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Literature summary for 3.2.1.52 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
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Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Aspergillus oryzae
-
-

Organism

Organism UniProt Comment Textmining
Aspergillus oryzae
-
-
-
Aspergillus oryzae CCF1066
-
-
-

Posttranslational Modification

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

Subunits

Subunits Comment Organism
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