Crystal structure of native beta-N-acetylhexosaminidase isolated from Aspergillus oryzae

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

glycosylated, proteolytically activated enzyme isolated from natural source; consists of a dimer of two catalytic cores and two associated propeptides. Chain A is a propeptide released during proteolytic activation and remains associated with chain B. Chains A and B form a monomer.

1 M ammonium sulfate, 20% PEG 3350 and 100 mM HEPES pH 8.0

Ministry of Education, Youth and Sports of the Czech Republic

projects LG14009 and LM2015043 CIISB for CMS BIOCEV

Chemical crosslinking combined with mass spectrometry was used to corroborate the crystal structure

Size-exclusion chromatography confirmed the dimeric assembly

U VALUES : WITH TLS ADDED HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

Glycosylation, Propeptide, Carbohydrate Biotechnology, HYDROLASE