EzCatDB: D00480
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DB codeD00480
RLCP classification1.13.10900.463 : Hydrolysis
CATH domainDomain 13.10.170.10 : Elastase; domain 1Catalytic domain
Domain 21.10.390.10 : Neutral Protease; domain 2Catalytic domain
E.C.3.4.24.29

CATH domainRelated DB codes (homologues)
1.10.390.10 : Neutral Protease; domain 2D00233,D00234,D00235
3.10.170.10 : Elastase; domain 1D00233,D00234,D00235

Enzyme Name
UniProtKBKEGG

P81177
Protein nameZinc metalloproteinase aureolysinaureolysin
Staphylococcus aureus neutral proteinase
Staphylococcus aureus neutral protease
SynonymsEC 3.4.24.29
Staphylococcus aureus neutral proteinase
MEROPSM04.009 (Metallo)
PfamPF07504 (FTP)
PF03413 (PepSY)
PF01447 (Peptidase_M4)
PF02868 (Peptidase_M4_C)
[Graphical view]


UniProtKB:Accession NumberP81177
Entry nameAURE_STAAU
ActivityCleavage 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.
Subunit
Subcellular location
CofactorBinds 3 calcium ions per subunit.,Binds 1 zinc ion per subunit.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProductsintermediates
KEGG-idC00038C00017C00012C00001C00017C00012
CompoundZincProteinPeptideH2OProteinPeptide
Typeheavy metalpeptide/proteinpeptide/proteinH2Opeptide/proteinpeptide/protein
ChEBI29105


15377



PubChem32051


962
22247451



               
1bqbA01Bound:_ZNUnboundUnbound UnboundUnboundUnbound
1bqbA02UnboundUnboundUnbound UnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P81177
pdbCatalytic residuesCofactor-binding residuesMain-chain involved in catalysis
           
1bqbA01ASN 114;GLU 145
HIS 144;HIS 148(Zinc binding)
ALA 115
1bqbA02TYR 159;HIS 228
GLU 168(Zinc binding)
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]p.1187-1189
[4]p.278-279

references
[1]
PubMed ID2512988
JournalBiochim Biophys Acta
Year1989
Volume993
Pages301-4
AuthorsPotempa J, Porwit-Bobr Z, Travis J
TitleStabilization vs. degradation of Staphylococcus aureus metalloproteinase.
[2]
CommentsPROTEIN SEQUENCE OF 210-509, AND X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS).
PubMed ID9753696
JournalStructure
Year1998
Volume6
Pages1185-93
AuthorsBanbula A, Potempa J, Travis J, Fernandez-Catalan C, Mann K, Huber R, Bode W, Medrano F
TitleAmino-acid sequence and three-dimensional structure of the Staphylococcus aureus metalloproteinase at 1.72 A resolution
Related PDB1bqb
Related UniProtKBP81177
[3]
PubMed ID10639475
JournalInfect Immun
Year2000
Volume68
Pages973-6
AuthorsSabat A, Kosowska K, Poulsen K, Kasprowicz A, Sekowska A, van Den Burg B, Travis J, Potempa J
TitleTwo allelic forms of the aureolysin gene (aur) within Staphylococcus aureus.
[4]
PubMed ID11831461
JournalBiometals
Year2001
Volume14
Pages271-313
AuthorsAuld DS
TitleZinc coordination sphere in biochemical zinc sites.
[5]
PubMed ID15740737
JournalJ Mol Biol
Year2005
Volume347
Pages231-41
AuthorsNovotny M, Kleywegt GJ
TitleA survey of left-handed helices in protein structures.

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.

createdupdated
2005-04-012009-02-26


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