Literature summary for 3.4.22.16 extracted from

Nishimura, Y.; Amano, J.; Sato, H.; Tsuji, H.; Kato, K.
Biosynthesis of lysosomal cathepsins B and H in cultures rat hepatocytes (1988), Arch. Biochem. Biophys., 262, 159-170.

Search for more literature for 3.4.22.16

General Stability

General Stability	Organism
effects of endoglycosidase H on proenzyme stability	Rattus norvegicus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
lysosome	biosynthesis in endoplasmic reticulum, proteolytic cleavage of proenzyme during translocation to lysosomes	Rattus norvegicus	5764	-

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
17000	-	1 * 17000, 1 * 5000, gel filtration after reduction	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	time-course of synthesis and posttranslational processing: proforms of MW 41000 are converted to single-chain cathepsin of MW 28000 within 1 h of translation	Rattus norvegicus
side-chain modification	high-mannose oligosaccharide, one N-glycosylation site per molecule	Rattus norvegicus

Source Tissue

Source Tissue	Comment	Organism	Textmining
hepatocyte	cultured	Rattus norvegicus	-

Subunits

Subunits	Comment	Organism
dimer	1 * 17000, 1 * 5000, gel filtration after reduction	Rattus norvegicus

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)