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Information on EC 3.5.1.14 - N-acyl-aliphatic-L-amino acid amidohydrolase and Organism(s) Mus musculus and UniProt Accession Q99JW2

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IUBMB Comments
Contains Zn2+. The enzyme is found in animals and is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). It acts on mercapturic acids (S-conjugates of N-acetyl-L-cysteine) and neutral aliphatic N-acyl-alpha-amino acids. Some bacterial aminoacylases demonstrate substrate specificity of both EC 3.5.1.14 and EC 3.5.1.114. cf. EC 3.5.1.15, aspartoacylase and EC 3.5.1.114, N-acyl-aromatic-L-amino acid amidohydrolase.
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Mus musculus
UNIPROT: Q99JW2
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The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
aminoacylase, acylase i, acy-1, aminoacylase i, aminoacylase 1, aminoacylase-1, l-aminoacylase, l-acy-1, aaiii, pacy1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acy1
-
-
acylase
-
-
-
-
acylase I
-
-
-
-
alpha-N-acylaminoacid hydrolase
-
-
-
-
amido acid deacylase
-
-
-
-
aminoacylase 1
-
-
aminoacylase 3
-
-
aminoacylase I
-
-
-
-
benzamidase
-
-
-
-
dehydropeptidase II
-
-
-
-
hippurase
-
-
-
-
hippuricase
-
-
-
-
histozyme
-
-
-
-
L-amido-acid acylase
-
-
-
-
L-aminoacylase
-
-
-
-
long acyl amidoacylase
-
-
-
-
N-acyl-L-amino-acid amidohydrolase
-
-
-
-
short acyl amidoacylase
-
-
-
-
sphingosine kinase 1-interacting protein
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of N-acetylated amino acids
deacylation
-
-
-
-
hydrolysis of amide bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
N-acyl-aliphatic-L-amino acid amidohydrolase (carboxylate-forming)
Contains Zn2+. The enzyme is found in animals and is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). It acts on mercapturic acids (S-conjugates of N-acetyl-L-cysteine) and neutral aliphatic N-acyl-alpha-amino acids. Some bacterial aminoacylases demonstrate substrate specificity of both EC 3.5.1.14 and EC 3.5.1.114. cf. EC 3.5.1.15, aspartoacylase and EC 3.5.1.114, N-acyl-aromatic-L-amino acid amidohydrolase.
CAS REGISTRY NUMBER
COMMENTARY hide
9012-37-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-acetyl-L-histidine + H2O
acetate + L-histidine
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
N-acetyl-S-(4-chlorobenzyl)-L-cysteine + H2O
acetate + S-(4-chlorobenzyl)-L-cysteine
show the reaction diagram
-
-
-
?
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
N-alpha-acetyl-L-lysine + H2O
acetate + L-lysine
show the reaction diagram
-
-
-
?
N-acetyl-1,2-dichlorovinyl-L-cysteine + H2O
acetate + 1,2-dichlorovinyl-L-cysteine
show the reaction diagram
-
a metabolite of a xenobiotic trichloroethylene, substrate of AA3
-
-
?
N-acetyl-L-aspartate + H2O
acetate + L-aspartate
show the reaction diagram
-
no activity of wild type protein, mutant E167R protein shows activity
-
-
?
N-acetyl-L-tyrosine + H2O
acetate + L-tyrosine
show the reaction diagram
-
-
-
-
?
