EC Number | Cloned (Comment) | Organism |
---|---|---|
3.2.1.57 | recombinant IPU produced by Pichia pastoris | Aspergillus niger |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.2.1.57 | for crystallization, the enzyme is treated with endoglycosidase Hf, by hanging drop vapor-diffusion method, unliganded and isopanose-complexed forms of IPU, both solved at 1.7 A resolution. Unliganded IPU belongs to space group P212121, which contains two molecules and 1273 water molecules in an asymmetric unit. IPU is composed of domains N and C joined by a short linker, with electron density maps for 11 or 12 N-acetylglucosamine residues per molecule. Domain N consists of 13 beta-strands and forms a beta-sandwich. Domain C, where the active site is located, forms a right-handed beta-helix. Overall conformation of IPU in complex with isopanose is essentially identical with that of unliganded IPU | Aspergillus niger |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.57 | Aspergillus niger | O00105 | ATCC9642 | - |
3.2.1.57 | Aspergillus niger ATCC 9642 | O00105 | ATCC9642 | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.2.1.57 | - |
Aspergillus niger |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.57 | pullulan + H2O | Asp353, Asp372 and Asp373 are the catalytic residues of IPU | Aspergillus niger | isopanose + ? | - |
? | |
3.2.1.57 | pullulan + H2O | Asp353, Asp372 and Asp373 are the catalytic residues of IPU | Aspergillus niger ATCC 9642 | isopanose + ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.57 | IPU | - |
Aspergillus niger |
3.2.1.57 | pullulan 4-glucanohydrolase | - |
Aspergillus niger |