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Literature summary extracted from

  • Ettrich, R.; Kopecky, V.; Hofbauerova, K.; Baumruk, V.; Novak, P.; Pompach, P.; Man, P.; Plihal, O.; Kuty, M.; Kulik, N.; Sklenar, J.; Ryslava, H.; Kren, V.; Bezouska, K.
    Structure of the dimeric N-glycosylated form of fungal beta-N-acetylhexosaminidase revealed by computer modeling, vibrational spectroscopy, and biochemical studies (2007), BMC Struct. Biol., 7, 32.
    View publication on PubMedView publication on EuropePMC

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.52 extracellular
-
 Aspergillus oryzae
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-

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.52 Aspergillus oryzae
-
-
-
3.2.1.52 Aspergillus oryzae CCF1066
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-
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Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.52 glycoprotein dimerization and N-glycosylation are the strategies of the enzyme for catalytic subunit stabilization Aspergillus oryzae

Subunits

EC Number Subunits Comment Organism
3.2.1.52 dimer dimerization appears to be a reversible process that is strictly pH dependent. Oligosaccharide moieties may also participate in the dimerization process. Dimerization and N-glycosylation are the strategies of the enzyme for catalytic subunit stabilization Aspergillus oryzae