N-acetyl-S-1,2-dichlorovinyl-L-cysteine + H2O
acetate + S-1,2-dichlorovinyl-L-cysteine
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N-acetyl-1,2-dichlorovinyl-L-cysteine + H2O
acetate + 1,2-dichlorovinyl-L-cysteine
show the reaction diagram
-
a metabolite of a xenobiotic trichloroethylene, substrate of AA3
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
three-dimensional modelling of Co2+ binding structure. AA3 is a metalloenzyme significantly activated by Co2+ and Ni2+. Cobalt increases the Vmax several times and decreases the Km of wild-type AA3. Co2+ can substitute for zinc ions in AA1 without a substantial loss of activity. Wild-type mouse AA3 expressed in Escherichia coli does not contain cobalt
Mn2+
-
Mn2+ can substitute for zinc ions in AA1 without a substantial loss of activity
Ni2+
-
AA3 is a metalloenzyme significantly activated by Co2+ and Ni2+
Zn2+
-
AA1 is a Zn2+ -metalloprotein containing stoichiometric amounts of this metal per monomer. Recombinant AA3 expressed in Escherichia coli contains 0.35 zinc atoms per monomer, but Zn2+ does not affect AA3 activity
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
PCMB
inhibits murine AAIII
L-benzylsuccinate
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
DTT
activates murine AAIII
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.8
N-acetyl-L-histidine
37°C, pH 7.5
1.6
N-acetyl-L-phenylalanine
37°C, pH 7.5
1.2
N-acetyl-L-tryptophan
37°C, pH 7.5
1.4
N-acetyl-L-tyrosine
37°C, pH 7.5
0.25
N-acetyl-S-(1,1,2,2-tetrafluoroethyl)-L-cysteine
37°C, pH 7.5
1.2
N-acetyl-S-(1,2,2-trichlorovinyl)-L-cysteine
37°C, pH 7.5
1
N-acetyl-S-(1,2,3,4,4-pentachlorobutadienyl)-L-cysteine
37°C, pH 7.5
0.9
N-acetyl-S-(1,2-dichlorovinyl)-L-cysteine
37°C, pH 7.5
5.3
N-acetyl-S-(2,2-dichloro-1,1-difluoroethyl)-L-cysteine
37°C, pH 7.5
0.4
N-acetyl-S-(2,2-dichlorovinyl)-L-cysteine
37°C, pH 7.5
0.3
N-acetyl-S-(2,2-difluoro-1,1-dichloroethyl)-L-cysteine
37°C, pH 7.5
0.28
N-acetyl-S-(2-chloro-1,1,2-trifluoroethyl)-L-cysteine
37°C, pH 7.5
1.45
N-acetyl-S-(2-chlorobenzyl)-L-cysteine
37°C, pH 7.5
1.3
N-acetyl-S-(2-fluorobenzyl)-L-cysteine
37°C, pH 7.5
0.6
N-acetyl-S-(3-fluorobenzyl)-L-cysteine
37°C, pH 7.5
0.5
N-acetyl-S-(4-bromobenzyl)-L-cysteine
37°C, pH 7.5
0.3
N-acetyl-S-(4-chlorobenzyl)-L-cysteine
37°C, pH 7.5
0.8
N-acetyl-S-(4-methoxybenzyl)-L-cysteine
37°C, pH 7.5
1.1
N-acetyl-S-benzyl-L-cysteine
37°C, pH 7.5
1.3
N-alpha-acetyl-L-lysine
37°C, pH 7.5
additional information
additional information
-
kinetics of wild-type AA3 in presnece of different metal ions, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
N-acetyl-L-aspartate
-
E167R mutant protein, pH not specified in the publication, temperature not specified in the publication
0.6
N-acetyl-L-tyrosine
-
E167R mutant protein, pH not specified in the publication, temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025
L-benzylsuccinate
-
pH not specified in the publication, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11.7
activity of the tetramer toward S-benzyl-N-acetyl-L-cysteine
9.4
activity of the dimer toward S-benzyl-N-acetyl-L-cysteine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 7.7
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
high expression level of AA1 and AA3
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACY1_MOUSE
408
0
45781
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
140000
expressed in HEK293T cells
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion technique
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D68A
-
site-directed mutagenesis of AA3, the mutant is inactive
E167R
-
involved in substrate specificity
E177A
E177D
-
reduces the kcat value more than threefold
E24A
-
site-directed mutagenesis of AA3, metal content and activity compared to the wild-type enzyme, overview
H116A
-
site-directed mutagenesis of AA3, metal content and activity compared to the wild-type enzyme, overview
H21A
-
site-directed mutagenesis of AA3, metal content and activity compared to the wild-type enzyme, overview
H21D
-
site-directed mutagenesis of AA3, metal content and activity compared to the wild-type enzyme, overview
N70A
-
site-directed mutagenesis of AA3, the mutant is active
R63A
-
site-directed mutagenesis of AA3, the mutant is inactive
R71A
-
site-directed mutagenesis of AA3, the mutant is active
Y287A
-
site-directed mutagenesis of AA3, the mutant is inactive
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged C-terminal fragment from an in vitro expression system by glutathione affinity chromatography
-
StrepTactin Sepharose
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in HEK293T cells
cloning of Acy1 from a mouse kidney library, expression of the C-terminal fragment in HEK-293 cells, in vitro expression of the GST-tagged C-terminal fragment, expression as myc-tagged enzyme in Cos-7 cells, expression with murine sphingosine kinase type 1, SphK1, in a yeast two-hybrid system
-
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Maceyka, M.; Nava, V.E.; Milstien, S.; Spiegel, S.
Aminoacylase 1 is a sphingosine kinase 1-interacting protein
FEBS Lett.
568
30-34
2004
Mus musculus
Manually annotated by BRENDA team
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 (Q99JW2), Mus musculus
Manually annotated by BRENDA team
Ryazantsev, S.; Abuladze, N.; Newman, D.; Bondar, G.; Kurtz, I.; Pushkin, A.
Structural characterization of dimeric murine aminoacylase III
FEBS Lett.
581
1898-1902
2007
Mus musculus (Q99JW2), Mus musculus
Manually annotated by BRENDA team
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
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team