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Literature summary for 3.2.1.57 extracted from

  • Mizuno, M.; Koide, A.; Yamamura, A.; Akeboshi, H.; Yoshida, H.; Kamitori, S.; Sakano, Y.; Nishikawa, A.; Tonozuka, T.
    Crystal structure of Aspergillus niger isopullulanase, a member of glycoside hydrolase family 49 (2008), J. Mol. Biol., 376, 210-220.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant IPU produced by Pichia pastoris Aspergillus niger

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Organism

Organism UniProt Comment Textmining
Aspergillus niger O00105 ATCC9642
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Aspergillus niger ATCC 9642 O00105 ATCC9642
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Purification (Commentary)

Purification (Comment) Organism
-
Aspergillus niger

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pullulan + H2O Asp353, Asp372 and Asp373 are the catalytic residues of IPU Aspergillus niger isopanose + ?
-
?
pullulan + H2O Asp353, Asp372 and Asp373 are the catalytic residues of IPU Aspergillus niger ATCC 9642 isopanose + ?
-
?

Synonyms

Synonyms Comment Organism
IPU
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Aspergillus niger
pullulan 4-glucanohydrolase
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Aspergillus niger