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Information on EC 3.5.1.14 - N-acyl-aliphatic-L-amino acid amidohydrolase and Organism(s) Homo sapiens and UniProt Accession Q03154
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3.5.1.14 N-acyl-aliphatic-L-amino acid amidohydrolaseIUBMB 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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Word Map
- 3.5.1.14
-
n-acetylated
- synthesis
- n-acetyl-l-methionine
-
mercapturic
- acylases
-
cobalt-activated
- medicine
- diagnostics
- analysis
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
aminoacylase, acylase i, acy-1, aminoacylase i, aminoacylase 1, aminoacylase-1, l-aminoacylase, l-acy-1, aaiii, pacy1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acylase
-
-
-
-
acylase I
-
-
-
-
alpha-N-acylaminoacid hydrolase
-
-
-
-
amido acid deacylase
-
-
-
-
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
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an N-acyl-aliphatic-L-amino acid + H2O = an aliphatic L-amino acid + a carboxylate
active site structure, catalysis involves residues H206, N263, R276, and D274, the dimerization domain residues play important roles in binding and catalysis, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of N-acetylated amino acids
deacylation
-
-
-
-
hydrolysis of amide bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
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
9012-37-7
-
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
N-2,2-dimethylpropionyl-L-methionine + H2O
2,2-dimethyl-propionate + L-methionine
-
-
-
?
2-acetylamino-3-((1S,2S)-2-hydroxycyclohexylsulfanyl)-propionic acid + H2O
S-[(1S,2S)-2-hydroxycyclohexyl]cysteine + acetate
-
-
-
-
?
2-acetylamino-3-((3S,4S)-3-hydroxy-2,2-dimethyl-chroman-4-ylsulfanyl)-propionic acid + H2O
S-[(3S,4S)-3-hydroxy-2,2-dimethyl-3,4-dihydro-2H-chromen-4-yl]cysteine + acetate
-
-
-
-
?
2-acetylamino-3-[(S)-1-((R)-hydroxyphenyl-methyl)-2-oxo-2-phenyl-ethylsulfanyl]-propionic acid + H2O
S-[(1R,2R)-1-hydroxy-3-oxo-1,3-diphenylpropan-2-yl]cysteine + acetate
-
-
-
-
?
N-acetyl-1,2-dichlorovinyl-L-cysteine + H2O
acetate + 1,2-dichlorovinyl-L-cysteine
-
a metabolite of a xenobiotic trichloroethylene, substrate of AA3
-
-
?
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
N-acetyl-1,2-dichlorovinyl-L-cysteine + H2O
acetate + 1,2-dichlorovinyl-L-cysteine
-
a metabolite of a xenobiotic trichloroethylene, substrate of AA3
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
additional information
-
metal removal completely inactivates AA3, whereas addition of Zn2+, Mn2+ or Fe2+ restores initial activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-[(E)-2-[7-(diethylamino)-2-oxo-2H-1-benzopyran-3-yl]ethenyl]phenyl prop-2-enoate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
168
N-2,2-dimethylpropionyl-L-methionine
hydrolysis of N-acyl-L-methionine substrates by hAcy1
0.73
N-butanoyl-L-methionine
hydrolysis of N-acyl-L-methionine substrates by hAcy1
7.18
N-cyclopentanoyl-L-methionine
hydrolysis of N-acyl-L-methionine substrates by hAcy1
16.8
N-formyl-L-methionine
hydrolysis of N-acyl-L-methionine substrates by hAcy1
15.3
N-isobutanoyl-L-methionine
hydrolysis of N-acyl-L-methionine substrates by hAcy1
0.19
N-pentanoyl-L-methionine
hydrolysis of N-acyl-L-methionine substrates by hAcy1
0.34
N-propionyl-L-methionine
hydrolysis of N-acyl-L-methionine substrates by hAcy1
0.2
2-acetylamino-3-((1S,2S)-2-hydroxy-2,2-dimethyl-chroman-4-ylsulfanyl)-propionic acid
-
analysis by HPLC, pH 7.6, 37°C
0.5
2-acetylamino-3-((1S,2S)-2-hydroxycyclohexylsulfanyl)-propionic acid
-
analysis by HPLC, pH 7.6, 37°C
0.3
2-acetylamino-3-[(S)-1-((R)-hydroxyphenyl-methyl)-2-oxo-2-phenyl-ethylsulfanyl]-propionic acid
-
analysis by HPLC, pH 7.6, 37°C
additional information
additional information
-
steady-state kinetics of wild-type and mutant enzymes, kinetics of mutants N263D, R276N, and R276Q are not measurable
-
63
N-acetyl-L-glutamate
hydrolysis of N-acetyl-L-glutamate substrates by wild-type human Acy1
70
N-acetyl-L-glutamate
hydrolysis of N-acetyl-L-glutamate substrates by wild-type human Acy1
0.4
N-acetyl-L-methionine
hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-T347S-mutant
0.43
N-acetyl-L-methionine
hydrolysis of N-acyl-L-methionine substrates by hAcy1
0.76
N-acetyl-L-methionine
hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-T347F-mutant
1.14
N-acetyl-L-methionine
hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-I177A-mutant
