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Information on EC 3.5.1.14 - N-acyl-aliphatic-L-amino acid amidohydrolase and Organism(s) Sus scrofa and UniProt Accession P37111
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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: Sus scrofa
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 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
2-acetylamino-3-((1S,2S)-2-hydroxycyclohexylsulfanyl)-propionic acid + H2O
S-[(1S,2S)-2-hydroxycyclohexyl]cysteine + acetate
-
-
-
?
2-acetylamino-3-((1S,2S)-2-hydroxycyclooctylsulfanyl)-propionic acid + H2O
S-[(1S,2S)-2-hydroxycyclooctyl]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
-
-
-
?
3-(2-furyl)acryloyl-L-methionine + H2O
3-(2-furyl)acrylate + L-methionine
-
-
-
?
(2-chloroacetamido)(phenyl)acetate + H2O
chloroacetate + amino(phenyl)acetate
-
-
-
-
?
chloracetyl-DL-aminoheptylic acid + H2O
chloroacetate + DL-aminoheptanoate
-
-
-
-
?
chloroacetyl-L-4-fluorophenylalanine + H2O
chloroacetate + L-4-fluorophenylalanine
-
-
-
-
?
chloroacetyl-L-4-methoxyphenylalanine + H2O
chloroacetate + L-4-methoxyphenylalanine
-
-
-
-
?
hydroxyacetyl-DL-alanine + H2O
hydroxyacetate + DL-alanine
-
isolated as the barium salt
-
-
?
methyl-mercaptoacetyl-DL-alanine + H2O
methylmercaptoacetate + DL-alanine
-
-
-
-
?
methylmercaptoacetyl-DL-phenylalanine + H2O
methylmercaptoacetate + DL-phenylalanine
-
-
-
-
?
N-2,2-dimethylpropionyl-L-methionine + H2O
2,2-dimethyl-propionate + L-methionine
-
-
-
-
?
N-acetyl-DL-aspartate + H2O
acetate + DL-aspartate
-
pure acylated D-forms hydrolyzed 10000-40000 times more slowly than corresponding pure acylated L-isomers
-
-
?
N-acetyl-DL-methionine + H2O
DL-methionine + acetate
-
-
288852, 288853, 288856, 288857, 288859, 288860, 288862, 288863, 288864, 288866, 288867, 288868, 288869, 288870, 288871, 288872, 288873, 288874
-
-
?
N-acetyl-L-alanine + H2O
L-alanine + acetate
-
-
-
-
?
N-acetyl-L-glutamine + H2O
L-glutamine + acetate
-
-
-
-
?
N-acetyl-L-methionine
L-methionine + acetate
-
-
288852, 288853, 288854, 288856, 288857, 288859, 288860, 288862, 288863, 288864, 288866, 288867, 288868, 288869, 288870, 288871, 288872, 288873, 288874
-
-
?
N-acetyl-L-phenylalanine + H2O
L-phenylalanine + acetate
-
-
-
-
?
N-acetyl-L-valine + H2O
L-valine + acetate
-
-
-
-
?
N-acetyl-O-benzyl-DL-serine + H2O
acetate + O-benzyl-DL-serine
-
no hydrolysis with immobilized enzyme
-
-
?
N-chloroacetyl-2-amino-2-cyclohexylacetate + H2O
chloroacetate + 2-amino-2-cyclohexylacetate
-
-
-
-
?
N-chloroacetyl-2-amino-3-cyclohexylpropionate + H2O
chloroacetate + 2-amino-3-cyclohexylpropionate
-
-
-
-
?
N-chloroacetyl-2-amino-4-cyclohexylbutyrate + H2O
chloroacetate + 2-amino-4-cyclohexylbutyrate
-
-
-
-
?
N-chloroacetyl-DL-norvaline + H2O
chloroacetate + DL-norvaline
-
N-acylated racemic amino acids, pure acylated D forms hydrolyzed 10000-40000 times more slowly than corresponding pure acylated L isomers
-
-
?
