DB code: D00480
| RLCP classification | 1.13.10900.463 : Hydrolysis | |
|---|---|---|
| CATH domain | 3.10.170.10 : Elastase; domain 1 | Catalytic domain |
| 1.10.390.10 : Neutral Protease; domain 2 | Catalytic domain | |
| E.C. | 3.4.24.29 | |
| CSA | ||
| M-CSA | ||
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 1.10.390.10 : Neutral Protease; domain 2 | D00233 D00234 D00235 |
| 3.10.170.10 : Elastase; domain 1 | D00233 D00234 D00235 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | MEROPS | Pfam |
|---|---|---|---|---|
| P81177 |
Zinc metalloproteinase aureolysin
|
EC
3.4.24.29
Staphylococcus aureus neutral proteinase |
M04.009
(Metallo)
|
PF07504
(FTP)
PF03413 (PepSY) PF01447 (Peptidase_M4) PF02868 (Peptidase_M4_C) [Graphical View] |
| KEGG enzyme name |
|---|
|
aureolysin
Staphylococcus aureus neutral proteinase Staphylococcus aureus neutral protease |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P81177 | AURE_STAAU | Cleavage of insulin B chain with specificity similar to that of thermolysin, preferring hydrophobic P1'' residues. Activates the glutamyl endopeptidase (EC 3.4.21.19) of Staphylococcus aureus. | Binds 3 calcium ions per subunit. Binds 1 zinc ion per subunit. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|
| Compound table | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Cofactors | Substrates | Products | Intermediates | |||||||||
| KEGG-id | C00038 | C00017 | C00012 | C00001 | C00017 | C00012 | ||||||
| E.C. | ||||||||||||
| Compound | Zinc | Protein | Peptide | H2O | Protein | Peptide | ||||||
| Type | heavy metal | peptide/protein | peptide/protein | H2O | peptide/protein | peptide/protein | ||||||
| ChEBI |
29105 29105 |
15377 15377 |
||||||||||
| PubChem |
32051 32051 |
22247451 962 22247451 962 |
||||||||||
| 1bqbA01 |
|
|
|
|
|
Bound:_ZN | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1bqbA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Swiss-prot;P81177 | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1bqbA01 |
|
|
|
|
|
ASN 114;GLU 145 | HIS 144;HIS 148(Zinc binding) | ALA 115 | ||
| 1bqbA02 |
|
|
|
|
|
TYR 159;HIS 228 | GLU 168(Zinc binding) | |||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[2]
|
p.1187-1189 | |
|
[4]
|
p.278-279 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 2512988 |
| Journal | Biochim Biophys Acta |
| Year | 1989 |
| Volume | 993 |
| Pages | 301-4 |
| Authors | Potempa J, Porwit-Bobr Z, Travis J |
| Title |
Stabilization vs. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments |
PROTEIN SEQUENCE OF 210-509, |
| Medline ID | |
| PubMed ID | 9753696 |
| Journal | Structure |
| Year | 1998 |
| Volume | 6 |
| Pages | 1185-93 |
| Authors | Banbula A, Potempa J, Travis J, Fernandez-Catalan C, Mann K, Huber R, Bode W, Medrano F |
| Title | Amino-acid sequence and three-dimensional structure of the Staphylococcus aureus metalloproteinase at 1.72 A resolution |
| Related PDB | 1bqb |
| Related UniProtKB | P81177 |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10639475 |
| Journal | Infect Immun |
| Year | 2000 |
| Volume | 68 |
| Pages | 973-6 |
| Authors | Sabat A, Kosowska K, Poulsen K, Kasprowicz A, Sekowska A, van Den Burg B, Travis J, Potempa J |
| Title | Two allelic forms of the aureolysin gene (aur) within Staphylococcus aureus. |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11831461 |
| Journal | Biometals |
| Year | 2001 |
| Volume | 14 |
| Pages | 271-313 |
| Authors | Auld DS |
| Title | Zinc coordination sphere in biochemical zinc sites. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 15740737 |
| Journal | J Mol Biol |
| Year | 2005 |
| Volume | 347 |
| Pages | 231-41 |
| Authors | Novotny M, Kleywegt GJ |
| Title | A survey of left-handed helices in protein structures. |
| Related PDB | |
| Related UniProtKB | |
| Comments |
|---|
|
This enzyme belongs to the peptidase family-M4 (Thermolysin family).
Although this enzyme binds three calcium ions, According to the literature [4], As the active site is the same as the thermolysin (D00234 in EzCatDB), |
| Created | Updated |
|---|---|
| 2005-04-01 | 2009-02-26 |