DB code: S00446
| RLCP classification | 1.13.30000.44 : Hydrolysis | |
|---|---|---|
| CATH domain | 3.90.70.10 : Cathepsin B; Chain A | Catalytic domain |
| E.C. | 3.4.22.6 | |
| CSA | ||
| M-CSA | ||
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 3.90.70.10 : Cathepsin B; Chain A | S00444 S00445 S00447 S00448 S00449 S00450 S00451 S00518 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | MEROPS | Pfam |
|---|---|---|---|---|
| P14080 |
Chymopapain
|
EC
3.4.22.6
Papaya proteinase II PPII |
I29.003
()
|
PF08246
(Inhibitor_I29)
PF00112 (Peptidase_C1) [Graphical View] |
| KEGG enzyme name |
|---|
|
chymopapain
chymopapain A chymopapain B chymopapain S |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P14080 | PAPA2_CARPA | Specificity similar to that of papain. |
| 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 15377 |
||||||||||
| PubChem |
22247451 962 22247451 962 |
||||||||||
| 1yalA |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1yalA |
|
|
|
|
|
GLN 19;HIS 159;ASN 179 | SCH 25 (methylated CYS) | |||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[2]
|
||
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8010964 |
| Journal | Biochem J |
| Year | 1994 |
| Volume | 300 |
| Pages | 805-20 |
| Authors | Thomas MP, Topham CM, Kowlessur D, Mellor GW, Thomas EW, Whitford D, Brocklehurst K |
| Title | Structure 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. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | X-ray crystallography (1.7 Angstroms) |
| Medline ID | |
| PubMed ID | 8973203 |
| Journal | Biochemistry |
| Year | 1996 |
| Volume | 35 |
| Pages | 16292-8 |
| Authors | Maes D, Bouckaert J, Poortmans F, Wyns L, Looze Y |
| Title | Structure of chymopapain at 1.7 A resolution. |
| Related PDB | 1yal |
| Related UniProtKB | |
| Comments |
|---|
|
This enzyme belongs to the peptidase family-C1.
The paper [2] annotated the catalytic residues as Cys25, |
| Created | Updated |
|---|---|
| 2002-07-01 | 2009-02-26 |