N-chloroacetyl-DL-phenylalanine + H2O
chloroacetate + phenylalanine
-
-
-
-
?
N-chloroacetyl-DL-valine + H2O
chloroacetate + DL-valine
-
-
-
-
?
N-chloroacetyl-L-leucine + H2O
chloroacetate + L-leucine
-
-
-
-
?
N-cyclohexanoyl-L-methionine + H2O
cyclohexanecarboxylate + L-methionine
-
-
-
-
?
N-cyclopentanoyl-L-methionine + H2O
cyclopentanecarboxylate + L-methionine
-
-
-
-
?
N-trifluoroacetyl 2-trifluoromethylalanine + H2O
trifluoroacetate + 2-trifluoromethylalanine
-
-
-
-
?
trifluoroacetyl-DL-alanine + H2O
trifluoroacetate + DL-alanine
-
trifluoroacetyl derivatives are most rapidly hydrolyzed
-
-
?
trifluoroacetyl-DL-phenylalanine + H2O
trifluoroacetate + DL-phenylalanine
-
-
-
-
?
additional information
?
-
pAcy1 catalyzes the highly stereoselective acylation of amino acids, a useful conversion for the preparation of optically pure N-acyl-L-amino acids, the catalytic base is E146. pAcy1 from pig kidney displays a marked preference for short-chain acyl moieties and non-branched aliphatic L-amino acids. Modeling of pAcy1 catalyzed N-acylation, overview
-
-
?
additional information
?
-
-
pAcy1 catalyzes the highly stereoselective acylation of amino acids, a useful conversion for the preparation of optically pure N-acyl-L-amino acids, the catalytic base is E146. pAcy1 from pig kidney displays a marked preference for short-chain acyl moieties and non-branched aliphatic L-amino acids. Modeling of pAcy1 catalyzed N-acylation, overview
-
-
?
additional information
?
-
-
the enzyme cataylzes high enantioselective reactions
-
-
?
additional information
?
-
-
the ability of the enzyme to discriminate between methyls and fluorinated methyls is limited. For example, there is no enantioselectivity in the enzymatic hydrolysis of N-trifluoroacetyl 2-fluoromethylalanine
-
-
-
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-L-methionine
L-methionine + acetate
-
-
288852, 288853, 288854, 288856, 288857, 288859, 288860, 288862, 288863, 288864, 288866, 288867, 288868, 288869, 288870, 288871, 288872, 288873, 288874
-
-
?
additional information
?
-
pAcy1 catalyzes the highly stereoselective acylation of amino acids, a useful conversion for the preparation of optically pure N-acyl-L-amino acids, the catalytic base is E146. pAcy1 from pig kidney displays a marked preference for short-chain acyl moieties and non-branched aliphatic L-amino acids. Modeling of pAcy1 catalyzed N-acylation, overview
-
-
?
additional information
?
