Literature summary for 3.2.1.7 extracted from

Pouyez, J.; Mayard, A.; Vandamme, A.M.; Roussel, G.; Perpete, E.A.; Wouters, J.; Housen, I.; Michaux, C.
First crystal structure of an endo-inulinase, INU2, from Aspergillus ficuum: discovery of an extra-pocket in the catalytic domain responsible for its endo-activity (2012), Biochimie, 94, 2423-2430.

Crystallization (Commentary)

Crystallization (Comment)	Organism
to 1.5 A resolution. Structural arrangement shows a N-terminal 5fold beta-propeller catalytic domain with four beta-sheets and a C-terminal beta-sandwich domain organized in two beta-sheets with five beta-strands. Comparison with other GH32 enzymes reveals the presence of an extra pocket in the isoform INU2 catalytic site, formed by two loops and the conserved motif W-M(I)-N-D(E)-P-N-G. This cavity explains the endo-activity of the enzyme, the critical role of residue Trp40 and particularly the cleavage at the third unit of the inulin(-like) substrates	Aspergillus ficuum

Crystallization (Comment)

Organism

to 1.5 A resolution. Structural arrangement shows a N-terminal 5fold beta-propeller catalytic domain with four beta-sheets and a C-terminal beta-sandwich domain organized in two beta-sheets with five beta-strands. Comparison with other GH32 enzymes reveals the presence of an extra pocket in the isoform INU2 catalytic site, formed by two loops and the conserved motif W-M(I)-N-D(E)-P-N-G. This cavity explains the endo-activity of the enzyme, the critical role of residue Trp40 and particularly the cleavage at the third unit of the inulin(-like) substrates

Aspergillus ficuum

Organism

Organism	UniProt	Comment	Textmining
Aspergillus ficuum	O94220	-	-

Synonyms

Synonyms	Comment	Organism
Inu2	-	Aspergillus ficuum

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Release 2023.1 (January 2023)