Literature summary for 3.2.1.52 extracted from

Plihal, O.; Sklenar, J.; Hofbauerova, K.; Novak, P.; Man, P.; Pompach, P.; Kavan, D.; Ryslava, H.; Weignerova, L.; Charvatova-Pisvejcova, A.; Kren, V.; Bezouska, K.
Large propeptides of fungal beta-N-acetylhexosaminidases are novel enzyme regulators that must be intracellularly processed to control activity, dimerization, and secretion into the extracellular environment (2007), Biochemistry, 46, 2719-2734.

Search for more literature for 3.2.1.52

Organism

Organism	UniProt	Comment	Textmining
Aspergillus oryzae	Q8J2T0	-	-
Aspergillus oryzae CCF 1066	Q8J2T0	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	-	Aspergillus oryzae
proteolytic modification	the enzyme precursor is processed early in the biosynthesis, shortly after the addition of N-glycans through the action of a dibasic peptidase, cleaving both before and after the dibasic sequence. Binding of the released propeptide to the catalytic subunit of Hex is essential for its activation. The fungus is able to actively regulate the concentration of the processed propeptide in endoplasmic reticulum and thus the specific activity of the produced Hex. This regulatory mechanism enables the control of the catalytic activity and architecture of the secreted enzyme according to the needs of the producing cell at various stages of its growth cycle	Aspergillus oryzae

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)