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Literature summary for 3.2.1.41 extracted from
- Structure of a pullulanase from Bacillus acidopullulyticus (2009), Proteins, 76, 516-519.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| X-ray diffraction structure determination and analysis at 1.7 A resolution | Bacillus acidopullulyticus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus acidopullulyticus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the BaPul13A active centre in which hydrolysis of alpha-1,6 linkages occurs with net retention of anomeric configuration, via a covalent glycosyl-enzyme intermediate. Complete starch hydrolysis requires a consortium of enzymes including endo-amylases, glucoamylases and alpha-glucosidases as well as diverse alpha-1,6 cleaving enzymes including pullulanases | Bacillus acidopullulyticus | ? | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | enzyme modular architecture and domain structure, it contains CBM48 and CBM41 domains, and X25 and X45 domains, overview | Bacillus acidopullulyticus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| BaPul13A | - |
Bacillus acidopullulyticus |
| More | the enzyme belongs to the glycosidase family GH13 | Bacillus acidopullulyticus |
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