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4-hydroxy-2-nonenal mercapturate + H2O
?
acrolein mercapturate + H2O
?
N-acetyl-1,2-dichlorovinyl-L-cysteine + H2O
acetate + 1,2-dichlorovinyl-L-cysteine
-
-
-
?
N-acetyl-L-histidine + H2O
acetate + L-histidine
N-acetyl-L-lysine + H2O
acetate + L-lysine
-
-
-
-
?
N-acetyl-L-phenylalanine + H2O
acetate + L-phenylalanine
N-acetyl-L-tryptophan + H2O
acetate + L-tryptophan
-
-
-
-
?
N-acetyl-L-tyrosine + H2O
acetate + L-tyrosine
N-acetyl-S-(1,1,2,2-tetrafluoroethyl)-L-cysteine + H2O
acetate + S-(1,1,2,2-tetrafluoroethyl)-L-cysteine
-
-
-
-
?
N-acetyl-S-(1,2,2-trichlorovinyl)-L-cysteine + H2O
acetate + S-(1,2,2-trichlorovinyl)-L-cysteine
-
-
-
-
?
N-acetyl-S-(1,2,3,4,4-pentachlorobutadienyl)-L-cysteine + H2O
acetate + S-(1,2,3,4,4-pentachlorobutadienyl)-L-cysteine
-
good substrate
-
-
?
N-acetyl-S-(1,2-dichlorovinyl)-L-cysteine + H2O
acetate + S-(1,2-dichlorovinyl)-L-cysteine
N-acetyl-S-(2,2-dichloro-1,1-difluoroethyl)-L-cysteine + H2O
acetate + S-(2,2-dichloro-1,1-difluoroethyl)-L-cysteine
-
-
-
-
?
N-acetyl-S-(2,2-dichlorovinyl)-L-cysteine + H2O
acetate + S-(2,2-dichlorovinyl)-L-cysteine
-
good substrate
-
-
?
N-acetyl-S-(2,2-difluoro-1,1-dichloroethyl)-L-cysteine + H2O
acetate + S-(2,2-difluoro-1,1-dichloroethyl)-L-cysteine
-
-
-
-
?
N-acetyl-S-(2-chloro-1,1,2-trifluoroethyl)-L-cysteine + H2O
acetate + S-(2-chloro-1,1,2-trifluoroethyl)-L-cysteine
-
-
-
-
?
N-acetyl-S-(2-chlorobenzyl)-L-cysteine + H2O
acetate + S-(2-chlorobenzyl)-L-cysteine
-
-
-
-
?
N-acetyl-S-(2-fluorobenzyl)-L-cysteine + H2O
acetate + S-(2-fluorobenzyl)-L-cysteine
-
-
-
-
?
N-acetyl-S-(3-fluorobenzyl)-L-cysteine + H2O
acetate + S-(3-fluorobenzyl)-L-cysteine
-
-
-
-
?
N-acetyl-S-(4-bromobenzyl)-L-cysteine + H2O
acetate + S-(4-bromobenzyl)-L-cysteine
-
good substrate
-
-
?
N-acetyl-S-(4-chlorobenzyl)-L-cysteine + H2O
acetate + S-(4-chlorobenzyl)-L-cysteine
-
good substrate
-
-
?
N-acetyl-S-(4-methoxybenzyl)-L-cysteine + H2O
acetate + S-(4-methoxybenzyl)-L-cysteine
-
-
-
-
?
N-acetyl-S-benzyl-L-cysteine + H2O
acetate + S-benzyl-L-cysteine
N-acetyl-S-geranylgeranyl-L-cysteine + H2O
3-geranylgeranyl-L-cysteine + acetate
N-acetyl-S-[(2E,6E)-farnesyl]-L-cysteine + H2O
S-[(2E,6E)-farnesyl]-L-cysteine + acetate
Nalpha-acetylated peptide + H2O
acetate + peptide
N-terminal peptides derived from hepatitis C virus core protein
-
-
?
additional information
?
-
4-hydroxy-2-nonenal mercapturate + H2O
?
substrate of aminoacylase 3, not aminoacylase 1, deacetylation
-
-
?
4-hydroxy-2-nonenal mercapturate + H2O
?
substrate of aminoacylase 3, not aminoacylase 1, deacetylation
-
-
?
4-hydroxy-2-nonenal mercapturate + H2O
?
substrate of aminoacylase 3, not aminoacylase 1, deacetylation
-
-
?
4-hydroxy-2-nonenal mercapturate + H2O
?
substrate of aminoacylase 3, not aminoacylase 1, deacetylation
-
-
?
acrolein mercapturate + H2O
?
substrate of aminoacylase 3, not aminoacylase 1, deacetylation
-
-
?
acrolein mercapturate + H2O
?
substrate of aminoacylase 3, not aminoacylase 1, deacetylation
-
-
?
acrolein mercapturate + H2O
?
substrate of aminoacylase 3, not aminoacylase 1, deacetylation
-
-
?
acrolein mercapturate + H2O
?
substrate of aminoacylase 3, not aminoacylase 1, deacetylation
-
-
?
