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)
3.10.170.10 : Elastase; domain 1 D00233 D00234 D00235
1.10.390.10 : Neutral Protease; domain 2 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
15377
PubChem 32051
22247451
962
1bqbA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_ZN Unbound Unbound Unbound Unbound Unbound
1bqbA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain 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 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 114;GLU 145 HIS 144;HIS 148(Zinc binding) ALA 115
1bqbA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain 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. degradation of Staphylococcus aureus metalloproteinase.
Related PDB
Related UniProtKB
[2]
Resource
Comments PROTEIN SEQUENCE OF 210-509, AND X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS).
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, they are not involved in catalysis.
According to the literature [4], Glu145 might act as a general acid-base. This residue is bound to the water molecule, which is bound to the catalytic zinc ion.
As the active site is the same as the thermolysin (D00234 in EzCatDB), the catalytic mechanism must be the same.

Created Updated
2005-04-01 2009-02-26