-
-
pAcy1 catalyzes the highly stereoselective acylation of amino acids, a useful conversion for the preparation of optically pure N-acyl-L-amino acids, the catalytic base is E146. pAcy1 from pig kidney displays a marked preference for short-chain acyl moieties and non-branched aliphatic L-amino acids. Modeling of pAcy1 catalyzed N-acylation, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1 - 0.15
2-acetylamino-3-((1S,2S)-2-hydroxy-2,2-dimethyl-chroman-4-ylsulfanyl)-propionic acid
1
2-acetylamino-3-((3S,4S)-2-hydroxycyclooctylsulfanyl)-propionic acid
analysis by HPLC, pH 7.6, 37°C
0.2 - 0.4
2-acetylamino-3-[(S)-1-((R)-hydroxyphenyl-methyl)-2-oxo-2-phenyl-ethylsulfanyl]-propionic acid
585
N-2,2-dimethylpropionyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by pAcy1
102
N-acetyl-L-glutamate
-
hydrolysis of N-acetyl-L-glutamate substrates by Wild-Type porcine Acy1
3.71
N-benzoyl-L-glutamate
-
hydrolysis of N-acetyl-L-glutamate substrates by Wild-Type porcine Acy1
0.38
N-benzoyl-L-methionine
-
hydrolysis of N-acetyl-L-methionine substrates by Wild-Type porcine Acy1
0.31
N-butanoyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by pAcy1
0.31
N-cyclohexanoyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by pAcy1
0.64
N-cyclopentanoyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by pAcy1
0.01
N-hexanoyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by pAcy1
58.5
N-isobutanoyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by pAcy1
0.9
N-isopentanoyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by pAcy1
0.03
N-pentanoyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by pAcy1
0.55
N-propionyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by pAcy1
0.1
2-acetylamino-3-((1S,2S)-2-hydroxy-2,2-dimethyl-chroman-4-ylsulfanyl)-propionic acid
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37°C
0.15
2-acetylamino-3-((1S,2S)-2-hydroxy-2,2-dimethyl-chroman-4-ylsulfanyl)-propionic acid
analysis by HPLC, pH 7.6, 37°C
0.3
2-acetylamino-3-((1S,2S)-2-hydroxycyclohexylsulfanyl)-propionic acid
analysis by HPLC, pH 7.6, 37°C
0.5
2-acetylamino-3-((1S,2S)-2-hydroxycyclohexylsulfanyl)-propionic acid
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37°C
0.2
2-acetylamino-3-[(S)-1-((R)-hydroxyphenyl-methyl)-2-oxo-2-phenyl-ethylsulfanyl]-propionic acid
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37°C
0.4
2-acetylamino-3-[(S)-1-((R)-hydroxyphenyl-methyl)-2-oxo-2-phenyl-ethylsulfanyl]-propionic acid
analysis by HPLC, pH 7.6, 37°C
0.5
N-acetyl-L-Cys
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37°C
0.3
N-acetyl-L-Met
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37°C
0.5
N-acetyl-L-Val
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37°C
2.72
N-acetyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by pAcy1
5.6
N-acetyl-L-phenylalanine
-
hydrolysis in D2O, MOPS/NaOH buffer, distinctly inverse deuterium isotope effect
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
45 - 50
2-acetylamino-3-((1S,2S)-2-hydroxy-2,2-dimethyl-chroman-4-ylsulfanyl)-propionic acid
3
2-acetylamino-3-((3S,4S)-2-hydroxycyclooctylsulfanyl)-propionic acid
analysis by HPLC, pH 7.6, 37°C
19.5 - 21
2-acetylamino-3-[(S)-1-((R)-hydroxyphenyl-methyl)-2-oxo-2-phenyl-ethylsulfanyl]-propionic acid
0.0015
N-2,2-dimethylpropionyl-L-methionine
-
kcat for the hydrolysis of N-acetyl-L-methionine substrates by pAcy1
207
N-acetyl-L-glutamate
-
kcat for the hydrolysis of N-acetyl-L-glutamate substrates by pAcy1
134
N-acetyl-L-methionine
-
kcat for the hydrolysis of N-acetyl-L-methionine substrates by pAcy1
0.115
N-benzoyl-L-glutamate
-
kcat for the hydrolysis of N-acetyl-L-glutamate substrates by pAcy1
1.3
N-benzoyl-L-methionine
-
kcat for the hydrolysis of N-acetyl-L-methionine substrates by pAcy1
107
N-butanoyl-L-methionine
-
kcat for the hydrolysis of N-acetyl-L-methionine substrates by pAcy1
0.145
N-cyclohexanoyl-L-methionine
-
kcat for the hydrolysis of N-acetyl-L-methionine substrates by pAcy1
11.2
N-cyclopentanoyl-L-methionine
-
