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Information on EC 3.5.1.114 - N-acyl-aromatic-L-amino acid amidohydrolase and Organism(s) Mus musculus and UniProt Accession Q91XE4
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3.5.1.114 N-acyl-aromatic-L-amino acid amidohydrolaseIUBMB Comments
This enzyme is found in animals and is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). It preferentially deacetylates Nalpha-acetylated aromatic amino acids and mercapturic acids (S-conjugates of N-acetyl-L-cysteine) that are usually not deacetylated by EC 3.5.1.14, N-acyl-aliphatic-L-amino acid amidohydrolase. The enzyme is significantly activated by Co2+ and Ni2+ . Some bacterial aminoacylases demonstrate substrate specificity for both EC 3.5.1.14 and EC 3.5.1.114. cf. EC 3.5.1.14, N-acyl-aliphatic-L-amino acid amidohydrolase and EC 3.5.1.15, aspartoacylase.
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
aminoacylase iii, n-acyl-aromatic-l-amino acid amidohydrolase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)
This enzyme is found in animals and is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). It preferentially deacetylates Nalpha-acetylated aromatic amino acids and mercapturic acids (S-conjugates of N-acetyl-L-cysteine) that are usually not deacetylated by EC 3.5.1.14, N-acyl-aliphatic-L-amino acid amidohydrolase. The enzyme is significantly activated by Co2+ and Ni2+ [3]. Some bacterial aminoacylases demonstrate substrate specificity for both EC 3.5.1.14 and EC 3.5.1.114. cf. EC 3.5.1.14, N-acyl-aliphatic-L-amino acid amidohydrolase and EC 3.5.1.15, aspartoacylase.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
N-acetyl-1,2-dichlorovinyl-L-cysteine + H2O
acetate + 1,2-dichlorovinyl-L-cysteine
-
-
-
?
N-acetyl-S-(1,2-dichlorovinyl)-L-cysteine + H2O
acetate + S-(1,2-dichlorovinyl)-L-cysteine
-
-
-
?
Nalpha-acetylated peptide + H2O
acetate + peptide
N-terminal peptides derived from hepatitis C virus core protein
-
-
?
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
-
-
-
-
?
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
-
-
?
additional information
?
-
-
no activity with N-acetyl-L-cysteine, N-acetyl-L-aspartic acid and Nepsilon-acetyl-L-lysine
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Nalpha-acetylated peptide + H2O
acetate + peptide
N-terminal peptides derived from hepatitis C virus core protein
-
-
?
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Ni2+
Co2+ and to a lesser extent Ni2+ increases activity several times in comparison with intact wild type AA3. Co2+ drastically increases the rate of deacetylation of N-acetyl-1,2-dichlorovinyl-L-cysteine and significantly increased the toxicity of Ac-DCVC in the HEK293T cells expressing wt-AA3. Aminoacylase 3 is a metalloenzyme significantly activated by Co2+ and Ni2+
Zn2+
Wild type mouse aminoacylase 3 expressed in Escherichia coli contains 0.35 zinc atoms per monomer
additional information
Co2+
Co2+ and to a lesser extent Ni2+ increases activity several times in comparison with intact wild type AA3. Co2+ drastically increases the rate of deacetylation of N-acetyl-1,2-dichlorovinyl-L-cysteine and significantly increased the toxicity of Ac-DCVC in the HEK293T cells expressing wt-AA3. Aminoacylase 3 is a metalloenzyme significantly activated by Co2+ and Ni2+. The Co2+ -activated enzyme contains about 1 cobalt atom per monomer and trace amounts of zinc and other metals indicating that cobalt completely replaces them from the enzyme
additional information
Mn2+, Fe2+, Cd2+, Mg2+, Ca2+, K+ and Na+ do not significantly alter activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
trichloroethylene is one of the most widespread environmental contaminants, which is metabolized to N-acetyl-S-1,2-dichlorovinyl-L-cysteine (NA-DCVC) before being excreted in the urine. Alternatively, NA-DCVC can be deacetylated by aminoacylase 3, an enzyme that is highly expressed in the kidney, liver, and brain. NA-DCVC deacetylation initiates the transformation into toxic products that ultimately causes acute renal failure. Aminoacylase 3 inhibition is therefore a target of interest to prevent TCE induced nephrotoxicity
-
additional information
the enzyme is a metalloenzyme that is inactivated by metal chelating compounds. Molecular docking, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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+
1.3
N-acetyl-S-(1,2-dichlorovinyl)-L-cysteine
pH and temperature not specified in the publication, absence of Co2+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.27
4-hydroxy-2-nonenal mercapturate
pH and temperature not specified in the publication, absence of Co2+
1.67
4-hydroxy-2-nonenal mercapturate
pH and temperature not specified in the publication, presence of Co2+
