3.2.1.166	glycoprotein	4 potential N-glycosylation sites	692954	
3.2.1.166	glycoprotein	enzyme HPSE contains 6 putative N-glycosylation sites, all residing on the 50 kDa subunit. N-linked GlcNAcs (corresponding to N-glycan trees trimmed by endoglycosidase (Endo)H during protein preparation) are found in the apo-HPSE structure at Asn162, Asn200, Asn217, Asn238 and Asn459. Additionally a core alpha1->6 linked fucose is located on the GlcNAc linked to Asn459. No noticeable density corresponding to GlcNAc is observed at the N-glycosylation site Asn178, suggesting this position may not be well N-glycosylated during baculoviral expression, or that N-GlcNAc here is not compatible with crystal packing	754873	
3.2.1.166	glycoprotein	glycosylation of Hpa1 is essential for solubility	690801	
3.2.1.166	glycoprotein	synthesized as an inactive 65000 Da glycoprotein that is cleaved at the N-terminus to generate the active enzyme	692520	
3.2.1.166	glycoprotein	the enzyme contains six N-glycosylation sites	731884	
3.2.1.166	glycoprotein	the enzyme contains six N-linked oligosaccharides	693320	
3.2.1.166	proteolytic modification	an endo-acting binding cleft is exposed by proteolytic activation of latent proenzyme, proHPSE. Enzyme HPSE is initially translated as a pre-proenzyme, containing a signal sequence spanning Met1-Ala35. Cleavage of this signal sequence by signal peptidase leaves an inactive 65 kDa proHPSE, which must undergo further processing for activity. Proteolytic removal by cathepsin L of a linker spanning Ser110-Gln157 liberates an N-terminal 8 kDa subunit and a C-terminal 50 kDa subunit, which remain associated as a non-covalent heterodimer in mature active HPSE29	754873	
3.2.1.166	proteolytic modification	heparanase is initially translated as a preproenzyme containing a signal sequence spanning Met1-Ala35. Cleavage of this signal sequence by signal peptidase yields an inactive 65-kDa pro-heparanase, which must undergo further processing for activity. Proteolytic removal by cathepsin L of a linker spanning Ser110-Gln157 liberates an N-terminal 8-kDa subunit and a C-terminal 50-kDa subunit, which remain associated as a noncovalent heterodimer in mature active heparanase. Processing of heparanase is mediated by syndecan 1 cytoplasmic domain and involves syntenin and alpha-actinin. Heparanase uptake is regarded a pre-requisite for the delivery of latent 65 kDa heparanase to lysosomes and its subsequent proteolytic processing and activation into 8 and 50 kDa protein subunits	753404	
3.2.1.166	proteolytic modification	heparanase-1 is synthesized as an inactive precursor of about 65000 Da that subsequently undergoes proteolytic cleavage, yielding 8000 Da and 50000 Da protein subunits that heterodimerize to form the active enzyme. The protein contains a putative N-terminal signal peptide (Met1-Ala35) and a C-terminal hydrophobic region (Pro515-Ile534)	693320	
3.2.1.166	proteolytic modification	Hpa1 protein is initially synthesized as an inactive 65000 Da proenzyme and subsequently activated by proteolytic cleavage to generate an active heterodimer of 8000 Da and 50000 Da polypeptides	690801