1.35
N-acetyl-L-methionine
hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-L372I-mutant
1.72
N-acetyl-L-methionine
hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-I177L-mutant
2.76
N-acetyl-L-methionine
hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-L372V-mutant
2.78
N-acetyl-L-methionine
hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-T347G-mutant
4.32
N-acetyl-L-methionine
hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-L372G-mutant
0.41
N-benzoyl-L-methionine
hydrolysis of N-acetyl-L-methionine substrates by wild-type human Acy1
0.81
N-benzoyl-L-methionine
hydrolysis of N-acetyl-L-methionine substrates by wild-type human Acy1
1.63
N-benzoyl-L-methionine
hydrolysis of N-acetyl-L-glutamate substrates by wild-type human Acy1
1.17
N-cyclohexanoyl-L-methionine
hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-T347S-mutant
6.23
N-cyclohexanoyl-L-methionine
hydrolysis of N-acyl-L-methionine substrates by hAcy1
1.01
N-hexanoyl-L-methionine
hydrolysis of N-acyl-L-methionine substrates by hAcy1
3.56
N-hexanoyl-L-methionine
hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-I177A-mutant
5.22
N-hexanoyl-L-methionine
hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-I177L-mutant
0.54
N-isopentanoyl-L-methionine
hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-L372V-mutant
2.1
N-isopentanoyl-L-methionine
hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-L372A-mutant
4.27
N-isopentanoyl-L-methionine
hydrolysis of N-acyl-L-methionine substrates by hAcy1
7.29
N-isopentanoyl-L-methionine
hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-L372I-mutant
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0015
N-2,2-dimethylpropionyl-L-methionine
kcat for the hydrolysis of N-acyl-L-methionine substrates by hAcy1
0.0101
N-benzoyl-L-glutamate
kcat for the hydrolysis of N-acyl-L-glutamate substrates by hAcy1
139
N-butanoyl-L-methionine
kcat for the hydrolysis of N-acyl-L-methionine substrates by hAcy1
13.3
N-cyclopentanoyl-L-methionine
kcat the hydrolysis of N-acyl-L-methionine substrates by hAcy1
177
N-formyl-L-methionine
kcat for the hydrolysis of N-acyl-L-methionine substrates by hAcy1
16.2
N-pentanoyl-L-methionine
kcat for the hydrolysis of N-acyl-L-methionine substrates by hAcy1
25.7
N-propionyl-L-methionine
kcat for the hydrolysis of N-acyl-L-methionine substrates by hAcy1
150
2-acetylamino-3-((1S,2S)-2-hydroxy-2,2-dimethyl-chroman-4-ylsulfanyl)-propionic acid
-
analysis by HPLC, pH 7.6, 37°C
120
2-acetylamino-3-((1S,2S)-2-hydroxycyclohexylsulfanyl)-propionic acid
-
analysis by HPLC, pH 7.6, 37°C
80
2-acetylamino-3-[(S)-1-((R)-hydroxyphenyl-methyl)-2-oxo-2-phenyl-ethylsulfanyl]-propionic acid
-
analysis by HPLC, pH 7.6, 37°C
additional information
additional information
-
kinetics of mutants N263D, R276N, and R276Q are not measurable
-
63.4
N-acetyl-L-glutamate
kcat for the hydrolysis of N-acyl-L-glutamate substrates by hAcy1-T347S-mutant
120
N-acetyl-L-glutamate
kcat for the hydrolysis of N-acyl-L-glutamate substrates by hAcy1-T347S-mutant
156
N-acetyl-L-glutamate
kcat for the hydrolysis of N-acyl-L-glutamate substrates by hAcy1
1.2
N-acetyl-L-methionine
kcat for the hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-T347F-mutant
4.49
N-acetyl-L-methionine
kcat for the hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-L372I-mutant
12.1
N-acetyl-L-methionine
kcat for the hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-L372V-mutant
16.6
N-acetyl-L-methionine
kcat for the hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-L372G-mutant
38.3
N-acetyl-L-methionine
kcat for the hydrolysis of N-acyl-L-methionine substrates by hAcy1
46
N-acetyl-L-methionine
kcat for the hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-T347G-mutant
64.6
N-acetyl-L-methionine
kcat for the hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-T347S-mutant
66.7
N-acetyl-L-methionine
kcat for the hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-I177A-mutant
93.7
N-acetyl-L-methionine
kcat for the hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-I177L-mutant
0.158
N-benzoyl-L-methionine
kcat for the hydrolysis of N-acyl-L-methionine substrates by hAcy1
20.1
N-benzoyl-L-methionine
kcat for the hydrolysis of N-acyl-L-methionine substrates by hAcy1-T347S-mutant
0.00623
N-cyclohexanoyl-L-methionine
kcat for the hydrolysis of N-acyl-L-methionine substrates by hAcy1
0.129
N-cyclohexanoyl-L-methionine
kcat for the hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-T347S-mutant
