3.4.24.26: pseudolysin
This is an abbreviated version!
For detailed information about pseudolysin, go to the full flat file.
Word Map on EC 3.4.24.26
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3.4.24.26
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thermolysin
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metalloproteinases
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collagenase
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metalloprotease
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3.4.24.4
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elastin
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gelatinase
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elastases
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phosphoramidon
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pseudomonal
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stromelysin
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thermolysin-like
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metalloendopeptidase
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medicine
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thermoproteolyticus
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aureolysin
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vibriolysin
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intrastromal
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industry
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nutrition
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biotechnology
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synthesis
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pharmacology
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diagnostics
- 3.4.24.26
- thermolysin
- metalloproteinases
- collagenase
- metalloprotease
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3.4.24.4
- elastin
- gelatinase
- elastases
- phosphoramidon
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pseudomonal
- stromelysin
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thermolysin-like
- metalloendopeptidase
- medicine
- thermoproteolyticus
- aureolysin
- vibriolysin
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intrastromal
- industry
- nutrition
- biotechnology
- synthesis
- pharmacology
- diagnostics
Reaction
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 =
Synonyms
A2 elastase, aeruginolysin, ealastase LasB, EC 3.4.24.4, elastase, elastase B, elastolytic metalloproteinase, EPa, LasB, LasB protease, LepA, More, Neutral metalloproteinase, PAE, PASP, PE, PsE, Pseudomonas aeruginosa elastase, Pseudomonas aeruginosa neutral metalloproteinase, Pseudomonas aeruginosa small protease, Pseudomonas elastase, Pseudomonas protease
ECTree
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Inhibitors
Inhibitors on EC 3.4.24.26 - pseudolysin
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2-mercaptoacetyl-L-phenylalanyl-L-leucine
prevents corneal perforation completely
2-mercaptoacetyl-Phe-Leu
at 0.1 mM 96% inhibition with azocasein as substrate, 97% inhibition with elastin as substrate and 97% inhibition with cartilage as substrate, at 0.01 mM 77% inhibition with azocasein as substrate, 33% inhibition with elastin as substrate and 66% inhibition with cartilage as substrate
2-[(biphenyl-4-ylsulfonyl)[2-(hydroxyamino)-2-oxoethyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide (non-preferred name)
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2-[benzyl[2-(hydroxyamino)-2-oxoethyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide (non-preferred name)
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the phenyl group of the strong binder occupies the S'2-subpocket, while a second ring system occupy the S1-subpocket in both thermolysin, EC 3.4.24.27, and pseudolysin
2-[benzyl[2-(hydroxyamino)-2-oxoethyl]amino]-N-[3-(4-phenylpiperazin-1-yl)propyl]acetamide (non-preferred name)
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the phenyl group of the strong binder occupies the S'2-subpocket, while a second ring system occupy the S1-subpocket in both thermolysin, EC 3.4.24.27, and pseudolysin
2-[[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide (non-preferred name)
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2-[[2-(hydroxyamino)-2-oxoethyl][(4-phenoxyphenyl)sulfonyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide (non-preferred name)
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ammonium chloride
extracellular elastase activity decreases if cells are cultured in the presence of ammonium chloride
anti elastase monoclonal antibody
reduces PE activity significantly
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benzyloxycarbonyl-Gly-NHOH
at 14 mM 98% inhibition with azocasein as substrate, 95% inhibition with elastin as substrate and 95% inhibition with cartilage as substrate, at 1.4 mM 77% inhibition with azocasein as substrate, 84% inhibition with elastin as substrate and 67% inhibition with cartilage as substrate
benzyloxycarbonyl-Leu-NHOH
