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Literature summary extracted from

  • Jeang, C.L.; Lin, D.G.; Hsieh, S.H.
    Characterization of cyclodextrin glycosyltransferase of the same gene expressed from Bacillus macerans, Bacillus subtilis, and Escherichia coli (2005), J. Agric. Food Chem., 53, 6301-6304.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.4.1.19 cytosol
-
 Escherichia coli 5829
-
2.4.1.19 extracellular
-
 Bacillus subtilis
-
-
2.4.1.19 extracellular
-
 Paenibacillus macerans
-
-
2.4.1.19 periplasm
-
 Escherichia coli
-
-

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.19 Bacillus subtilis
-
-
-
2.4.1.19 Escherichia coli
-
-
-
2.4.1.19 Paenibacillus macerans
-
 IAM1243
-
2.4.1.19 Paenibacillus macerans IAM1243
-
 IAM1243
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.19
-
 Bacillus subtilis
2.4.1.19
-
 Escherichia coli
2.4.1.19
-
 Paenibacillus macerans

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.1.19 culture medium
-
 Bacillus subtilis
-
2.4.1.19 culture medium
-
 Escherichia coli
-
2.4.1.19 culture medium
-
 Paenibacillus macerans
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.19 additional information when the coupling reaction is measured utilizing beta-cyclodextrin as substrate, CGTase from Escherichia coli displays a 14fold greater catalytic activity as compared to CGTase from Bacillus macerans or CGTase from Bacillis subtilis. The coupling activity of CGTase from Escherichia coli is not significantly different from that of CGTase from Bacillus macerans or CGTase from Bacillus subtilis when alpha-cyclodextrin is used as the substrate Bacillus subtilis ?
-
 ?
2.4.1.19 additional information when the coupling reaction is measured utilizing beta-cyclodextrin as substrate, CGTase from Escherichia coli displays a 14fold greater catalytic activity as compared to CGTase from Bacillus macerans or CGTase from Bacillis subtilis. The coupling activity of CGTase from Escherichia coli is not significantly different from that of CGTase from Bacillus macerans or CGTase from Bacillus subtilis when alpha-cyclodextrin is used as the substrate Escherichia coli ?
-
 ?
2.4.1.19 additional information when the coupling reaction is measured utilizing beta-cyclodextrin as substrate, CGTase from Escherichia coli displays a 14fold greater catalytic activity as compared to CGTase from Bacillus macerans or CGTase from Bacillis subtilis. The coupling activity of CGTase from Escherichia coli is not significantly different from that of CGTase from Bacillus macerans or CGTase from Bacillus subtilis when alpha-cyclodextrin is used as the substrate Paenibacillus macerans ?
-
 ?
2.4.1.19 additional information when the coupling reaction is measured utilizing beta-cyclodextrin as substrate, CGTase from Escherichia coli displays a 14fold greater catalytic activity as compared to CGTase from Bacillus macerans or CGTase from Bacillis subtilis. The coupling activity of CGTase from Escherichia coli is not significantly different from that of CGTase from Bacillus macerans or CGTase from Bacillus subtilis when alpha-cyclodextrin is used as the substrate Paenibacillus macerans IAM1243 ?
-
 ?
2.4.1.19 starch enzymes from Escherichia coli, Bacillus macerans and Bacillus subtilis show similar production profile in cyclization reaction Bacillus subtilis cyclodextrin
-
 ?
2.4.1.19 starch enzymes from Escherichia coli, Bacillus macerans and Bacillus subtilis show similar pruduction profile in cyclization reaction Escherichia coli cyclodextrin
-
 ?
2.4.1.19 starch enzymes from Escherichia coli, Bacillus macerans and Bacillus subtilis show similar pruduction profile in cyclization reaction Paenibacillus macerans cyclodextrin
-
 ?
2.4.1.19 starch enzymes from Escherichia coli, Bacillus macerans and Bacillus subtilis show similar pruduction profile in cyclization reaction Paenibacillus macerans IAM1243 cyclodextrin
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.4.1.19 50
-
 30 min, stable Bacillus subtilis
2.4.1.19 50
-
 30 min, stable Escherichia coli
2.4.1.19 50
-
 30 min, stable Paenibacillus macerans
2.4.1.19 60
-
 30 min, about 50% loss of activity Bacillus subtilis
2.4.1.19 60
-
 30 min, about 50% loss of activity Paenibacillus macerans
2.4.1.19 60
-
 30 min, about 90% loss of activity Escherichia coli
2.4.1.19 70
-
 30 min, complete loss of activity Bacillus subtilis
2.4.1.19 70
-
 30 min, about 90% loss of activity Paenibacillus macerans