0.052 - 2.1
N-hexanoyl-L-methionine
kcat for the hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-I177A-mutant
9.51
N-hexanoyl-L-methionine
kcat for the hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-I177A-mutant
16.1
N-hexanoyl-L-methionine
kcat for the hydrolysis of N-acyl-L-methionine substrates by hAcy1
39.4
N-hexanoyl-L-methionine
kcat for the hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-I177L-mutant
0.529
N-isobutanoyl-L-methionine
kcat for the hydrolysis of N-acyl-L-methionine substrates by hAcy1
6.08
N-isobutanoyl-L-methionine
kcat for the hydrolysis of N-acyl-L-methionine substrates by hAcy1
0.105
N-isopentanoyl-L-methionine
kcat for the hydrolysis of N-acyl-L-methionine substrates by hAcy1
0.34
N-isopentanoyl-L-methionine
kcat for the hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-L372V-mutant
2.01
N-isopentanoyl-L-methionine
kcat for the hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-L372I-mutant
3.3
N-isopentanoyl-L-methionine
kcat for the hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-L372A-mutant
5.36
N-isopentanoyl-L-methionine
kcat for the hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-L372A-mutant
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
750
2-acetylamino-3-((1S,2S)-2-hydroxy-2,2-dimethyl-chroman-4-ylsulfanyl)-propionic acid
-
analysis by HPLC, pH 7.6, 37°C
240
2-acetylamino-3-((1S,2S)-2-hydroxycyclohexylsulfanyl)-propionic acid
-
analysis by HPLC, pH 7.6, 37°C
270
2-acetylamino-3-[(S)-1-((R)-hydroxyphenyl-methyl)-2-oxo-2-phenyl-ethylsulfanyl]-propionic acid
-
analysis by HPLC, pH 7.6, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
enzyme expression patterns in tumor cells, overview. No expression in stroma cells
additional information
-
enzyme expression patterns in tumor cells, overview. No expression in stroma cells
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
overexpression of aminoacylase 1 is associated with colorectal cancer progression. Enzyme knockdown inhibits cell proliferation and causes cell cycle perturbation
physiological function
the enzyme is responsible for amino acid deacylation during intracellular protein degradation, it is implicated in a number of human tumor types. Strong expression of the enzyme is significantly associated with more advanced TNM stage, lymph node metastasis, positive vascular invasion, and shorter cancer-specific survival
additional information
additional information
strong ACY1 immunoreactivity is an adverse prognostic indicator compared with combined negative and weak ACY 1 expression
additional information
-
strong ACY1 immunoreactivity is an adverse prognostic indicator compared with combined negative and weak ACY 1 expression
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). ACY1_HUMAN
408
0
45885
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
dimerization domain residues play important roles in binding and catalysis, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
I177A
I177L
L372A
2fold decreased KM-value compared to the wildtype with N-isopentanoyl-L-methionine
L372G
10fold increased KM-value compared to the wildtype with N-acetyl-L-methionine moiety
L372I
L372V
T347F
1.8fold increased KM-value compared to the wildtype with N-acetyl-L-methionine moiety
T347G
6.5fold increased KM-value compared to the wildtype with N-acetyl-L-methionine moiety
T347S
D274A
-
site-directed mutagenesis, the mutant shows 5695fold reduced activity compared to the wild-type enzyme, but the same expression and purification behaviour
H206A
-
site-directed mutagenesis, dimerization domain mutant, the mutant shows 560fold reduced activity compared to the wild-type enzyme, but the same expression and purification behaviour
H206K
-
site-directed mutagenesis, dimerization domain mutant, the mutant shows 348fold reduced activity compared to the wild-type enzyme, but the same expression and purification behaviour
H206N
-
site-directed mutagenesis, dimerization domain mutant, the mutant shows 11837fold reduced activity compared to the wild-type enzyme
N263D
-
site-directed mutagenesis, dimerization domain mutant, nearly inactive mutant showing the same expression and purification behaviour compared to the wild-type enzyme
N263S
-
site-directed mutagenesis, dimerization domain mutant, the mutant shows 152fold reduced activity compared to the wild-type enzyme, but the same expression and purification behaviour
R276A
-
