EzCatDB: S00446
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DB codeS00446
RLCP classification1.13.30000.44 : Hydrolysis
CATH domainDomain 13.90.70.10 : Cathepsin B; Chain ACatalytic domain
E.C.3.4.22.6

CATH domainRelated DB codes (homologues)
3.90.70.10 : Cathepsin B; Chain AS00444,S00445,S00447,S00448,S00449,S00450,S00451,S00518

Enzyme Name
UniProtKBKEGG

P14080
Protein nameChymopapainchymopapain
chymopapain A
chymopapain B
chymopapain S
SynonymsEC 3.4.22.6
Papaya proteinase II
PPII
PfamPF08246 (Inhibitor_I29)
PF00112 (Peptidase_C1)
[Graphical view]


UniProtKB:Accession NumberP14080
Entry namePAPA2_CARPA
ActivitySpecificity similar to that of papain.
Subunit
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

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

15377


PubChem

962
22247451


             
1yalAUnboundUnbound UnboundUnbound

Active-site residues
pdbCatalytic residuesModified residues
          
1yalAGLN 19;HIS 159;ASN 179
SCH 25 (methylated CYS)

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


references
[1]
PubMed ID8010964
JournalBiochem J
Year1994
Volume300
Pages805-20
AuthorsThomas MP, Topham CM, Kowlessur D, Mellor GW, Thomas EW, Whitford D, Brocklehurst K
TitleStructure of chymopapain M the late-eluted chymopapain deduced by comparative modelling techniques and active-centre characteristics determined by pH-dependent kinetics of catalysis and reactions with time-dependent inhibitors: the Cys-25/His-159 ion-pair is insufficient for catalytic competence in both chymopapain M and papain.
[2]
CommentsX-ray crystallography (1.7 Angstroms)
PubMed ID8973203
JournalBiochemistry
Year1996
Volume35
Pages16292-8
AuthorsMaes D, Bouckaert J, Poortmans F, Wyns L, Looze Y
TitleStructure of chymopapain at 1.7 A resolution.
Related PDB1yal

comments
This enzyme belongs to the peptidase family-C1.
The paper [2] annotated the catalytic residues as Cys25, His159, and Asn179. Moreover, the active site can be superimposed onto other cysteine protease, such as cathepsin B, which suggests that Gln19 might form an oxyanion hole together with mainchan amide of Cys25.

createdupdated
2002-07-012009-02-26


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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)
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