3.4.22.43: cathepsin V
This is an abbreviated version!
For detailed information about cathepsin V, go to the full flat file.
Word Map on EC 3.4.22.43
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3.4.22.43
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cathepsins
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papain-like
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elastases
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elastolytic
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legumain
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l-like
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medicine
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diagnostics
- 3.4.22.43
- cathepsins
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papain-like
- elastases
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elastolytic
- legumain
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l-like
- medicine
- diagnostics
Reaction
The recombinant enzyme hydrolyses proteins (serum albumin, collagen) and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec) =
Synonyms
cathepsin L2, cathepsin L2/V, cathepsin like 2, cathepsin U, cathepsin V, cathepsin V/L2, cathepsin-V, CatV, CL2, CTSL2, CTSV, CV/L2, hcatV, More, stratum corneum thiol protease
ECTree
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Inhibitors
Inhibitors on EC 3.4.22.43 - cathepsin V
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(1R)-1-{2-[butyl(dichloro)-l4-tellanyl]phenyl}ethyl methyl ether
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less than 10% residual activity at 0.001 mM
(1R)-1-{2-[dibromo(butyl)-l4-tellanyl]phenyl}ethyl methyl ether
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less than 10% residual activity at 0.001 mM
(1S)-1-{2-[butyl(dichloro)-l4-tellanyl]phenyl}ethyl methyl ether
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less than 10% residual activity at 0.001 mM
(1S)-1-{2-[dibromo(butyl)-l4-tellanyl]phenyl}ethyl methyl ether
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less than 10% residual activity at 0.001 mM
1,3,5-trihydroxy-4-methoxy-10-methyl-2,8-bis(3-methylbut-2-enyl)acridin-9(10H)-one
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2,3-dihydro-4,9-dihydroxy-2-(2-hydroxy-propan-2-yl)-11-methoxy-10-methylfuro[3,2-b]acridin-5(10H)-one
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2-[butyl(dichloro)-l4-tellanyl]benzyl methyl ether
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about 10% residual activity at 0.001 mM
2-[dibromo(butyl)-l4-tellanyl]benzyl methyl ether
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less than 10% residual activity at 0.001 mM
3,4-dihydro-3,5,8-trihydroxy-6-methoxy-2,2,7-trimethyl-2H-pyrano[2,3-a]acridin-12(7H)-one
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4-fluoro-N-prop-2-yn-1-yl-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
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4-methylpiperazine-1-carboxylic acid [1-[(3-benzenesulfonyl-1-phenethylallyl)carbamoyl]-2-phenylethyl]amide
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i.e. APC-3316
chondroitin 4-sulfate
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specific inhibition of elastolytic activity, formation of specific complexes with the enzyme, no inhibition of the activity with Z-Phe-Arg-4-methyl-7-coumaryl amide
cystatin C
endogenous inhibitor of cathepsin V analyzed, expression of cystatin C increased in stenotic valves, cystatin C protein particularly found in areas with infiltrates of inflammatory cells
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fragment p41 of major histocompatibility complex class II-associated invariant chain
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inhibitory to human cathepsin V, cathepsin L, cathepsin K, cathepsin F with Ki values in the low nanomolar range. Ki values are sufficiently low to ensure complex formation at physiological concentrations. Regulation of the proteolytic activity of most of the cysteine cathepsins by the p41 fragment is an important and widespread control mechanism of antigen presentation
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N-(3-bromoprop-2-yn-1-yl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
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N-(cyanomethyl)-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
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N-but-3-yn-2-yl-4-fluoro-N2-[(1S)-2,2,2-trifluoro-1-[4'-(methanesulfonyl)[1,1'-biphenyl]-4-yl]ethyl]-L-leucinamide
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N-[(1,1-dimethylethoxy)carbonyl]-L-tryptophan-2-[[[2-[(2-ethylphenyl)amino]-2-oxoethyl]thio]carbonyl]hydrazide
saquinavir
SQV, the HIV protease inhibitor Inhibits the interaction between cathepsin V and the TLR4-MyD88 receptor complex, also blocks disulfide HMGB1-induced TLR4 activation
serpin
cofactors fine tuning serpin activity in the extracellular milieu analyzed, DNA accelerate the rate at which the model serpin MENT inhibit cathepsin V up to 50-fold, primarily effected via the protease and secondarily by the recruitment of the DNA as a template onto which cathepsin V and MENT are bound, altered substrate turnover and conformational change within the protease observed, enzyme concentration constant at 0.1 nM, serpin concentration varying between 0.5 and 60 nM with a maximum of 5 nM serpin in the presence of DNA
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STO33438
334, a mammalian protease inhibitor, inhibits cathepsin V, also blocks disulfide HMGB1-induced TLR4 activation
cystatin
cystatin inhibition relies on occlusion of the active site rather than the substrate-like behavior of serpins, unaltered by addition of DNA
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cystatin M/E wild-type and mutant N64A show high affinity for cathepsin V, but not cystatin M/E mutant W135A
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cystatin M/E
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regulatory role, two distinct binding sites for cysteine proteases of the C1 peptidase family, the endogenous inhibitor is co-localized with the enzyme in lamellar granules and corneodesmosomes
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cystatin M/E
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the antiprotease activity of cystatin M/E inhibits the activity of cathepsin V
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cystatin M/E
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high-affinity inhibitor of cathepsin V, directly controls the activity of cathepsin V
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N-[(1,1-dimethylethoxy)carbonyl]-L-tryptophan-2-[[[2-[(2-ethylphenyl)amino]-2-oxoethyl]thio]carbonyl]hydrazide
SID, suppresses the activity of cathepsin V and reverses the upregulation of inflammatory cytokines (IL-6, IL-8 and TNF-alpha), adhesion and chemotaxis of leukocytes and vascular inflammation induced by L-homocysteine (L-Hcy) in vivo and in vitro. SID also inhibits the monocyte-endothelial adhesion and neutrophil chemotaxis induced by L-Hcy. SID reverses this increased phosphorylation of ERK1/2 and STAT1, which is similar to the results obtained in vitro
N-[(1,1-dimethylethoxy)carbonyl]-L-tryptophan-2-[[[2-[(2-ethylphenyl)amino]-2-oxoethyl]thio]carbonyl]hydrazide
SID, inhibits the enzyme and also blocks HMGB1-induced TNF-alpha production