at 5.0 mM 98% inhibition with azocasein as substrate, 100% inhibition with elastin as substrate and 94% inhibition with cartilage as substrate, at 0.5 mM 76% inhibition with azocasein as substrate, 93% inhibition with elastin as substrate and 57% inhibition with cartilage as substrate
D-glucose
extracellular elastase activity decreases if cells are cultured in the presence of glucose
HS-CH2-CO-Phe-Tyr-NH2
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at 0.2 mM and 0.025 mM inhibits the degradation of the pseudolysin natural substrates nucleoside diphosphate kinase and IgG, respectively
HSAc-Leu-Phe
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0.1 mM, inhibits 97% of the degradation of azocasein and elastin substrates by pseudolysin
HSAc-Phe-Leu
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0.1 mM, inhibits 97% of the degradation of azocasein and elastin substrates by pseudolysin
N-(1-carboxy-3-phenylpropyl)-phenylalanyl-alpha-asparagine
enzyme binding structure analysis, PDB ID 1U4G. The inhibitor is bound in the S1-S1 sub-sites of pseudolysin by hydrogen bonding and hydrophobic and weak van der Waal's interactions
N-[(2R)-1-(hydroxyamino)-3-methyl-1-oxobutan-2-yl]-N-[(4-phenoxyphenyl)sulfonyl]glycine
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peptides
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containing the hydroxamic acid, N-hydroxypeptide and thiol functional groups
Streptomyces metalloproteinase inhibitor
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i.e. SMPI, molecular dynamics study of enzyme-inhibitor complex. Inhibitor interacts with pseudolysin via the rigid active side loop and several contact sites outside this loop
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[(biphenyl-4-ylmethyl)[2-(hydroxyamino)-2-oxoethyl]amino]acetic acid
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[(biphenyl-4-ylsulfonyl)[2-(hydroxyamino)-2-oxoethyl]amino]acetic acid
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[1-[2-(hydroxyamino)-2-oxoethyl]-2-[3-(4-phenylpiperazin-1-yl)propyl]hydrazinyl]acetic acid
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[[(4-methoxyphenyl)sulfonyl](2-oxo-2-[[2-(4-sulfamoylphenyl)ethyl]amino]ethyl)amino]acetic acid
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[[2-(hydroxyamino)-2-oxoethyl](4-nitrobenzyl)amino]acetic acid
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[[2-(hydroxyamino)-2-oxoethyl](4-phenoxybenzyl)amino]acetic acid
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[[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]acetic acid
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[[2-(hydroxyamino)-2-oxoethyl][(4-phenoxyphenyl)sulfonyl]amino]acetic acid
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phosphoramidon
N-(alpha-rhamnopyranosyloxyhydroxyphosphinyl)-Leu-Trp
phosphoramidon
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N-(alpha-L-rhamnopyranosyloxyhydroxyphosphinyl)-L-leucyl-L-tryptophan
at 0.1 mM 98% inhibition with azocasein as substrate, 94% inhibition with elastin as substrate and 98% inhibition with cartilage as substrate, at 0.01 mM 83% inhibition with azocasein as substrate, 87% inhibition with elastin as substrate and 89% inhibition with cartilage as substrate
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inhibitor synthesis, docking analysis and binding structure, molecular modeling and Molecular dynamics simulation of pseudolysin-ligand interactions, overview. When the compounds possess two ring systems, the largest and most electron rich ring system seems to occupy the S1-subpocket. The fourth zinc coordinating ligand in the free enzyme is a water molecule. Upon inhibitor binding this water molecule is replaced by a metal binding group of the inhibitor
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additional information
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diisopropyl fluorophosphate; not: ClCH2CO-N-hydroxyleucine-OCH3; tosyl-L-Phe chloromethyl ketone, PCMB
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additional information
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no inhibition by diisopropylphosphofluoridate at 20 mM
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additional information
extracellular elastase activity decreases if cells are cultured in the presence of sub-inhibitory concentrations of certain antibiotics
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additional information
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extracellular elastase activity decreases if cells are cultured in the presence of sub-inhibitory concentrations of certain antibiotics
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additional information
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no inhibition by dithio-bis(nitrobenzoic acid) and phenylmethylsulfonyl fluoride, and by K+ and Na+
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additional information
N-alpha mercaptoamide-containing dipeptides as inhibitors
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additional information
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N-alpha mercaptoamide-containing dipeptides as inhibitors
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