Crystal structure of native β‐N‐acetylhexosaminidase isolated from Aspergillus oryzae sheds light onto its substrate specificity, high stability, and regulation by propeptide

We present the first crystal structure of a native fungal β‐N‐acetylhexosaminidase, isolated from Aspergillus oryzae. This chitobiose‐processing enzyme adopts a tight dimeric assembly further stabilized by a chain‐swapped propeptide. The propeptide possesses unique O‐glycosylation involved in enzyme dimerization. Loops and the propeptide of the second monomer in the dimer affect active pocket shape and enzyme specificity.

Source: FEBS Journal - December 30, 2017 Category: Research Authors: Jana Škerlová, Jan Bláha, Petr Pachl, Kateřina Hofbauerová, Zdeněk Kukačka, Petr Man, Petr Pompach, Petr Novák, Zbyszek Otwinowski, Jiří Brynda, Ondřej Vaněk, Pavlína Řezáčová Tags: Original Article Source Type: research