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Literature summary 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)

EC Number Crystallization (Comment) Organism
3.4.22.16 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)

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

Organism

EC Number Organism UniProt Comment Textmining
3.4.22.16 Homo sapiens
-
-
-
3.4.22.16 Sus scrofa
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.22.16 proteolytic modification
-
 Homo sapiens
3.4.22.16 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
3.4.22.16 side-chain modification
-
 Homo sapiens
3.4.22.16 side-chain modification 2 N-glycosylation sites Sus scrofa

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.22.16 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
a

Substrates and Products (Substrate)

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