DB code: S00444
| RLCP classification | 1.13.30000.44 : Hydrolysis | |
|---|---|---|
| CATH domain | 3.90.70.10 : Cathepsin B; Chain A | Catalytic domain |
| E.C. | 3.4.18.1 | |
| CSA | ||
| M-CSA | ||
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 3.90.70.10 : Cathepsin B; Chain A | S00445 S00447 S00448 S00449 S00450 S00451 S00446 S00518 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | MEROPS | Pfam |
|---|---|---|---|---|---|
| Q9UBR2 |
Cathepsin Z
|
EC
3.4.18.1
Cathepsin X Cathepsin P |
NP_001327.2
(Protein)
NM_001336.3 (DNA/RNA sequence) |
C01.013
(Cysteine)
|
PF00112
(Peptidase_C1)
[Graphical View] |
| KEGG enzyme name |
|---|
|
cathepsin X
cathepsin B2 cysteine-type carboxypeptidase cathepsin IV cathepsin Z acid carboxypeptidase lysosomal carboxypeptidase B |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| Q9UBR2 | CATZ_HUMAN | Release of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity. | Lysosome. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|
| Compound table | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| Substrates | Products | Intermediates | ||||||||
| KEGG-id | C00012 | C00001 | C00045 | C00012 | ||||||
| E.C. | ||||||||||
| Compound | Peptide | H2O | Amino acid | Peptide | ||||||
| Type | peptide/protein | H2O | amino acids | peptide/protein | ||||||
| ChEBI |
15377 15377 |
|||||||||
| PubChem |
22247451 962 22247451 962 |
|||||||||
| 1ef7A |
|
|
|
|
|
Unbound | Unbound | Unbound | ||
| 1ef7B |
|
|
|
|
|
Unbound | Unbound | Unbound | ||
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Swiss-prot;Q9UBR2 | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1ef7A |
|
|
|
|
|
GLN 22;CYS 31;HIS 180;ASN 200 | CYS 31 | |||
| 1ef7B |
|
|
|
|
|
GLN 22;CYS 31;HIS 180;ASN 200 | CYS 31 | |||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[2]
|
||
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9738465 |
| Journal | FEBS Lett |
| Year | 1998 |
| Volume | 434 |
| Pages | 135-9 |
| Authors | Nagler DK, Menard R |
| Title | Human cathepsin X: a novel cysteine protease of the papain family with a very short proregion and unique insertions. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10656802 |
| Journal | J Mol Biol |
| Year | 2000 |
| Volume | 295 |
| Pages | 939-51 |
| Authors | Sivaraman J, Nagler DK, Zhang R, Menard R, Cygler M |
| Title | Crystal structure of human procathepsin X: a cysteine protease with the proregion covalently linked to the active site cysteine. |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | X-ray crystallography (2.67 Angstroms) |
| Medline ID | |
| PubMed ID | 10745011 |
| Journal | Structure Fold Des |
| Year | 2000 |
| Volume | 8 |
| Pages | 305-13 |
| Authors | Guncar G, Klemencic I, Turk B, Turk V, Karaoglanovic-Carmona A, Juliano L, Turk D |
| Title | Crystal structure of cathepsin X: a flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease. |
| Related PDB | 1ef7 |
| Related UniProtKB | |
| Comments |
|---|
|
This enzyme belongs to the peptidase family-C1.
Accoriding to the literature [2], Cys31, |
| Created | Updated |
|---|---|
| 2002-07-01 | 2010-02-02 |