N-acetyl-L-histidine + H2O
acetate + L-histidine
-
-
-
-
?
N-acetyl-L-histidine + H2O
acetate + L-histidine
-
-
-
?
N-acetyl-L-phenylalanine + H2O
acetate + L-phenylalanine
-
-
-
-
?
N-acetyl-L-phenylalanine + H2O
acetate + L-phenylalanine
-
-
-
?
N-acetyl-L-tyrosine + H2O
acetate + L-tyrosine
-
-
-
-
?
N-acetyl-L-tyrosine + H2O
acetate + L-tyrosine
-
-
-
?
N-acetyl-S-(1,2-dichlorovinyl)-L-cysteine + H2O
acetate + S-(1,2-dichlorovinyl)-L-cysteine
-
-
-
-
?
N-acetyl-S-(1,2-dichlorovinyl)-L-cysteine + H2O
acetate + S-(1,2-dichlorovinyl)-L-cysteine
-
-
-
?
N-acetyl-S-benzyl-L-cysteine + H2O
acetate + S-benzyl-L-cysteine
-
-
-
-
?
N-acetyl-S-benzyl-L-cysteine + H2O
acetate + S-benzyl-L-cysteine
-
-
-
?
N-acetyl-S-geranylgeranyl-L-cysteine + H2O
3-geranylgeranyl-L-cysteine + acetate
-
-
-
?
N-acetyl-S-geranylgeranyl-L-cysteine + H2O
3-geranylgeranyl-L-cysteine + acetate
the 90000-100000 Da AA3 form (that is detected in most hepatocellular carcinoma cell lines but not in normal hepatocytes) is functionally active and together with the normal 35000 Da AA3 form mediates the deacetylation of N-acetylfarnesylcysteine and N-acetylgeranylgeranylcysteine
-
-
?
N-acetyl-S-[(2E,6E)-farnesyl]-L-cysteine + H2O
S-[(2E,6E)-farnesyl]-L-cysteine + acetate
-
-
-
?
N-acetyl-S-[(2E,6E)-farnesyl]-L-cysteine + H2O
S-[(2E,6E)-farnesyl]-L-cysteine + acetate
the 90000-100000 Da AA3 form (that is detected in most hepatocellular carcinoma cell lines but not in normal hepatocytes) is functionally active and together with the normal 35000 Da AA3 form mediates the deacetylation of N-acetylfarnesylcysteine and N-acetylgeranylgeranylcysteine
-
-
?
additional information
?
-
-
no activity with N-acetyl-L-cysteine, N-acetyl-L-aspartic acid and Nepsilon-acetyl-L-lysine
-
-
?
additional information
?
-
the enzyme uses as a substrate the N-acetylated L-aromatic amino acids tyrosine, phenylalanine, and tryptophan
-
-
?
additional information
?
-
-
the enzyme uses as a substrate the N-acetylated L-aromatic amino acids tyrosine, phenylalanine, and tryptophan
-
-
?
additional information
?
-
the enzyme directly binds to the hepatitis C virus core protein and also reveals a weak endopeptidase activity towards the N-terminus of hepatitis C virus core protein, interaction analysis of the enzyme with N-terminal peptides derived from hepatitis C virus core protein via surface plasmon resonance method, overview
-
-
?