kcat for the hydrolysis of N-acetyl-L-methionine substrates by pAcy1
200
N-formyl-Lmethionine
-
kcat for the hydrolysis of N-acetyl-L-methionine substrates by pAcy1
4.3
N-hexanoyl-L-methionine
-
kcat for the hydrolysis of N-acetyl-L-methionine substrates by pAcy1
89.8
N-isobutanoyl-L-methionine
-
kcat for the hydrolysis of N-acetyl-L-methionine substrates by pAcy1
18.2
N-pentanoyl-L-methionine
-
kcat for the hydrolysis of N-acetyl-L-methionine substrates by pAcy1
168
N-propionyl-L-methionine
-
kcat for the hydrolysis of N-acetyl-L-methionine substrates by pAcy1
45
2-acetylamino-3-((1S,2S)-2-hydroxy-2,2-dimethyl-chroman-4-ylsulfanyl)-propionic acid
analysis by HPLC, pH 7.6, 37°C
50
2-acetylamino-3-((1S,2S)-2-hydroxy-2,2-dimethyl-chroman-4-ylsulfanyl)-propionic acid
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37°C
26
2-acetylamino-3-((1S,2S)-2-hydroxycyclohexylsulfanyl)-propionic acid
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37°C
30
2-acetylamino-3-((1S,2S)-2-hydroxycyclohexylsulfanyl)-propionic acid
analysis by HPLC, pH 7.6, 37°C
19.5
2-acetylamino-3-[(S)-1-((R)-hydroxyphenyl-methyl)-2-oxo-2-phenyl-ethylsulfanyl]-propionic acid
analysis by HPLC, pH 7.6, 37°C
21
2-acetylamino-3-[(S)-1-((R)-hydroxyphenyl-methyl)-2-oxo-2-phenyl-ethylsulfanyl]-propionic acid
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37°C
18
N-acetyl-L-Cys
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37°C
30
N-acetyl-L-Met
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37°C
2
N-acetyl-L-Val
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37°C
0.694
N-isopentanoyl-L-methionine
-
kcat for the hydrolysis of N-acetyl-L-methionine substrates by pAcy1
6.08
N-isopentanoyl-L-methionine
-
kcat for the hydrolysis of N-acetyl-L-methionine substrates by pAcy1
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
300 - 500
2-acetylamino-3-((1S,2S)-2-hydroxy-2,2-dimethyl-chroman-4-ylsulfanyl)-propionic acid
3
2-acetylamino-3-((3S,4S)-2-hydroxycyclooctylsulfanyl)-propionic acid
analysis by HPLC, pH 7.6, 37°C
49 - 110
2-acetylamino-3-[(S)-1-((R)-hydroxyphenyl-methyl)-2-oxo-2-phenyl-ethylsulfanyl]-propionic acid
300
2-acetylamino-3-((1S,2S)-2-hydroxy-2,2-dimethyl-chroman-4-ylsulfanyl)-propionic acid
analysis by HPLC, pH 7.6, 37°C
500
2-acetylamino-3-((1S,2S)-2-hydroxy-2,2-dimethyl-chroman-4-ylsulfanyl)-propionic acid
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37°C
52
2-acetylamino-3-((1S,2S)-2-hydroxycyclohexylsulfanyl)-propionic acid
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37°C
100
2-acetylamino-3-((1S,2S)-2-hydroxycyclohexylsulfanyl)-propionic acid
analysis by HPLC, pH 7.6, 37°C
49
2-acetylamino-3-[(S)-1-((R)-hydroxyphenyl-methyl)-2-oxo-2-phenyl-ethylsulfanyl]-propionic acid
analysis by HPLC, pH 7.6, 37°C
110
2-acetylamino-3-[(S)-1-((R)-hydroxyphenyl-methyl)-2-oxo-2-phenyl-ethylsulfanyl]-propionic acid
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37°C
36
N-acetyl-L-Cys
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37°C
100
N-acetyl-L-Met
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37°C
4
N-acetyl-L-Val
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.9
recombinant wild-type enzyme, substrate L-methionine, synthesis reaction, pH 6.0, 25°C
77
recombinant wild-type enzyme, substrate N-acetyl-L-methionine, hydrolytic reaction, pH 6.0, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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_PIG
407
0
45347
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45260
2 * 45260, gel filtration and ESI-MS following a desalting step on a RP-HPLC column
85500
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
dimer
additional information
dimer
2 * 45260, gel filtration and ESI-MS following a desalting step on a RP-HPLC column
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D346A
site-directed mutagenesis, mutation of D346 significantly reduces the rates of both N-actyl-L-Met synthesis and hydrolysis, by 4000fold, at pH 7.5, the pH optimum with substrate 3-(2-furyl)acryloyl-L-methionine is altered compared to the wild-type enzyme
