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Literature summary for 3.4.24.26 extracted from

  • Galdino, A.C.M.; de Oliveira, M.P.; Ramalho, T.C.; de Castro, A.A.; Branquinha, M.H.; Santos, A.L.S.
    Anti-virulence strategy against the multidrug-resistant bacterial pathogen Pseudomonas aeruginosa pseudolysin (elastase B) as a potential druggable target (2019), Curr. Protein Pept. Sci., 20, 471-487 .
    View publication on PubMed

Application

Application Comment Organism
medicine the enzyme is a promising target for the development of new anti-virulence compounds Pseudomonas aeruginosa

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline 1 mM, complete inhibition Pseudomonas aeruginosa
1-(biphenyl-4-ylmethyl)-3-hydroxy-2-methylpyridine-4(1H)-thione
-
Pseudomonas aeruginosa
5-fluorouracil
-
Pseudomonas aeruginosa
Baicalin
-
Pseudomonas aeruginosa
dehydroleucodine
-
Pseudomonas aeruginosa
EDTA
-
Pseudomonas aeruginosa
EGTA
-
Pseudomonas aeruginosa
eriodictyol
-
Pseudomonas aeruginosa
eugenol
-
Pseudomonas aeruginosa
HS-CH2-CO-Phe-Tyr-NH2 at 0.2 mM and 0.025 mM inhibits the degradation of the pseudolysin natural substrates nucleoside diphosphate kinase and IgG, respectively Pseudomonas aeruginosa
HSAc-Leu-Phe 0.1 mM, inhibits 97% of the degradation of azocasein and elastin substrates by pseudolysin Pseudomonas aeruginosa
HSAc-Phe-Leu 0.1 mM, inhibits 97% of the degradation of azocasein and elastin substrates by pseudolysin Pseudomonas aeruginosa
N-aryl mercaptoacetamide
-
Pseudomonas aeruginosa
N-mercaptoacetyl-Phe-Tyr-amide
-
Pseudomonas aeruginosa
naringenin
-
Pseudomonas aeruginosa
phosphoramidon powerful inhibition action on pseudolysin Pseudomonas aeruginosa
taxifolin
-
Pseudomonas aeruginosa
vitexin
-
Pseudomonas aeruginosa
zingerone
-
Pseudomonas aeruginosa

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular most abundant peptidase found in pseudomonal secretions, which contributes to the invasiveness of Pseudomonas aeruginosa due to its ability to cleave several extracellular matrix proteins and to disrupt the basolateral intercellular functions present in the host tissues Pseudomonas aeruginosa
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ zinc-dependent metallopeptidase Pseudomonas aeruginosa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
33000
-
-
Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
azocasein + H2O
-
Pseudomonas aeruginosa ?
-
?
IgG + H2O
-
Pseudomonas aeruginosa ?
-
?
N-succinyl-Ala-Ala-Ala-4-nitroanilide + H2O
-
Pseudomonas aeruginosa N-succinyl-Ala-Ala-Ala + 4-nitroaniline
-
?
nucleoside diphosphate kinase + H2O
-
Pseudomonas aeruginosa ?
-
?

Synonyms

Synonyms Comment Organism
elastase B
-
Pseudomonas aeruginosa

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.000041
-
N-mercaptoacetyl-Phe-Tyr-amide pH and temperature not specified in the publication Pseudomonas aeruginosa

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.0000059
-
pH and temperature not specified in the publication Pseudomonas aeruginosa N-aryl mercaptoacetamide
0.00273
-
pH and temperature not specified in the publication Pseudomonas aeruginosa 1-(biphenyl-4-ylmethyl)-3-hydroxy-2-methylpyridine-4(1H)-thione

General Information

General Information Comment Organism
physiological function the enzyme outstands as a pivotal virulence attribute during the infectious process, playing multifunctional roles in different aspects of the pathogen-host interaction. Most abundant peptidase found in pseudomonal secretions, which contributes to the invasiveness of Pseudomonas aeruginosa due to its ability to cleave several extracellular matrix proteins and to disrupt the basolateral intercellular functions present in the host tissues. Pseudolysin makes Pseudomonas aeruginosa able to overcome host defenses by the hydrolysis of many immunologically relevant molecules, including antibodies and complement components Pseudomonas aeruginosa