EzCatDB: S00444
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DB codeS00444
RLCP classification1.13.30000.44 : Hydrolysis
CATH domainDomain 13.90.70.10 : Cathepsin B; Chain ACatalytic domain
E.C.3.4.18.1

CATH domainRelated DB codes (homologues)
3.90.70.10 : Cathepsin B; Chain AS00445,S00447,S00448,S00449,S00450,S00451,S00446,S00518

Enzyme Name
UniProtKBKEGG

Q9UBR2
Protein nameCathepsin Zcathepsin X
cathepsin B2
cysteine-type carboxypeptidase
cathepsin IV
cathepsin Z
acid carboxypeptidase
lysosomal carboxypeptidase B
SynonymsEC 3.4.18.1
Cathepsin X
Cathepsin P
RefSeqNP_001327.2 (Protein)
NM_001336.3 (DNA/RNA sequence)
MEROPSC01.013 (Cysteine)
PfamPF00112 (Peptidase_C1)
[Graphical view]


UniProtKB:Accession NumberQ9UBR2
Entry nameCATZ_HUMAN
ActivityRelease of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity.
Subunit
Subcellular locationLysosome.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00012C00001C00045C00012
CompoundPeptideH2OAmino acidPeptide
Typepeptide/proteinH2Oamino acidspeptide/protein
ChEBI
15377


PubChem
962
22247451


            
1ef7AUnbound UnboundUnbound
1ef7BUnbound UnboundUnbound

Active-site residues
resource
Swiss-prot;Q9UBR2
pdbCatalytic residuesMain-chain involved in catalysis
          
1ef7AGLN 22;CYS 31;HIS 180;ASN 200
CYS 31
1ef7BGLN 22;CYS 31;HIS 180;ASN 200
CYS 31

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]


references
[1]
PubMed ID9738465
JournalFEBS Lett
Year1998
Volume434
Pages135-9
AuthorsNagler DK, Menard R
TitleHuman cathepsin X: a novel cysteine protease of the papain family with a very short proregion and unique insertions.
[2]
PubMed ID10656802
JournalJ Mol Biol
Year2000
Volume295
Pages939-51
AuthorsSivaraman J, Nagler DK, Zhang R, Menard R, Cygler M
TitleCrystal structure of human procathepsin X: a cysteine protease with the proregion covalently linked to the active site cysteine.
[3]
CommentsX-ray crystallography (2.67 Angstroms)
PubMed ID10745011
JournalStructure Fold Des
Year2000
Volume8
Pages305-13
AuthorsGuncar G, Klemencic I, Turk B, Turk V, Karaoglanovic-Carmona A, Juliano L, Turk D
TitleCrystal structure of cathepsin X: a flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease.
Related PDB1ef7

comments
This enzyme belongs to the peptidase family-C1.
Accoriding to the literature [2], the active site is consisting of Cys31, His180, Asn200 and an oxyanion hole, which precedes the catalytic Cys31. Unlike other papain-like enzymes, three residues are inserted in the oxyanion hole region, and form a mini-loop that bends away from the active site. This paper mentioned that the oxyanion hole is formed by the sidechain of Gln and the mainchain amide group of Cys31.
Cys31, which is activated by His180, can act as a nucleophile.

createdupdated
2002-07-012010-02-02


Copyright: Nozomi Nagano, JST & CBRC-AIST
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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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