D346E
site-directed mutagenesis, mutation of D346 significantly reduces the rates of both N-actyl-L-Met synthesis and hydrolysis at pH 7.5
D346N
site-directed mutagenesis, mutation of D346 significantly reduces the rates of both N-actyl-L-Met synthesis and hydrolysis at pH 7.5
D346Q
site-directed mutagenesis, mutation of D346 significantly reduces the rates of both N-actyl-L-Met synthesis and hydrolysis at pH 7.5, the pH optimum with substrate 3-(2-furyl)acryloyl-L-methionine is altered compared to the wild-type enzyme
E146A
site-directed mutagenesis, mutation of D346 significantly reduces the rates of both N-actyl-L-Met synthesis and hydrolysis at pH 7.5
E146D
site-directed mutagenesis, mutation of D346 significantly reduces the rates of both N-actyl-L-Met synthesis and hydrolysis at pH 7.5
E146N
site-directed mutagenesis, mutation of D346 significantly reduces the rates of both N-actyl-L-Met synthesis and hydrolysis at pH 7.5
E146Q
site-directed mutagenesis, mutation of D346 significantly reduces the rates of both N-actyl-L-Met synthesis and hydrolysis at pH 7.5
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 8.5
-
stable in 0.1 M potassium phosphate buffer at 55, 60 and 70°C, maximum stability from pH 6.5-6.6, immobilized enzyme at pH 7.2
288859
7 - 8.5
-
gradually inactivated below pH 7 or above pH 8.5, all activity lost below pH 4 and above pH 10
288870
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50 - 65
-
retains 80% initial activity up to 50°C, becomes rapidly inactive above 65°C
60
70
-
immobilized enzyme more thermally stable, preserved during prolonged incubation at 70°C, soluble enzyme completely inactivated in 10 min under same conditions
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
relatively stable, urea causes marked activation of the immobilized enzyme, immobilized enzyme resistant against denaturation by guanidinium hydrochloride
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, immobilized enzyme stable for more than 2 months without significant loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from kidney by acetone precipitation, ion exchange chromatography, and gel filtration
-
native enzyme from kidney by acetone precipitation, ion exchange chromatography, and gel filtration to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ACYI, DNA and amino acid sequence determination and analysis, comparison with the rat kidney enzyme
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
60fold dilution of guanidinum hydrochloride-denatured enzyme, role of osmolytes, e.g. glycerol, DMSO, sucrose, or proline, as chemical chaperones during the refolding of aminoacylase, off-pathway aggregation occurs, osmolytes inhibits aggregation and recover enzyme activity during refolding, overview
-
assisting the reactivation of guanidine hydrochloride-denatured aminoacylase by hydroxypropyl cyclodextrins in a concentration-dependent manner, most efficiently by hydroxypropyl beta-cyclodextrin, low concentrations of hydroxypropyl alpha-cyclodextrin and high concentrations of hydroxypropyl gamma-cyclodextrin promoted off-pathway aggregation, recovery of secondary and tertiary structures, overview
-
denaturation of the enzyme with 6 M guanidinium hydrochloride, dilution 60fold with Tris-HCl buffer, pH 7.5, determination of the refolding intermediate of guanidine hydrochloride denatured aminoacylase, the refolded enzyme shows 58-24% of maximal activity dependent on the temperature during refolding, 58% of native activity after refolding at 4°C, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
pAcy1 catalyzes the highly stereoselective acylation of amino acids, a useful conversion for the preparation of optically pure N-acyl-L-amino acids, the enzyme acts as chiral catalyst
synthesis
synthesis
-
aminoacylase-catalyzed enantioselective synthesis of aromatic beta-amino acids
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Birnbaum, S.M.; Levintow, L.; Kingsley, R.B.; Greenstein, J.P.
