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Literature summary for 2.4.1.19 extracted from

  • Abdel-Naby, M.A.; Fouad, A.A.; El-Refai, H.A.
    Catalytic and thermodynamic properties of glycosylated Bacillus cereus cyclodextrin glycosyltransferase (2015), Int. J. Biol. Macromol., 76, 132-137.
    View publication on PubMed
Search for more literature for 2.4.1.19

General Stability

General Stability Organism
the dextran (MW 47000)-conjugated form of the enzyme retains about 70.28% of the original specific catalytic activity exhibited by the native enzyme Bacillus cereus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
62000
-
 x * 62000, SDS-PAGE Bacillus cereus

Organism

Organism UniProt Comment Textmining
Bacillus cereus
-
-
-
Bacillus cereus NRC7
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
soluble starch + glycosyl acceptor
-
 Bacillus cereus alpha-cyclodextrin
-
 ?
soluble starch + glycosyl acceptor
-
 Bacillus cereus NRC7 alpha-cyclodextrin
-
 ?

Subunits

Subunits Comment Organism
? x * 62000, SDS-PAGE Bacillus cereus

Synonyms

Synonyms Comment Organism
CGTase
-
 Bacillus cereus
cyclodextrin glucosyltransferase
-
 Bacillus cereus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60 80 the native enzyme shows a half-life of 93.45 min, 56.34 min, and 43.57 min at 60, 70, and 80°C, respectively Bacillus cereus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.86
-
 soluble starch native enzyme, at pH 6.5 and 60°C Bacillus cereus
2.32
-
 soluble starch dextran-conjugated enzyme, at pH 6.5 and 60°C Bacillus cereus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
-
 Bacillus cereus