EzCatDB: S00448
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DB codeS00448
RLCP classification1.13.30000.44 : Hydrolysis
CATH domainDomain 13.90.70.10 : Cathepsin B; Chain ACatalytic domain
E.C.3.4.22.16
CSA8pch

CATH domainRelated DB codes (homologues)
3.90.70.10 : Cathepsin B; Chain AS00444,S00445,S00447,S00449,S00450,S00451,S00446,S00518

Enzyme Name
UniProtKBKEGG

O46427
Protein nameCathepsin Hcathepsin H
cathepsin B3
benzoylarginine-naphthylamide (BANA) hydrolase (obsolete)
cathepsin Ba, aleurain
N-benzoylarginine-beta-naphthylamide hydrolase
SynonymsEC 3.4.22.16
ContainsCathepsin H mini chain
Cathepsin H heavy chain
Cathepsin H light chain
RefSeqNP_999094.1 (Protein)
NM_213929.2 (DNA/RNA sequence)
MEROPSC01.040 (Cysteine)
PfamPF08246 (Inhibitor_I29)
PF00112 (Peptidase_C1)
[Graphical view]


UniProtKB:Accession NumberO46427
Entry nameCATH_PIG
ActivityHydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-|-Xaa bonds) as well as an endopeptidase.
SubunitComposed 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 locationLysosome.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00017C00012C00001C00017C00012
CompoundProteinPeptideH2OProteinPeptide
Typepeptide/proteinpeptide/proteinH2Opeptide/proteinpeptide/protein
ChEBI

15377


PubChem

22247451
962


             
8pchAUnboundUnbound UnboundUnbound
1nb3AUnboundUnbound UnboundUnbound
1nb3BUnboundUnbound UnboundUnbound
1nb3CUnboundUnbound UnboundUnbound
1nb3DUnboundUnbound UnboundUnbound
1nb5AUnboundUnbound UnboundUnbound
1nb5BUnboundUnbound UnboundUnbound
1nb5CUnboundUnbound UnboundUnbound
1nb5DUnboundUnbound UnboundUnbound

Active-site residues
resource
Swiss-prot;O46427 & literature [1]
pdbCatalytic residues
         
8pchAGLN 19;CYS 25;ASN 158;HIS 159;ASN 175
1nb3AGLN 19;CYS 25;ASN 158;HIS 159;ASN 175
1nb3BGLN 19;CYS 25;ASN 158;HIS 159;ASN 175
1nb3CGLN 19;CYS 25;ASN 158;HIS 159;ASN 175
1nb3DGLN 19;CYS 25;ASN 158;HIS 159;ASN 175
1nb5AGLN 19;CYS 25;ASN 158;HIS 159;ASN 175
1nb5BGLN 19;CYS 25;ASN 158;HIS 159;ASN 175
1nb5CGLN 19;CYS 25;ASN 158;HIS 159;ASN 175
1nb5DGLN 19;CYS 25;ASN 158;HIS 159;ASN 175

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]p.52-54, p.55-57

references
[1]
CommentsX-ray crystallography (2.1 Angstroms)
PubMed ID9493267
JournalStructure
Year1998
Volume6
Pages51-61
AuthorsGuncar G, Podobnik M, Pungercar J, Strukelj B, Turk V, Turk D
TitleCrystal 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 PDB8pch
Related UniProtKBO46427
[2]
PubMed ID12581647
JournalJ Mol Biol
Year2003
Volume326
Pages875-85
AuthorsJenko S, Dolenc I, Guncar G, Dobersek A, Podobnik M, Turk D
TitleCrystal 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 PDB1nb3,1nb5

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.

createdupdated
2002-07-042009-02-26
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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