EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   3.2.1.59 | alpha-1,3-glucan + H2O |
- |
Schizosaccharomyces pombe |
? |
- |
? |
| 3.2.1.59 | alpha-1,3-glucan + H2O |
100% activity |
Streptomyces thermodiastaticus |
? |
- |
? |
| 3.2.1.59 | alpha-1,3-glucan + H2O |
Agn2p-his shows high specificity for (1,3)-alpha-glucosidic linkages |
Schizosaccharomyces pombe |
? |
- |
? |
| 3.2.1.59 | alpha-1,3-glucan + H2O |
prepared from sucrose using Streptococcus mutans ATCC700610 glucosyltransferase I |
Niallia circulans |
? |
- |
? |
| 3.2.1.59 | alpha-1,3-glucan + H2O |
the enzyme exhibits high specificity against alpha-1,3-glucan |
Streptomyces thermodiastaticus |
? |
- |
? |
| 3.2.1.59 | alpha-1,3-glucan + H2O |
100% activity |
Streptomyces thermodiastaticus HF3-3 |
? |
- |
? |
| 3.2.1.59 | alpha-1,3-glucan + H2O |
prepared from sucrose using Streptococcus mutans ATCC700610 glucosyltransferase I |
Niallia circulans KA-304 |
? |
- |
? |
| 3.2.1.59 | alpha-1,3-glucan + H2O |
the enzyme exhibits high specificity against alpha-1,3-glucan |
Streptomyces thermodiastaticus HF 3-3 |
? |
- |
? |
| 3.2.1.59 | alpha-1,3-glucan + H2O |
MutAp displays endo-hydrolytic activity. A tetrasaccharide is the minimal substrate for MutAp. The polysaccharide-binding domain in MutAp may be involved in processivity, either by partially disrupting the crystalline structure of (1-3)-alpha-glucan and thereby making it more accessible to hydrolysis, or by assisting in retention of (1-3)-alpha-glucan after each round of hydrolysis. The enzyme breaks an intrachain glycosidic linkage of (1-3)-alpha-glucan, and then continues its hydrolysis towards the non-reducing end by releasing beta-glucose residues in a processive manner. Acts by inversion of the anomeric configuration |
Trichoderma harzianum |
beta-D-glucose + ? |
- |
? |
| 3.2.1.59 | alpha-1,3-glucan pentasaccharide + H2O |
minimum size of substrate accepted |
Paenibacillus humicus |
alpha-1,3-glucan tetrasaccharide + D-glucose |
- |
? |
