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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Reaction
Reaction on EC 3.4.22.16 - cathepsin H
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Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-/- bonds) as well as an endopeptidase
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
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Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-/- bonds) as well as an endopeptidase
mechanism: specific interactions of an anionic active site residue with the charged alpha-amino group of substrates cause transition state stabilization which proves the enzyme to act preferentially as an aminopeptidase
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Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-/- bonds) as well as an endopeptidase
mechanism: interactive catalytic-site system in which the nucleophilic character of the sulphur atom is maintained in acidic media
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Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-/- bonds) as well as an endopeptidase
number of possible subsites: three
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Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-/- bonds) as well as an endopeptidase
same catalytic mechanism as in papain and actinidin
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