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| Enzyme Name | | Swiss-prot | KEGG |
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| O46427 |
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| Protein name | Cathepsin H | cathepsin Hcathepsin B3benzoylarginine-naphthylamide (BANA) hydrolase (obsolete)cathepsin Ba, aleurainN-benzoylarginine-beta-naphthylamide hydrolase |
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| Synonyms | EC 3.4.22.16 |
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| Contains | Cathepsin H mini chainCathepsin H heavy chainCathepsin H light chain |
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| Swiss-prot:Accession Number | O46427 |
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| Entry name | CATH_PIG |
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| Activity | Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-|-Xaa bonds) as well as an endopeptidase. |
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| Subunit | Composed of cathepsin H and mini chain, disulfide-linked. Cathepsin H may be split into heavy and light chain. All chains are held together by disulfide bonds. |
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| Subcellular location | Lysosome. |
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| Cofactor |
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| Substrates | Products |
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| KEGG-id | C00017 | C00012 | C00001 | C00017 | C00012 |
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| Compound | Protein | Peptide | H2O | Protein | Peptide |
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| Type | peptide/protein | peptide/protein | H2O | peptide/protein | peptide/protein |
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| 8pchA |  | Unbound | Unbound |
| Unbound | Unbound |
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| 1nb3A | | Unbound | Unbound |
| Unbound | Unbound |
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| 1nb3B | | Unbound | Unbound |
| Unbound | Unbound |
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| 1nb3C | | Unbound | Unbound |
| Unbound | Unbound |
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| 1nb3D | | Unbound | Unbound |
| Unbound | Unbound |
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| 1nb5A | | Unbound | Unbound |
| Unbound | Unbound |
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| 1nb5B | | Unbound | Unbound |
| Unbound | Unbound |
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| 1nb5C | | Unbound | Unbound |
| Unbound | Unbound |
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| 1nb5D | | Unbound | Unbound |
| Unbound | Unbound |
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| References for Catalytic Mechanism | | References | Sections | No. of steps in catalysis |
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| [1] | p.52-54, p.55-57 |
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| references | | [1] |
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| Comments | X-ray crystallography (2.1 Angstroms) |
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| PubMed ID | 9493267 |
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| Journal | Structure |
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| Year | 1998 |
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| Volume | 6 |
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| Pages | 51-61 |
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| Authors | Guncar G, Podobnik M, Pungercar J, Strukelj B, Turk V, Turk D |
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| Title | 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. |
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| Related PDB | 8pch |
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| Related Swiss-prot | O46427 |
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| [2] |
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| PubMed ID | 12581647 |
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| Journal | J Mol Biol |
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| Year | 2003 |
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| Volume | 326 |
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| Pages | 875-85 |
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| Authors | Jenko S, Dolenc I, Guncar G, Dobersek A, Podobnik M, Turk D |
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| Title | Crystal structure of Stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases. |
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| Related PDB | 1nb3,1nb5 |
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| comments | This enzyme belongs to the peptidase family-C1.
Although this enzyme has got a set of active-site residues (Gln19, Cys25, His159 & Asn175), as observed in other homologous enzymes, such as cathepsin B, their relative positions are slightly different from those of other homologous enzymes (see [1]). Firstly, the position of His159 is slightly distant from the catalytic Cys25, and does not form a thiolate-imidazolium ion pair with the residue. Secondly, His159 interacts with Asn158, instead of the conserved Asn175. This ovserved structure might be an inactive form of the enzyme.
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| created | updated |
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| 2002-07-04 | 2009-02-26 |
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