Literature summary for 2.4.1.19 extracted from
Chen, X.; Huang, L.; Sun, J.; Liu, J.; Wang, W.; Sun, M.; Hao, J.
Production and characterization of a new alpha-cyclodextrin glycosyltransferase from a marine strain of Bacillus sp. Y112 (2017), J. Biobased Mat. Bioenergy, 11, 236-241 .
No PubMed abstract available
Inhibitors
Inhibitors |
Comment |
Organism |
Structure |
Ag+ |
complete inhibition at 5 mM |
Bacillus sp. Y112 |
|
Al3+ |
98% residual activity at 5 mM |
Bacillus sp. Y112 |
|
Ca2+ |
93.9% residual activity at 5 mM |
Bacillus sp. Y112 |
|
Co2+ |
87.8% residual activity at 5 mM |
Bacillus sp. Y112 |
|
CTAB |
98% residual activity at 5 mM |
Bacillus sp. Y112 |
|
Cu2+ |
98% residual activity at 5 mM |
Bacillus sp. Y112 |
|
DMSO |
98% residual activity at 5 mM |
Bacillus sp. Y112 |
|
EDTA |
87.8% residual activity at 5 mM |
Bacillus sp. Y112 |
|
Fe2+ |
91.8% residual activity at 5 mM |
Bacillus sp. Y112 |
|
Fe3+ |
91.8% residual activity at 5 mM |
Bacillus sp. Y112 |
|
Hg2+ |
95.9% residual activity at 5 mM |
Bacillus sp. Y112 |
|
Li+ |
95.9% residual activity at 5 mM |
Bacillus sp. Y112 |
|
SDS |
81.6% residual activity at 5 mM |
Bacillus sp. Y112 |
|
Tween 20 |
98% residual activity at 5 mM |
Bacillus sp. Y112 |
|
Zn2+ |
85.7% residual activity at 5 mM |
Bacillus sp. Y112 |
|
Metals/Ions
Metals/Ions |
Comment |
Organism |
Structure |
Mg2+ |
the enzymatic activity increases to 104.1% in the presence of 5 mM MgCl2 |
Bacillus sp. Y112 |
|
Mn2+ |
the enzymatic activity increases to 104.1% in the presence of 5 mM MnCl2 |
Bacillus sp. Y112 |
|
additional information |
not influenced by 5 mM Ba2+ |
Bacillus sp. Y112 |
|
Molecular Weight [Da]
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
90000 |
- |
gel filtration |
Bacillus sp. Y112 |
Organism
Organism |
UniProt |
Comment |
Textmining |
Bacillus sp. Y112 |
- |
- |
- |
Purification (Commentary)
Purification (Comment) |
Organism |
ethanol precipitation, Superdex 200 gel filtration and DEAE-Sepharose column chromatography |
Bacillus sp. Y112 |
Substrates and Products (Substrate)
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
soluble starch + glycosyl acceptor |
- |
Bacillus sp. Y112 |
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin |
- |
? |
|
Subunits
Subunits |
Comment |
Organism |
monomer |
1 * 90000, SDS-PAGE |
Bacillus sp. Y112 |
Synonyms
Synonyms |
Comment |
Organism |
alpha-CGTase |
- |
Bacillus sp. Y112 |
alpha-cyclodextrin glycosyltransferase |
- |
Bacillus sp. Y112 |
Temperature Optimum [°C]
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
55 |
- |
- |
Bacillus sp. Y112 |
Temperature Range [°C]
Temperature Minimum [°C] |
Temperature Maximum [°C] |
Comment |
Organism |
50 |
60 |
the relative activity at 50°C and 60°C is 93% and 80%, respectively |
Bacillus sp. Y112 |
Temperature Stability [°C]
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Comment |
Organism |
25 |
45 |
the purified enzyme is stable up to 45°C after pre-incubation in buffer for 1 h at pH 8.5 |
Bacillus sp. Y112 |
pH Optimum
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
8.5 |
- |
- |
Bacillus sp. Y112 |
pH Range
pH Minimum |
pH Maximum |
Comment |
Organism |
5 |
10 |
more than 60% activity between pH 6.0 and 10.0 |
Bacillus sp. Y112 |
pH Stability
pH Stability |
pH Stability Maximum |
Comment |
Organism |
5 |
11 |
the enzyme retains 100% of its initial activity in a range of pH 7.0 to 9.0 after pre-incubation in buffer for 1 h at 25°C. The enzyme is highly stable at pH 5.0 and 11.0 as indicated by the maintenance of 77% and 72% residual activity, respectively |
Bacillus sp. Y112 |