DB code: S00448

RLCP classification 1.13.30000.44 : Hydrolysis
CATH domain 3.90.70.10 : Cathepsin B; Chain A Catalytic domain
E.C. 3.4.22.16
CSA 8pch
M-CSA 8pch
MACiE

CATH domain Related DB codes (homologues)
3.90.70.10 : Cathepsin B; Chain A S00444 S00445 S00447 S00449 S00450 S00451 S00446 S00518

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Contains RefSeq MEROPS Pfam
O46427 Cathepsin H
EC 3.4.22.16
Cathepsin H mini chain
Cathepsin H heavy chain
Cathepsin H light chain
NP_999094.1 (Protein)
NM_213929.2 (DNA/RNA sequence)
C01.040 (Cysteine)
PF08246 (Inhibitor_I29)
PF00112 (Peptidase_C1)
[Graphical View]

KEGG enzyme name
cathepsin H
cathepsin B3
benzoylarginine-naphthylamide (BANA) hydrolase (obsolete)
cathepsin Ba, aleurain
N-benzoylarginine-beta-naphthylamide hydrolase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
O46427 CATH_PIG Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-|-Xaa bonds) as well as an endopeptidase. 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. Lysosome.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C00017 C00012 C00001 C00017 C00012
E.C.
Compound Protein Peptide H2O Protein Peptide
Type peptide/protein peptide/protein H2O peptide/protein peptide/protein
ChEBI 15377
PubChem 962
22247451
8pchA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1nb3A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1nb3B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1nb3C Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1nb3D Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1nb5A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1nb5B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1nb5C Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1nb5D Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;O46427 & literature [1]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
8pchA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLN 19;CYS 25;ASN 158;HIS 159;ASN 175
1nb3A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLN 19;CYS 25;ASN 158;HIS 159;ASN 175
1nb3B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLN 19;CYS 25;ASN 158;HIS 159;ASN 175
1nb3C Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLN 19;CYS 25;ASN 158;HIS 159;ASN 175
1nb3D Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLN 19;CYS 25;ASN 158;HIS 159;ASN 175
1nb5A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLN 19;CYS 25;ASN 158;HIS 159;ASN 175
1nb5B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLN 19;CYS 25;ASN 158;HIS 159;ASN 175
1nb5C Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLN 19;CYS 25;ASN 158;HIS 159;ASN 175
1nb5D Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLN 19;CYS 25;ASN 158;HIS 159;ASN 175

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
p.52-54, p.55-57

References
[1]
Resource
Comments X-ray crystallography (2.1 Angstroms)
Medline ID
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]
Resource
Comments
Medline ID
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
Related UniProtKB

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