Specificity of amino acid acylases
J. Biol. Chem.
194
455-470
1952
Sus scrofa
Fones, W.S.; Lee, M.
Hydrolysis of N-acyl derivatives of alanine and phenylalanine by acylase I and carboxypeptidase
J. Biol. Chem.
201
847-856
1953
Sus scrofa
Park, R.W.; Fox, S.W.
An acylase system related to the utilization of benzoylamino acids by Lactobacillus arabinosus
J. Biol. Chem.
235
3193-3197
1960
Streptomyces sp., Lactiplantibacillus plantarum, Sus scrofa
Koerdel, W.; Schneider, F.
Chemical investigations on pig kidney aminoacylase
Biochim. Biophys. Acta
445
446-457
1976
Sus scrofa
Gentzen, I.; Lffler, H.G.; Schneider, F.
Aminoacylase from Aspergillus oryzae. Comparison with the pig kidney enzyme
Z. Naturforsch. C
35
544-550
1980
Aspergillus oryzae, Sus scrofa
Szajani, B.; Ivony, K.; Boross, L.
Comparative studies on soluble and immobilized pig kidney aminoacylase
J. Appl. Biochem.
2
72-80
1980
Aspergillus oryzae, Sus scrofa
-
Gade, W.; Brown, J.L.
Purification, characterization and possible function of alpha-N-acylamino acid hydrolase from bovine liver
Biochim. Biophys. Acta
662
86-93
1981
Bos taurus, Sus scrofa
Kumpe, E.; Lffler, H.G.; Schneider, F.
Studies on the Zn2+/Co2+ exchange with acylamino acid amidohydrolase from pig kidney
Z. Naturforsch. C
36
951-955
1981
Sus scrofa
Cho, H.Y.; Tanizawa, K.; Tanaka, H.; Soda, K.
Thermostable aminoacylase from Bacillus thermoglucosidius: Purification and characterization
Agric. Biol. Chem.
51
2793-2800
1987
Aspergillus oryzae, Bacillus sp. (in: Bacteria), Sus scrofa
-
Henseling, J.; Roehm, K.H.
Unusual solvent isotope effects on the aminoacylase-catalyzed hydrolysis of acetylamino acids
FEBS Lett.
219
27-30
1987
Sus scrofa
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
Yang, Y.B.; Hu, H.L.; Chang, M.C.; Li, H.; Tsai, Y.C.
Purification and characterization of L-aminoacylase from Alcaligenes denitrificans DA181
Biosci. Biotechnol. Biochem.
58
204-205
1994
Alcaligenes sp., Aspergillus oryzae, Bacillus sp. (in: Bacteria), Cercidium texanum, Sus scrofa, Aspergillus oryzae No.9
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
Yang, Y.; Wang, H.R.; Zhou, H.M.
Kinetics of inhibition of aminoacylase activity by dithiothreitol or 2-mercaptoethanol
Int. J. Pept. Protein Res.
48
532-538
1996
Sus scrofa
Giardina, T.; Biagini, A.; Dalle Ore, F.; Ferre, E.; Reynier, M.; Puigserver, A.
The hog intestinal mucosa acylase I: Subcellular localization, isolation, kinetic studies and biological function
Biochimie
79
265-273
1997
Bos taurus, 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
Wakayama, M.; Shiiba, E.; Sakai, K.; Moriguchi, M.
Purification and characterization of L-aminoacylase from Pseudomonas maltophila B1
J. Ferment. Bioeng.
85
278-282
1998
Aspergillus oryzae, Bacillus sp. (in: Bacteria), Stenotrophomonas maltophilia, Sus scrofa
-
Wang, H.J.; Bai, J.H.; Liu, D.S.; Zhang, T.; Zhou, H.M.
Preparation and properties of immobilized pig kidney aminoacylase and optical resolution of N-acyl-DL-alanine
Appl. Biochem. Biotechnol.