0.4
acrolein mercapturate
pH and temperature not specified in the publication, absence of Co2+
3.03
acrolein mercapturate
pH and temperature not specified in the publication, presence of Co2+
0.28
N-acetyl-L-tyrosine
pH and temperature not specified in the publication, absence of Co2+
2.28
N-acetyl-L-tyrosine
pH and temperature not specified in the publication, presence of Co2+
0.13
N-acetyl-S-(1,2-dichlorovinyl)-L-cysteine
pH and temperature not specified in the publication, absence of Co2+
1.09
N-acetyl-S-(1,2-dichlorovinyl)-L-cysteine
pH and temperature not specified in the publication, presence of Co2+
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.35
4-hydroxy-2-nonenal mercapturate
pH and temperature not specified in the publication, absence of Co2+
3.15
4-hydroxy-2-nonenal mercapturate
pH and temperature not specified in the publication, presence of Co2+
0.49
acrolein mercapturate
pH and temperature not specified in the publication, absence of Co2+
4.27
acrolein mercapturate
pH and temperature not specified in the publication, presence of Co2+
0.62
N-acetyl-L-tyrosine
pH and temperature not specified in the publication, absence of Co2+
7.6
N-acetyl-L-tyrosine
pH and temperature not specified in the publication, presence of Co2+
0.1
N-acetyl-S-(1,2-dichlorovinyl)-L-cysteine
pH and temperature not specified in the publication, absence of Co2+
1.93
N-acetyl-S-(1,2-dichlorovinyl)-L-cysteine
pH and temperature not specified in the publication, presence of Co2+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
the enzyme is expressed predominantly in kidney, localized predominantly to the apical domain of S1 proximal tubules and the cytoplasm of S2 and S3 proximal tubules. The data suggest that in kidney proximal tubules, aminoacylase III plays an important role in deacetylating mercapturic acids
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
aminoacylase 3 inhibition completely protects rat brain cortex neurons expressing the enzyme from the toxicity of 4-hydroxy-2-nonenal-mercapturate. 4-hydroxy-2-nonenal-cysteine is also neurotoxic and its toxicity is mostly prevented by a beta-lyase inhibitor, aminooxyacetate
physiological function
physiological function
-
the enzyme mediates deacetylation of the mercapturic acids derived from the metabolism of trichloroethylene in the proximal tubule cells, and this process is involved in their toxicity
physiological function
aminoacylase III contributes to the nephrotoxicity to cysteine S-conjugates
physiological function
the enzyme cleaves the conjugates 4-hydroxy-2-nonenal mercapturate and acrolein mercapturate formed by reaction with glutathione for detoxification in the GSH-conjugation pathway, overview. Aminoacylase 3 is involved in the neurotoxicity of the compounds 4-hydroxy-2-nonenal and acrolein
physiological function
the enzyme mediates deacetylation of N-acetyl aromatic amino acids and mercapturic acids. Deacetylation of mercapturic acids of exo- and endobiotics are likely involved in their toxicity
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ACY3_MOUSE
318
0
35286
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35000
4 * 35000, the monomers of the enzyme are arranged with a fourfold rotational symmetry, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
tetramer
4 * 35000, the monomers of the enzyme are arranged with a fourfold rotational symmetry, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme has consensus sites for N-glycosylation (Asn70 and Asn117), tyrosine sulfation (Tyr88, Tyr165, and Tyr272), protein kinase C (Thr298), and casein kinase II (Thr83, Ser130, Ser160, Thr201, and Ser266) phosphorylation, and myristylation (Gly18, Gly19, Gly22, Gly27, and Gly185)
additional information
-
the enzyme has consensus sites for N-glycosylation (Asn70 and Asn117), tyrosine sulfation (Tyr88, Tyr165, and Tyr272), protein kinase C (Thr298), and casein kinase II (Thr83, Ser130, Ser160, Thr201, and Ser266) phosphorylation, and myristylation (Gly18, Gly19, Gly22, Gly27, and Gly185)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of recombinant mouse AA3 (mAA3) in the presence of its acetate byproduct and two substrates: Nalpha-acetyl-L-tyrosine and N-acetyl-S-1,2-dichlorovinyl-L-cysteine
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of His6-tagged enzyme in Escherichia coli, recombinant expression of N-terminally Strep(II)-tagged enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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)
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)
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
Homo sapiens (Q96HD9), Mus musculus (Q91XE4), Rattus norvegicus (Q5M876), Rattus norvegicus Wistar (Q5M876)
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