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0.2 - 0.53
4-hydroxy-2-nonenal mercapturate
0.71 - 0.82
acrolein mercapturate
1.11 - 17.73
N-acetyl-1,2-dichlorovinyl-L-cysteine
1.3
N-acetyl-L-lysine
-
pH 7.5, 37°C
1.6
N-acetyl-L-phenylalanine
1.2
N-acetyl-L-tryptophan
-
pH 7.5, 37°C
0.18 - 5.2
N-acetyl-L-tyrosine
0.25
N-acetyl-S-(1,1,2,2-tetrafluoroethyl)-L-cysteine
-
pH 7.5, 37°C
1.2
N-acetyl-S-(1,2,2-trichlorovinyl)-L-cysteine
-
pH 7.5, 37°C
1
N-acetyl-S-(1,2,3,4,4-pentachlorobutadienyl)-L-cysteine
-
pH 7.5, 37°C
0.56 - 1.3
N-acetyl-S-(1,2-dichlorovinyl)-L-cysteine
5.3
N-acetyl-S-(2,2-dichloro-1,1-difluoroethyl)-L-cysteine
-
pH 7.5, 37°C
0.4
N-acetyl-S-(2,2-dichlorovinyl)-L-cysteine
-
pH 7.5, 37°C
0.3
N-acetyl-S-(2,2-difluoro-1,1-dichloroethyl)-L-cysteine
-
pH 7.5, 37°C
0.28
N-acetyl-S-(2-chloro-1,1,2-trifluoroethyl)-L-cysteine
-
pH 7.5, 37°C
1.45
N-acetyl-S-(2-chlorobenzyl)-L-cysteine
-
pH 7.5, 37°C
1.3
N-acetyl-S-(2-fluorobenzyl)-L-cysteine
-
pH 7.5, 37°C
0.6
N-acetyl-S-(3-fluorobenzyl)-L-cysteine
-
pH 7.5, 37°C
0.5
N-acetyl-S-(4-bromobenzyl)-L-cysteine
-
pH 7.5, 37°C
0.3
N-acetyl-S-(4-chlorobenzyl)-L-cysteine
-
pH 7.5, 37°C
0.8
N-acetyl-S-(4-methoxybenzyl)-L-cysteine
-
pH 7.5, 37°C
1.1
N-acetyl-S-benzyl-L-cysteine
0.14
N-acetyl-S-geranylgeranyl-L-cysteine
pH 7.5, 37°C
0.025
N-acetyl-S-[(2E,6E)-farnesyl]-L-cysteine
pH 7.5, 37°C
additional information
additional information
Michaelis-Menten kinetics
-
0.2
4-hydroxy-2-nonenal mercapturate
pH and temperature not specified in the publication, absence of Co2+
0.53
4-hydroxy-2-nonenal mercapturate
pH and temperature not specified in the publication, presence of Co2+
0.71
acrolein mercapturate
pH and temperature not specified in the publication, presence of Co2+
0.82
acrolein mercapturate
pH and temperature not specified in the publication, absence of Co2+
1.11
N-acetyl-1,2-dichlorovinyl-L-cysteine
pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme K290A
2.46
N-acetyl-1,2-dichlorovinyl-L-cysteine
pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme D114A
2.48
N-acetyl-1,2-dichlorovinyl-L-cysteine
pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme N70A
3.02
N-acetyl-1,2-dichlorovinyl-L-cysteine
pH 7.5, temperature not specified in the publication, activated by Co2+, wild-type enzyme
3.4
N-acetyl-1,2-dichlorovinyl-L-cysteine
pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme E289A
3.49
N-acetyl-1,2-dichlorovinyl-L-cysteine
pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme N70A
4.21
N-acetyl-1,2-dichlorovinyl-L-cysteine
pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme Y287A
4.51
N-acetyl-1,2-dichlorovinyl-L-cysteine
pH 7.5, temperature not specified in the publication, without Co2+, wild-type enzyme
5.14
N-acetyl-1,2-dichlorovinyl-L-cysteine
pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme D114A
6.76
N-acetyl-1,2-dichlorovinyl-L-cysteine
pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme Y288A
7
N-acetyl-1,2-dichlorovinyl-L-cysteine
pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme R71A
11
N-acetyl-1,2-dichlorovinyl-L-cysteine
pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme K290A
11.03
N-acetyl-1,2-dichlorovinyl-L-cysteine
pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme E289A
12.4
N-acetyl-1,2-dichlorovinyl-L-cysteine
pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme R71A
13.61
N-acetyl-1,2-dichlorovinyl-L-cysteine
pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme Y287A
17.73
N-acetyl-1,2-dichlorovinyl-L-cysteine
pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme Y288A
1.8
N-acetyl-L-histidine
-
pH 7.5, 37°C
1.8
N-acetyl-L-histidine
pH 7.5, 37°C
1.6
N-acetyl-L-phenylalanine
-
pH 7.5, 37°C
1.6
N-acetyl-L-phenylalanine
pH 7.5, 37°C
0.18
N-acetyl-L-tyrosine
pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme D114A
0.22
N-acetyl-L-tyrosine
pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme Y156A
0.23
N-acetyl-L-tyrosine
pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme Y287A
0.23
N-acetyl-L-tyrosine
pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme Y287A
0.25
N-acetyl-L-tyrosine
pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme E289A
0.25
N-acetyl-L-tyrosine
pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme D114A
0.25
N-acetyl-L-tyrosine
pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme E289A
0.26
N-acetyl-L-tyrosine
pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme K290A
