Information on EC 3.5.1.114 - N-acyl-aromatic-L-amino acid amidohydrolase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.5.1.114
-
RECOMMENDED NAME
GeneOntology No.
N-acyl-aromatic-L-amino acid amidohydrolase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an N-acetyl-L-cysteine-S-conjugate + H2O = an L-cysteine-S-conjugate + acetate
show the reaction diagram
(2)
-
-
-
an N-acyl-aromatic-L-amino acid + H2O = an aromatic-L-amino acid + a carboxylate
show the reaction diagram
-
-
-
-
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-hydroxy-2-nonenal mercapturate + H2O
?
show the reaction diagram
acrolein mercapturate + H2O
?
show the reaction diagram
N-acetyl-1,2-dichlorovinyl-L-cysteine + H2O
acetate + 1,2-dichlorovinyl-L-cysteine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-histidine + H2O
acetate + L-histidine
show the reaction diagram
N-acetyl-L-lysine + H2O
acetate + L-lysine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-phenylalanine + H2O
acetate + L-phenylalanine
show the reaction diagram
N-acetyl-L-tryptophan + H2O
acetate + L-tryptophan
show the reaction diagram
-
-
-
-
?
N-acetyl-L-tyrosine + H2O
acetate + L-tyrosine
show the reaction diagram
N-acetyl-S-(1,1,2,2-tetrafluoroethyl)-L-cysteine + H2O
acetate + S-(1,1,2,2-tetrafluoroethyl)-L-cysteine
show the reaction diagram
-
-
-
-
?
N-acetyl-S-(1,2,2-trichlorovinyl)-L-cysteine + H2O
acetate + S-(1,2,2-trichlorovinyl)-L-cysteine
show the reaction diagram
-
-
-
-
?
N-acetyl-S-(1,2,3,4,4-pentachlorobutadienyl)-L-cysteine + H2O
acetate + S-(1,2,3,4,4-pentachlorobutadienyl)-L-cysteine
show the reaction diagram
-
good substrate
-
-
?
N-acetyl-S-(1,2-dichlorovinyl)-L-cysteine + H2O
acetate + S-(1,2-dichlorovinyl)-L-cysteine
show the reaction diagram
N-acetyl-S-(2,2-dichloro-1,1-difluoroethyl)-L-cysteine + H2O
acetate + S-(2,2-dichloro-1,1-difluoroethyl)-L-cysteine
show the reaction diagram
-
-
-
-
?
N-acetyl-S-(2,2-dichlorovinyl)-L-cysteine + H2O
acetate + S-(2,2-dichlorovinyl)-L-cysteine
show the reaction diagram
-
good substrate
-
-
?
N-acetyl-S-(2,2-difluoro-1,1-dichloroethyl)-L-cysteine + H2O
acetate + S-(2,2-difluoro-1,1-dichloroethyl)-L-cysteine
show the reaction diagram
-
-
-
-
?
N-acetyl-S-(2-chloro-1,1,2-trifluoroethyl)-L-cysteine + H2O
acetate + S-(2-chloro-1,1,2-trifluoroethyl)-L-cysteine
show the reaction diagram
-
-
-
-
?
N-acetyl-S-(2-chlorobenzyl)-L-cysteine + H2O
acetate + S-(2-chlorobenzyl)-L-cysteine
show the reaction diagram
-
-
-
-
?
N-acetyl-S-(2-fluorobenzyl)-L-cysteine + H2O
acetate + S-(2-fluorobenzyl)-L-cysteine
show the reaction diagram
-
-
-
-
?
N-acetyl-S-(3-fluorobenzyl)-L-cysteine + H2O
acetate + S-(3-fluorobenzyl)-L-cysteine
show the reaction diagram
-
-
-
-
?
N-acetyl-S-(4-bromobenzyl)-L-cysteine + H2O
acetate + S-(4-bromobenzyl)-L-cysteine
show the reaction diagram
-
good substrate
-
-
?
N-acetyl-S-(4-chlorobenzyl)-L-cysteine + H2O
acetate + S-(4-chlorobenzyl)-L-cysteine
show the reaction diagram
-
good substrate
-
-
?
N-acetyl-S-(4-methoxybenzyl)-L-cysteine + H2O
acetate + S-(4-methoxybenzyl)-L-cysteine
show the reaction diagram
-
-
-
-
?