site-directed mutagenesis, dimerization domain mutant, the mutant shows 8995fold reduced activity compared to the wild-type enzyme, but the same expression and purification behaviour
R276N
-
site-directed mutagenesis, dimerization domain mutant, nearly inactive mutant showing the same expression and purification behaviour compared to the wild-type enzyme
R276Q
-
site-directed mutagenesis, dimerization domain mutant, nearly inactive mutant showing the same expression and purification behaviour compared to the wild-type enzyme
additional information
I177A
2.7fold increased KM-value compared to the wildtype with N-acetyl-L-methionine moiety
I177A
3.5fold increased KM-value compared to the wildtype with N-hexanoyl-L-methionine moiety
I177L
4fold increased KM-value compared to the wildtype with N-acetyl-L-methionine moiety
I177L
5.2fold increased KM-value compared to the wildtype with N-hexanoyl-L-methionine moiety
L372I
1,7fold increased KM-value compared to the wildtype with N-isopentanoyl-L-methionine moiety
L372I
3.1fold increased KM-value compared to the wildtype with N-acetyl-L-methionine moiety
L372V
6.4fold increased KM-value compared to the wildtype with N-acetyl-L-methionine moiety
L372V
7.9fold decreased KM-value compared to the wildtype with N-isopentanoyl-L-methionine moiety
T347S
1.1fold decreased KM-value compared to the wildtype with N-acetyl-L-methionine moiety
T347S
5.3fold decreased KM-value compared to the wildtype with N-cyclohexanoyl-L-methionine moiety
additional information
enzyme expression silencing in HCT-116 cells using a small interfering RNA
additional information
-
enzyme expression silencing in HCT-116 cells using a small interfering RNA
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
the enzyme is an important biomarker with potential prognostic utility in patients with delayed graft function following renal transplantation. The possibility of using 4-[(E)-2-[7-(diethylamino)-2-oxo-2H-1-benzopyran-3-yl]ethenyl]phenyl prop-2-enoate for quantification of aminoacylase-1 in blood serum samples is explored. Nontoxic nature and cell membrane permeability are key features of this probe and are ideally suited for imaging intracellular Cys in normal and cancerous cell lines .CA can be used for selective detection of Cys in the presence of the competing biothiols, cations, and anions of biological relevance. This reagent is successfully utilized for monitoring the hydrolysis of an important commercial drug molecule N-acetyl-L-cysteine by an industrially and biologically important endogenous enzyme, aminoacylase-1
medicine
the enzyme is an important biomarker with potential prognostic utility in patients with delayed graft function following renal transplantation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sakanyan, V.; Desmarez, L.; Legrain, C.; Charlier, D.; Mett, I.; Kochikyan, A.; Savchenko, A.; Boyen, A.; Falmagne, P.; Pierard, A.; Glansdorff, N.
Gene cloning, sequence analysis, purification, and characterization of an thermostable aminoacylase from Bacillus stearothermophilus
Appl. Environ. Microbiol.
59
3878-3888
1993
Aspergillus oryzae, Bacillus sp. (in: Bacteria), Homo sapiens, Sus scrofa
Palm, G.J.; Roehm, K.H.
Aminoacylase I from porcine kidney: Identification and characterization of two major protein domains
J. Protein Chem.
14
233-240
1995
Homo sapiens, Sus scrofa
Uttamsingh, V.; Keller, D.A.; Anders, M.W.
Acylase I-catalyzed deacetylatin of N-acetyl-L-cysteine and S-alkyl-N-acetyl-L-cysteines
Chem. Res. Toxicol.
11
801-809
1998
Homo sapiens, Rattus norvegicus, Sus scrofa
Lindner, H.A.; Alary, A.; Boju, L.I.; Sulea, T.; Menard, R.
Roles of dimerization domain residues in binding and catalysis by aminoacylase-1
Biochemistry
44
15645-15651
2005
Homo sapiens
Lindner, H.A.; Alary, A.; Wilke, M.; Sulea, T.
Probing the acyl-binding pocket of aminoacylase-1
Biochemistry
47
4266-4275
2008
Sus scrofa, Homo sapiens (Q03154), Homo sapiens
Lindner, H.A.; Taefler-Naumann, M.; Roehm, K.H.
N-acetylamino acid utilization by kidney aminoacylase-1
Biochimie
90
773-780
2008
Homo sapiens (Q03154), Homo sapiens, Sus scrofa (P37111), Sus scrofa
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
Stocker, P.; Brunel, J.; de Rezende, L.; -do Amaral, A.; Morelli, X.; Roche, P.; Vidal, N.; Giardina, T.; Perrier, J.
Aminoacylase 1-catalysed deacetylation of bioactives epoxides mycotoxin-derived mercapturates; 3,4-epoxyprecocenes as models of cytotoxic epoxides
Biochimie
94
1668-1675
2012
Homo sapiens, Sus scrofa (P37111), Sus scrofa
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