76
183-191
1999
Aspergillus oryzae, Sus scrofa
Tamura, T.; Oki, Y.; Yoshida, A.; Kuriyama, T.; Kawakami, H.; Inoue, H.; Inagaki, K.; Tanaka, H.
Noncompetitive, reversible inhibition of aminoacylase-1 by a series of L-alpha-hydroxyl and L-alpha-fluoro fatty acids: Ligand specificity of Aspergillus oryzae and porcine kindney enzymes
Arch. Biochem. Biophys.
379
261-266
2000
Aspergillus oryzae, Sus scrofa
D'Ambrosio, C.; Talamo, F.; Vitale, R.M.; Amodeo, P.; Tell, G.; Ferrara, L.; Scaloni, A.
Probing the dimeric structure of porcine aminoacylase 1 by mass spectrometric and modeling procedures
Biochemistry
42
4430-4443
2003
Sus scrofa (P37111), Sus scrofa
Kim, S.H.; Yan, Y.B.; Zhou, H.M.
Role of osmolytes as chemical chaperones during the refolding of aminoacylase
Biochem. Cell Biol.
84
30-38
2006
Sus scrofa
Kim, S.H.; Zhang, J.; Jiang, Y.; Zhou, H.M.; Yan, Y.B.
Assisting the reactivation of guanidine hydrochloride-denatured aminoacylase by hydroxypropyl cyclodextrins
Biophys. J.
91
686-693
2006
Sus scrofa
Perrier, J.; Durand, A.; Giardina, T.; Puigserver, A.
The rat kidney acylase 1. Evidence for a new cDNA form and comparisons with the porcine intestinal enzyme
Comp. Biochem. Physiol. B
138B
277-283
2004
Sus scrofa (P37111), Rattus norvegicus (Q6AYS7)
-
Xie, Q.; Zhou, H.M.
Refolding intermediate of guanidine hydrochloride denatured aminoacylase
Int. J. Biochem. Cell Biol.
36
1332-1340
2004
Sus scrofa
Groger, H.; Trauthwein, H.; Buchholz, S.; Drauz, K.; Sacherer, C.; Godfrin, S.; Werner, H.
The first aminoacylase-catalyzed enantioselective synthesis of aromatic beta-amino acids
Org. Biomol. Chem.
2
1977-1978
2004
Sus scrofa
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
Su, J.T.; Kim, S.H.; Yan, Y.B.
Dissecting the pretransitional conformational changes in aminoacylase I thermal denaturation
Biophys. J.
92
578-587
2007
Sus scrofa
Kim, S.H.; Zhou, H.M.; Yan, Y.B.
Effects of hydroxypropyl cyclodextrins on the reactivation of SDS-denatured aminoacylase
Int. J. Biol. Macromol.
40
76-82
2007
Sus scrofa
Liu, Z.; Zhen, Z.; Zuo, Z.; Wu, Y.; Liu, A.; Yi, Q.; Li, W.
Probing the catalytic center of porcine aminoacylase 1 by site-directed mutagenesis, homology modeling and substrate docking
J. Biochem.
139
421-430
2006
Sus scrofa (P37111), Sus scrofa
Wardenga, R.; Hollmann, F.; Thum, O.; Bornscheuer, U.
Functional expression of porcine aminoacylase 1 in E. coli using a codon optimized synthetic gene and molecular chaperones
Appl. Microbiol. Biotechnol.
81
721-729
2008
Sus scrofa (P37111), Sus scrofa
Wardenga, R.; Lindner, H.A.; Hollmann, F.; Thum, O.; Bornscheuer, U.
Increasing the synthesis/hydrolysis ratio of aminoacylase 1 by site-directed mutagenesis
Biochimie
92
102-109
2010
Sus scrofa (P37111), Sus scrofa
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
Keller, J.W.; Hamilton, B.J.
Enzymatic resolution of 2-trifluoromethylalanine
Tetrahedron Lett.
27
1249-1250
1986
Sus scrofa
-
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