EzCatDB: D00233
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DB codeD00233
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.3.4.24.26

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

Enzyme Name
UniProtKBKEGG

P14756
Protein namePseudolysinpseudolysin
Pseudomonas elastase
Pseudomonas aeruginosa neutral metalloproteinase
SynonymsEC 3.4.24.26
Elastase
Neutral metalloproteinase
RefSeqNP_252413.1 (Protein)
NC_002516.2 (DNA/RNA sequence)
MEROPSM04.005 (Metallo)
PfamPF07504 (FTP)
PF03413 (PepSY)
PF01447 (Peptidase_M4)
PF02868 (Peptidase_M4_C)
[Graphical view]


UniProtKB:Accession NumberP14756
Entry nameELAS_PSEAE
ActivityHydrolysis 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.
Subunit
Subcellular locationSecreted.
CofactorBinds 1 calcium ion per subunit.,Binds 1 zinc ion per subunit.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00038C00373C00589C00335C00516C00953C00001C00017C00012
CompoundZincElastinCollagen type IIICollagen type IVFibronectinImmunoglobulin AH2OProteinPeptide
Typeheavy metalpeptide/proteinpeptide/proteinpeptide/proteinpeptide/proteinpeptide/proteinH2Opeptide/proteinpeptide/protein
ChEBI29105





15377


PubChem32051
439221




962
22247451


                 
1ezmA01Bound:_ZNUnboundUnboundUnboundUnboundUnbound UnboundUnbound
1u4gA01Bound:_ZNAnalogue:HPIUnboundUnboundUnboundUnbound UnboundUnbound
1ezmA02UnboundUnboundUnboundUnboundUnboundUnbound UnboundUnbound
1u4gA02UnboundUnboundUnboundUnboundUnboundUnbound UnboundUnbound

Active-site residues
resource
PDB;1ezm & Swiss-prot;P14756
pdbCatalytic residuesCofactor-binding residuesMain-chain involved in catalysis
           
1ezmA01ASN 112;GLU 141
HIS 140;HIS 144(Zinc binding)
ALA 113
1u4gA01ASN 112;GLU 141
HIS 140;HIS 144(Zinc binding)
ALA 113
1ezmA02TYR 155;HIS 223
GLU 164(Zinc binding)
 
1u4gA02TYR 155;HIS 223
GLU 164(Zinc binding)
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[9]p.2867

references
[1]
PubMed ID6767718
JournalJ Biol Chem
Year1980
Volume255
Pages3482-6
AuthorsNishino N, Powers JC
TitlePseudomonas aeruginosa elastase. Development of a new substrate, inhibitors, and an affinity ligand.
[2]
PubMed ID6815099
JournalInfect Immun
Year1982
Volume38
Pages716-23
AuthorsKessler E, Israel M, Landshman N, Chechick A, Blumberg S
TitleIn vitro inhibition of Pseudomonas aeruginosa elastase by metal-chelating peptide derivatives.
[3]
PubMed ID6432034
JournalBiochemistry
Year1984
Volume23
Pages2766-72
AuthorsPoncz L, Gerken TA, Dearborn DG, Grobelny D, Galardy RE
TitleInhibition of the elastase of Pseudomonas aeruginosa by N alpha-phosphoryl dipeptides and kinetics of spontaneous hydrolysis of the inhibitors.
[4]
PubMed ID3142360
JournalArch Biochem Biophys
Year1988
Volume266
Pages508-15
AuthorsPoncz L
TitleSubstrate inhibition of Pseudomonas aeruginosa elastase by 3-(2-furyl)acryloyl-glycyl-L-phenylalanyl-L-phenylalanine.
[5]
PubMed ID2516450
JournalAm J Respir Cell Mol Biol
Year1989
Volume1
Pages37-9
AuthorsPelletier A, Dimicoli JL, Boudier C, Bieth JG
TitleNonchromogenic hydrolysis of elastase and cathepsin G p-nitroanilide substrates by Pseudomonas aeruginosa elastase.
[6]
PubMed ID2495818
JournalBiochim Biophys Acta
Year1989
Volume995
Pages285-90
AuthorsSaulnier JM, Curtil FM, Duclos MC, Wallach JM
TitleElastolytic activity of Pseudomonas aeruginosa elastase.
[7]
PubMed ID2493453
JournalJ Bacteriol
Year1989
Volume171
Pages1698-704
AuthorsFukushima J, Yamamoto S, Morihara K, Atsumi Y, Takeuchi H, Kawamoto S, Okuda K
TitleStructural gene and complete amino acid sequence of Pseudomonas aeruginosa IFO 3455 elastase.
[8]
PubMed ID1744034
JournalJ Bacteriol
Year1991
Volume173
Pages7781-9
AuthorsMcIver K, Kessler E, Ohman DE
TitleSubstitution 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.
[9]
CommentsX-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS)
Medline ID91131579
PubMed ID1899664
JournalJ Biol Chem
Year1991
Volume266
Pages2864-71
AuthorsThayer MM, Flaherty KM, McKay DB
TitleThree-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A resolution.
Related PDB1ezm
Related UniProtKBP14756
[10]
PubMed ID1445869
JournalBiochemistry
Year1992
Volume31
Pages11310-6
AuthorsHolland DR, Tronrud DE, Pley HW, Flaherty KM, Stark W, Jansonius JN, McKay DB, Matthews BW
TitleStructural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis.
[11]
PubMed ID1480011
JournalMatrix Suppl
Year1992
Volume1
Pages112-5
AuthorsMcKay DB, Thayer MM, Flaherty KM, Pley H, Benvegnu D
TitleCrystallographic structures of the elastase of Pseudomonas aeruginosa.
[12]
PubMed ID8484907
JournalBiotechnol Appl Biochem
Year1993
Volume17
Pages217-21
AuthorsPauchon V, Besson C, Saulnier J, Wallach J
TitlePeptide synthesis catalysed by Pseudomonas aeruginosa elastase.
[13]
PubMed ID8454342
JournalInfect Immun
Year1993
Volume61
Pages1400-5
AuthorsKawamoto S, Shibano Y, Fukushima J, Ishii N, Morihara K, Okuda K
TitleSite-directed mutagenesis of Glu-141 and His-223 in Pseudomonas aeruginosa elastase: catalytic activity, processing, and protective activity of the elastase against Pseudomonas infection.
[14]
PubMed ID10424483
JournalElectrophoresis
Year1999
Volume20
Pages1578-85
AuthorsViglio S, Zanaboni G, Lupi A, Gianelli L, Luisetti M, Casali L, Cetta G, Iadarola P
TitleMicellar electrokinetic chromatography for analyzing active site specificity of Pseudomonas aeruginosa elastase.
[15]
PubMed ID10195454
JournalJ Pept Res
Year1999
Volume53
Pages170-6
AuthorsRival S, Besson C, Saulnier J, Wallach J
TitleDipeptide derivative synthesis catalyzed by Pseudomonas aeruginosa elastase.

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.

createdupdated
2005-04-132009-02-26


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