3.4.22.16: cathepsin H
This is an abbreviated version!
For detailed information about cathepsin H, go to the full flat file.
Reaction
Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-/- bonds) as well as an endopeptidase =
Synonyms
aleurain, aleuron thiol protease, alpha-N-benzoyl-arginine 2-naphthylamide hydrolase, alpha-N-benzoylarginine-beta-naphthylamide hydrolase, Cat H, CatB3, CatH, cathepsin B3, cathepsin Ba, cathepsin H, cathepsin H-like cysteine proteinase, CTSH, procathepsin H
ECTree
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Posttranslational Modification
Posttranslational Modification on EC 3.4.22.16 - cathepsin H
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glycoprotein
proteolytic modification
side-chain modification
glycoprotein
the enzyme harbors two glycosylation sites, Asn79P on the mini-chain of the prodomain and Asn115 on the mature domain. No glycan is built for Asn79P in cathepsin H due to poor electron density, although it is glycosylated
glycoprotein
the deduced amino acid sequence has three potential N-glycosylation sites at the Asn96, Asn223 and Asn267 residues
proteolytic modification
-
mutant lacking the mini chain, autocatalytic processing at pH 5.0, 37°C, processing is accelerated in presence of 0.025 mg/ml of dextran, prolonged activation results in both cases in decrease of enzyme acivtiy
proteolytic modification
propeptide-binding region of enzyme is structurally rearranged during maturation processing and mini-chain formation, which impairs the effective recognition of mature enzyme by its propeptide
proteolytic modification
the enzyme is synthesized as an inactive proenzyme, the N-terminal prodomain (Ala1P-Pro93P) is cleaved off for maturation, a C-terminal mature domain (Tyr1-Val220) with a disulfide bridge between Cys212 and the mini-chain Cys80P remains. Procathepsin H is not autoactivated but can be transactivated by cathepsin L. The prodomain of procathepsin H has an N-terminal helical subdomain (Ala1P-Ser75P) and an extended portion (Glu76P-Pro93P) that links the helical subdomain to Tyr1 of the mature domain
proteolytic modification
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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
proteolytic modification
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processing in three steps from proenzyme to endopeptidase intermediate to aminopeptidase, mini-chain formed from part of propeptide that is cleaved off
side-chain modification
-
structural studies of carbohydrate moieties: 1 Asn-115-linked high-mannose type oligosaccharide per molecule, structure reported
side-chain modification
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glycosylated residues located on rather loose surface loop
side-chain modification
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high-mannose oligosaccharide, one N-glycosylation site per molecule
side-chain modification
-
2 mol of glucosamine and 5 mol of mannose per mol enzyme