 Paenibacillus macerans
beta-CGTase
-
 Niallia circulans
beta-cyclodextrin glycosyltransferase
-
 Niallia circulans