DB code: D00233

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. 3.4.24.26
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.10.170.10 : Elastase; domain 1 D00234 D00235 D00480
1.10.390.10 : Neutral Protease; domain 2 D00234 D00235 D00480

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq MEROPS Pfam
P14756 Pseudolysin
EC 3.4.24.26
Elastase
Neutral metalloproteinase
NP_252413.1 (Protein)
NC_002516.2 (DNA/RNA sequence)
M04.005 (Metallo)
PF07504 (FTP)
PF03413 (PepSY)
PF01447 (Peptidase_M4)
PF02868 (Peptidase_M4_C)
[Graphical View]

KEGG enzyme name
pseudolysin
Pseudomonas elastase
Pseudomonas aeruginosa neutral metalloproteinase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P14756 ELAS_PSEAE Hydrolysis of proteins including elastin, collagen types III and IV, fibronectin and immunoglobulin A, generally with bulky hydrophobic group at P1''. Insulin B chain cleavage pattern identical to that of thermolysin, but specificity differs in other respects. Secreted. Binds 1 calcium ion per subunit. Binds 1 zinc ion per subunit.

KEGG Pathways
Map code Pathways E.C.

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00038 C00373 C00589 C00335 C00516 C00953 C00001 C00017 C00012
E.C.
Compound Zinc Elastin Collagen type III Collagen type IV Fibronectin Immunoglobulin A H2O Protein Peptide
Type heavy metal peptide/protein peptide/protein peptide/protein peptide/protein peptide/protein H2O peptide/protein peptide/protein
ChEBI 29105
15377
PubChem 32051
439221
22247451
962
1ezmA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_ZN Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1u4gA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_ZN Analogue:HPI Unbound Unbound Unbound Unbound Unbound Unbound
1ezmA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1u4gA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1ezm & Swiss-prot;P14756

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1ezmA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 112;GLU 141 HIS 140;HIS 144(Zinc binding) ALA 113
1u4gA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 112;GLU 141 HIS 140;HIS 144(Zinc binding) ALA 113
1ezmA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 155;HIS 223 GLU 164(Zinc binding)
1u4gA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 155;HIS 223 GLU 164(Zinc binding)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[9]
p.2867

References
[1]
Resource
Comments
Medline ID
PubMed ID 6767718
Journal J Biol Chem
Year 1980
Volume 255
Pages 3482-6
Authors Nishino N, Powers JC
Title Pseudomonas aeruginosa elastase. Development of a new substrate, inhibitors, and an affinity ligand.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 6815099
Journal Infect Immun
Year 1982
Volume 38
Pages 716-23
Authors Kessler E, Israel M, Landshman N, Chechick A, Blumberg S
Title In vitro inhibition of Pseudomonas aeruginosa elastase by metal-chelating peptide derivatives.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 6432034
Journal Biochemistry
Year 1984
Volume 23
Pages 2766-72
Authors Poncz L, Gerken TA, Dearborn DG, Grobelny D, Galardy RE
Title Inhibition of the elastase of Pseudomonas aeruginosa by N alpha-phosphoryl dipeptides and kinetics of spontaneous hydrolysis of the inhibitors.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 3142360
Journal Arch Biochem Biophys
Year 1988
Volume 266
Pages 508-15
Authors Poncz L
Title Substrate inhibition of Pseudomonas aeruginosa elastase by 3-(2-furyl)acryloyl-glycyl-L-phenylalanyl-L-phenylalanine.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 2516450
Journal Am J Respir Cell Mol Biol
Year 1989
Volume 1
Pages 37-9
Authors Pelletier A, Dimicoli JL, Boudier C, Bieth JG
Title Nonchromogenic hydrolysis of elastase and cathepsin G p-nitroanilide substrates by Pseudomonas aeruginosa elastase.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 2495818
Journal Biochim Biophys Acta
Year 1989
Volume 995
Pages 285-90
Authors Saulnier JM, Curtil FM, Duclos MC, Wallach JM
Title Elastolytic activity of Pseudomonas aeruginosa elastase.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 2493453
Journal J Bacteriol
Year 1989
Volume 171
Pages 1698-704
Authors Fukushima J, Yamamoto S, Morihara K, Atsumi Y, Takeuchi H, Kawamoto S, Okuda K
Title Structural gene and complete amino acid sequence of Pseudomonas aeruginosa IFO 3455 elastase.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 1744034
Journal J Bacteriol
Year 1991
Volume 173
Pages 7781-9
Authors McIver K, Kessler E, Ohman DE
Title Substitution of active-site His-223 in Pseudomonas aeruginosa elastase and expression of the mutated lasB alleles in Escherichia coli show evidence for autoproteolytic processing of proelastase.
Related PDB
Related UniProtKB
[9]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS)
Medline ID 91131579
PubMed ID 1899664
Journal J Biol Chem
Year 1991
Volume 266
Pages 2864-71
Authors Thayer MM, Flaherty KM, McKay DB
Title Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A resolution.
Related PDB 1ezm
Related UniProtKB P14756
[10]
Resource
Comments
Medline ID
PubMed ID 1445869
Journal Biochemistry
Year 1992
Volume 31
Pages 11310-6
Authors Holland DR, Tronrud DE, Pley HW, Flaherty KM, Stark W, Jansonius JN, McKay DB, Matthews BW
Title Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 1480011
Journal Matrix Suppl
Year 1992
Volume 1
Pages 112-5
Authors McKay DB, Thayer MM, Flaherty KM, Pley H, Benvegnu D
Title Crystallographic structures of the elastase of Pseudomonas aeruginosa.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 8484907
Journal Biotechnol Appl Biochem
Year 1993
Volume 17
Pages 217-21
Authors Pauchon V, Besson C, Saulnier J, Wallach J
Title Peptide synthesis catalysed by Pseudomonas aeruginosa elastase.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 8454342
Journal Infect Immun
Year 1993
Volume 61
Pages 1400-5
Authors Kawamoto S, Shibano Y, Fukushima J, Ishii N, Morihara K, Okuda K
Title Site-directed mutagenesis of Glu-141 and His-223 in Pseudomonas aeruginosa elastase: catalytic activity, processing, and protective activity of the elastase against Pseudomonas infection.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 10424483
Journal Electrophoresis
Year 1999
Volume 20
Pages 1578-85
Authors Viglio S, Zanaboni G, Lupi A, Gianelli L, Luisetti M, Casali L, Cetta G, Iadarola P
Title Micellar electrokinetic chromatography for analyzing active site specificity of Pseudomonas aeruginosa elastase.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 10195454
Journal J Pept Res
Year 1999
Volume 53
Pages 170-6
Authors Rival S, Besson C, Saulnier J, Wallach J
Title Dipeptide derivative synthesis catalyzed by Pseudomonas aeruginosa elastase.
Related PDB
Related UniProtKB

Comments
This enzyme belongs to peptidase family-M4 (Thermolysin family).
Although this enzyme binds a calcium ion, it is not involved in catalysis.
As the active site is the same as the thermolysin (D00234 in EzCatDB), the catalytic mechanism must be the same.

Created Updated
2005-04-13 2009-02-26