0.26
N-acetyl-L-tyrosine
pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme R67D
0.27
N-acetyl-L-tyrosine
pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme K290A
0.3
N-acetyl-L-tyrosine
pH and temperature not specified in the publication, presence of Co2+
0.45
N-acetyl-L-tyrosine
pH and temperature not specified in the publication, absence of Co2+
0.53
N-acetyl-L-tyrosine
pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme R67D
0.55
N-acetyl-L-tyrosine
pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme D235R
0.56
N-acetyl-L-tyrosine
pH 7.5, temperature not specified in the publication, activated by Co2+, wild-type enzyme
0.61
N-acetyl-L-tyrosine
pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme E167R
0.64
N-acetyl-L-tyrosine
pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme E167A
0.71
N-acetyl-L-tyrosine
pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme R71A
0.79
N-acetyl-L-tyrosine
pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme Y156A
0.83
N-acetyl-L-tyrosine
pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme E167A
1.3
N-acetyl-L-tyrosine
pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme E167R
1.3
N-acetyl-L-tyrosine
pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme D235R
1.3
N-acetyl-L-tyrosine
pH 7.5, temperature not specified in the publication, without Co2+, wild-type enzyme
1.4
N-acetyl-L-tyrosine
-
pH 7.5, 37°C
1.4
N-acetyl-L-tyrosine
pH 7.5, 37°C
2.02
N-acetyl-L-tyrosine
pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme R71A
2.8
N-acetyl-L-tyrosine
pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme N70A
2.83
N-acetyl-L-tyrosine
pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme N70A
3.71
N-acetyl-L-tyrosine
pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme Y288A
5.2
N-acetyl-L-tyrosine
pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme Y288A
0.56
N-acetyl-S-(1,2-dichlorovinyl)-L-cysteine
pH and temperature not specified in the publication, presence of Co2+
0.9
N-acetyl-S-(1,2-dichlorovinyl)-L-cysteine
-
pH 7.5, 37°C
1.3
N-acetyl-S-(1,2-dichlorovinyl)-L-cysteine
pH and temperature not specified in the publication, absence of Co2+
1.1
N-acetyl-S-benzyl-L-cysteine
-
pH 7.5, 37°C
1.1
N-acetyl-S-benzyl-L-cysteine
pH 7.5, 37°C
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Newman, D.; Abuladze, N.; Scholz, K.; Dekant, W.; Tsuprun, V.; Ryazantsev, S.; Bondar, G.; Sassani, P.; Kurtz, I.; Pushkin, A.
Specificity of aminoacylase III-mediated deacetylation of mercapturic acids
Drug Metab. Dispos.
35
43-50
2007
Mus musculus
brenda
Pushkin, A.; Carpenito, G.; Abuladze, N.; Newman, D.; Tsuprun, V.; Ryazantsev, S.; Motemoturu, S.; Sassani, P.; Solovieva, N.; Dukkipati, R.; Kurtz, I.
Structural characterization, tissue distribution, and functional expression of murine aminoacylase III
Am. J. Physiol. Cell Physiol.
286
C848-856
2003
Mus musculus (Q91XE4), Mus musculus
brenda
Tsirulnikov, K.; Abuladze, N.; Newman, D.; Ryazantsev, S.; Wolak, T.; Magilnick, N.; Koag, M.C.; Kurtz, I.; Pushkin, A.
Mouse aminoacylase 3: a metalloenzyme activated by cobalt and nickel
Biochim. Biophys. Acta
1794
1049-1057
2009
Mus musculus (Q91XE4)
brenda
Hsieh, J.M.; Tsirulnikov, K.; Sawaya, M.R.; Magilnick, N.; Abuladze, N.; Kurtz, I.; Abramson, J.; Pushkin, A.
Structures of aminoacylase 3 in complex with acetylated substrates
Proc. Natl. Acad. Sci. USA
107
17962-17967
2010
Mus musculus (Q91XE4)
brenda
Tsirulnikov, K.; Abuladze, N.; Bragin, A.; Faull, K.; Cascio, D.; Damoiseaux, R.; Schibler, M.J.; Pushkin, A.
Inhibition of aminoacylase 3 protects rat brain cortex neuronal cells from the toxicity of 4-hydroxy-2-nonenal mercapturate and 4-hydroxy-2-nonenal
Toxicol. Appl. Pharmacol.
263
303-314
2012
Rattus norvegicus (Q5M876), Mus musculus (Q91XE4), Homo sapiens (Q96HD9), Rattus norvegicus Wistar (Q5M876)
brenda
Tsirulnikov, K.; Abuladze, N.; Vahi, R.; Hasnain, H.; Phillips, M.; Ryan, C.; Atanasov, I.; Faull, K.; Kurtz, I.; Pushkin, A.
Aminoacylase 3 binds to and cleaves the N-terminus of the hepatitis C virus core protein
FEBS Lett.
586
3799-3804
2012
Mus musculus (Q91XE4)
brenda
Tsirulnikov, K.; Duarte, S.; Ray, A.; Datta, N.; Zarrinpar, A.; Hwang, L.; Faull, K.; Pushkin, A.; Kurtz, I.
Aminoacylase 3 is a new potential marker and therapeutic target in hepatocellular carcinoma
J. Cancer
9
1-12
2018
Homo sapiens (Q96HD9), Homo sapiens
brenda