N-acetyl-S-benzyl-L-cysteine + H2O
acetate + S-benzyl-L-cysteine
show the reaction diagram
Nalpha-acetylated peptide + H2O
acetate + peptide
show the reaction diagram
-
N-terminal peptides derived from hepatitis C virus core protein
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Nalpha-acetylated peptide + H2O
acetate + peptide
show the reaction diagram
-
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
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-((E)-[(4H-1,2,4-triazol-4-yl)imino]methyl)-1-benzothiophene-3-ol
-
-
2-(4-ethoxyphenyl)-2-methylsuccinic acid
-
2-([(3-fluoro-4-methoxyphenyl)methyl]sulfanyl)-1-methyl-1H-benzimidazole-5-sulfonamide
-
-
2-([2-chloro-4-(thiocyanato)phenyl]carbamoyl)benzoic acid
-
-
2-[(1,3-benzothiazol-2-yl)sulfanyl]ethan-1-amine
-
ebselen
Ibuprofen
Q91XEY
-
N-(2,3,5-trichloro-4-oxocyclohexa-2,5-dien-1-ylidene)benzenesulfonamide
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
1.8
N-acetyl-L-histidine
-
pH 7.5, 37°C
1.3
N-acetyl-L-lysine
-
pH 7.5, 37°C
1.6
N-acetyl-L-phenylalanine
-
pH 7.5, 37°C
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
-
pH 7.5, 37°C
additional information
additional information
Q91XEY
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.27 - 1.67
4-hydroxy-2-nonenal mercapturate
-
0.4 - 3.03
acrolein mercapturate
-
0.28 - 2.28
N-acetyl-L-tyrosine
0.13 - 1.09
N-acetyl-S-(1,2-dichlorovinyl)-L-cysteine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.35 - 3.15
4-hydroxy-2-nonenal mercapturate
206930
0.49 - 4.27
acrolein mercapturate
206931
0.62 - 7.6
N-acetyl-L-tyrosine
1840
0.1 - 1.93
N-acetyl-S-(1,2-dichlorovinyl)-L-cysteine
37284
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.063
2-((E)-[(4H-1,2,4-triazol-4-yl)imino]methyl)-1-benzothiophene-3-ol
Rattus norvegicus
Q5M876
pH and temperature not specified in the publication
-
0.00000063
2-(4-ethoxyphenyl)-2-methylsuccinic acid
Rattus norvegicus
Q5M876
pH and temperature not specified in the publication
-
0.000079
2-([(3-fluoro-4-methoxyphenyl)methyl]sulfanyl)-1-methyl-1H-benzimidazole-5-sulfonamide
Rattus norvegicus
Q5M876
pH and temperature not specified in the publication
-
0.00004
2-([2-chloro-4-(thiocyanato)phenyl]carbamoyl)benzoic acid
Rattus norvegicus
Q5M876
pH and temperature not specified in the publication
-
0.0016
2-[(1,3-benzothiazol-2-yl)sulfanyl]ethan-1-amine
Rattus norvegicus
Q5M876
pH and temperature not specified in the publication
0.0101
clioquinol
Rattus norvegicus
Q5M876
pH and temperature not specified in the publication
10
ebselen
Rattus norvegicus
Q5M876
pH and temperature not specified in the publication
0.0000032
N-(2,3,5-trichloro-4-oxocyclohexa-2,5-dien-1-ylidene)benzenesulfonamide
Rattus norvegicus
Q5M876
pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 7.7
-
in 50 mM Na-phosphate buffer
7.6
-
substrate: N-acetyl-L-histidine or N-acetyl-L-tyrosine
7.7
-
substrate: N-acetyl-L-phenylalanine
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
lower expression level
Manually annotated by BRENDA team
-
less expression
Manually annotated by BRENDA team
-
less expression
Manually annotated by BRENDA team
-
less expression
Manually annotated by BRENDA team
-
less expression
Manually annotated by BRENDA team
-
less expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
-
4 * 35000, the monomers of the enzyme are arranged with a fourfold rotational symmetry, SDS-PAGE
35188
-
4 * 35188, calculated from sequence
140000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli to homogeneity
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in HEK-293T cells; expression in HEK-293 cells
-
expression in Escherichia coli
-
recombinant expression of His6-tagged enzyme in Escherichia coli, recombinant expression of N-terminally Strep(II)-tagged enzyme
-
recombinant expression of the enzyme in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D68A
-
inactive mutant enzyme
E177A
-
inactive mutant enzyme
E24A
-
inactive mutant enzyme
H116A
-
inactive mutant enzyme
H21A
-
inactive mutant enzyme
R63A
-
inactive mutant enzyme
Y287A
-
inactive mutant enzyme