|
Enzyme Name | UniProtKB | KEGG |
---|
| O46427 |
---|
Protein name | Cathepsin H | cathepsin Hcathepsin B3benzoylarginine-naphthylamide (BANA) hydrolase (obsolete)cathepsin Ba, aleurainN-benzoylarginine-beta-naphthylamide hydrolase |
---|
Synonyms | EC 3.4.22.16 |
---|
Contains | Cathepsin H mini chainCathepsin H heavy chainCathepsin H light chain |
---|
RefSeq | NP_999094.1 (Protein) NM_213929.2 (DNA/RNA sequence)
|
---|
MEROPS | C01.040 (Cysteine)
|
---|
Pfam | PF08246 (Inhibitor_I29) PF00112 (Peptidase_C1) [Graphical view]
|
---|
UniProtKB:Accession Number | O46427 |
---|
Entry name | CATH_PIG |
---|
Activity | Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-|-Xaa bonds) as well as an endopeptidase. |
---|
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. |
---|
Subcellular location | Lysosome. |
---|
Cofactor |
|
---|
Compound table: links to PDB-related databases & PoSSuM |
---|
| Substrates | Products |
---|
KEGG-id | C00017 | C00012 | C00001 | C00017 | C00012 |
---|
Compound | Protein | Peptide | H2O | Protein | Peptide |
---|
Type | peptide/protein | peptide/protein | H2O | peptide/protein | peptide/protein |
---|
ChEBI |
|
| 15377
|
|
|
---|
PubChem |
|
| 962 22247451
|
|
|
---|
| | | | | | | | | | | | |
---|
8pchA |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound |
---|
1nb3A |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound |
---|
1nb3B |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound |
---|
1nb3C |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound |
---|
1nb3D |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound |
---|
1nb5A |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound |
---|
1nb5B |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound |
---|
1nb5C |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound |
---|
1nb5D |  |  |  |  |  |  |  | Unbound | Unbound | | Unbound | Unbound |
---|
References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
---|
[1] | p.52-54, p.55-57 |
|
references | [1] |
---|
Comments | X-ray crystallography (2.1 Angstroms) |
---|
PubMed ID | 9493267 |
---|
Journal | Structure |
---|
Year | 1998 |
---|
Volume | 6 |
---|
Pages | 51-61 |
---|
Authors | Guncar G, Podobnik M, Pungercar J, Strukelj B, Turk V, Turk D |
---|
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. |
---|
Related PDB | 8pch |
---|
Related UniProtKB | O46427 |
---|
[2] |
---|
PubMed ID | 12581647 |
---|
Journal | J Mol Biol |
---|
Year | 2003 |
---|
Volume | 326 |
---|
Pages | 875-85 |
---|
Authors | Jenko S, Dolenc I, Guncar G, Dobersek A, Podobnik M, Turk D |
---|
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. |
---|
Related PDB | 1nb3,1nb5 |
---|
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.
|
created | updated |
---|
2002-07-04 | 2009-02-26 |
|
|