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Literature summary for 3.4.22.16 extracted from

  • Guncar, G.; Podobnik, M.; Pungercar, J.; Strukelj, B.; Turk, V.; Turk, D.
    Crystal structure of porcine cathepsin H determined at 2.1 A resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function (1998), Structure, 6, 51-61.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
general and secondary structure, structure of active-site cleft, mechanistic conclusions drawn from crystallographic study, mini-chain attached to active-site cleft of enzyme body via disulfide bond, structural comparison reveals high similarity to actinidin Sus scrofa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Proteins + H2O Homo sapiens involved in tumor metastasis ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Sus scrofa
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification
-
Homo sapiens
proteolytic modification processing in three steps from proenzyme to endopeptidase intermediate to aminopeptidase, mini-chain formed from part of propeptide that is cleaved off Sus scrofa
side-chain modification
-
Homo sapiens
side-chain modification 2 N-glycosylation sites Sus scrofa

Reaction

Reaction Comment Organism Reaction ID
Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-/- bonds) as well as an endopeptidase mini-chain has definitive role in substrate-recognition, implications for enzyme function Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Proteins + H2O involved in tumor metastasis Homo sapiens ?
-
?