Information on EC 3.5.1.14 - N-acyl-aliphatic-L-amino acid amidohydrolase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
3.5.1.14
-
RECOMMENDED NAME
GeneOntology No.
N-acyl-aliphatic-L-amino acid amidohydrolase
REACTION
REACTION DIAGRAM
COMMENTARY
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-aliphatic-L-amino acid + H2O = an aliphatic L-amino acid + a carboxylate
show the reaction diagram
active site structure, catalysis involves residues H206, N263, R276, and D274, the dimerization domain residues play important roles in binding and catalysis, overview
-
an N-acyl-aliphatic-L-amino acid + H2O = an aliphatic L-amino acid + a carboxylate
show the reaction diagram
active site structure, molecular modelling to determine Asp82 function in catalysis, Asp82 ensures a proper protonation of the catalytic His residue, overview
Q6AYS7
an N-acyl-aliphatic-L-amino acid + H2O = an aliphatic L-amino acid + a carboxylate
show the reaction diagram
(1)
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylic acid amide hydrolysis
-
-
deacylation
-
-
-
-
hydrolysis
-
-
hydrolysis of amide bond
-
-
-
-
hydrolysis of N-acetylated amino acids
-
-
hydrolysis of N-acetylated amino acids
-
-
hydrolysis of N-acetylated amino acids
Q03154
-
hydrolysis of N-acetylated amino acids
Q99JW2
-
hydrolysis of N-acetylated amino acids
O58453
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
-
arginine metabolism
-
-
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
Metabolic pathways
-
-
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
AAIII
Q99JW2
-
ACY 1a
Q6AYS7
-
ACY 1b
P37111
-
ACY-1A
Q6AYS7
-
Acy1
-
-
Acy1
-
-
Acy1
-
-
acylase
-
-
-
-
acylase 1
Q6AYS7
-
acylase 1
P37111
-
acylase I
-
-
-
-
alpha-N-acylaminoacid hydrolase
-
-
-
-
amido acid deacylase
-
-
-
-
aminoacylase
G8EJ32
-
aminoacylase 1
-
-
aminoacylase 1
-
-
aminoacylase 1
Q6AYS7
-
aminoacylase 1
P37111
-
aminoacylase 1a
Q6AYS7
-
aminoacylase 3
-
-
aminoacylase 3
-
-
aminoacylase I
-
-
-
-
aminoacylase I
-
-
aminoacylase-1
-
-
aminoacylase-1A
Q6AYS7
-
aminoacylase-1B
P37111
-
benzamidase
-
-
-
-
D-AAse
-
-
D-Aminoacylase
-
-
dehydropeptidase II
-
-
-
-
fungus aminoacylase-1
-
-
hAcy1
-
-
hAcy1
Q03154
-
hippurase
-
-
-
-
hippuricase
-
-
-
-
histozyme
-
-
-
-
hog intestinal acylase I
-
-
hog kidney aminoacylase I
-
-
intestine acylase I
-
-
L-amido-acid acylase
-
-
-
-
L-aminoacylase
-
-
-
-
L-aminoacylase
-
-
lepidopteran aminoacylase 1
G8EJ32
-
long acyl amidoacylase
-
-
-
-
N-Acyl-D-aspartate amidohydrolase
-
-
N-acyl-L-amino acid amidohydrolase
P37111
-
N-acyl-L-amino acid hydrolase
-
-
N-acyl-L-amino acid hydrolase
P37111
-
N-acyl-L-amino-acid amidohydrolase
-
-
-
-
N-acyl-L-amino-acid amidohydrolase
Q6AYS7
-
N-acyl-L-amino-acid amidohydrolase
C9K2Z6
-
N-acyl-L-aminoacylase 1
P37111
-
N-acylase IA
-
-
N-formylmethionine deformylase
-
-
Nalpha-acyl-L-amino acid amidohydrolase
-
-
pAcy1
P37111
-
PhoACY
O58453
-
pig kidney aminoacylase
-
-
porcine kidney aminoacylase
-
-
short acyl amidoacylase
-
-
-
-
sphingosine kinase 1-interacting protein
-
-
additional information
-
the enzyme belongs to the M20 metallopeptidase family
additional information
Q6AYS7
the enzyme is a member of the metalloprotein family M20
additional information
C9K2Z6
the enzyme belongs to the peptidase M20 family
CAS REGISTRY NUMBER
COMMENTARY
9012-37-7
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
denitrificans DA181, M14; xylosoxydans subsp. xylosoxydans A-6
-
-
Manually annotated by BRENDA team
xylosoxydans subsp. xylosoxydans A-6
-
-
Manually annotated by BRENDA team
Aspergillus oryzae No.9
No.9
-
-
Manually annotated by BRENDA team
stearothermophilus
-
-
Manually annotated by BRENDA team
thermoglucosidicus, strain DSM 2542
-
-
Manually annotated by BRENDA team
Cercidium texanum
paloverde tree
-
-
Manually annotated by BRENDA team
Corynebacterium striatum AX20
strain Ax20
-
-
Manually annotated by BRENDA team
strain MG1363
-
-
Manually annotated by BRENDA team
Lactococcus lactis MG1363
strain MG1363
-
-
Manually annotated by BRENDA team
avium, smegmatis, phlei
-
-
Manually annotated by BRENDA team
no activity in Streptomyces olivaceus
-
-
-
Manually annotated by BRENDA team
no activity in Streptomyces olivaceus IFO 12805
-
-
-
Manually annotated by BRENDA team
strain SE83
-
-
Manually annotated by BRENDA team
Pyrococcus horikoshii OT-3
-
SwissProt
Manually annotated by BRENDA team
male Wistar rats
SwissProt
Manually annotated by BRENDA team
rat, male Sprague-Dawley
-
-
Manually annotated by BRENDA team
Sprague-Dawley rats
-
-
Manually annotated by BRENDA team
Wistar rats, gene ACY1
SwissProt
Manually annotated by BRENDA team
gram-negative, motile, nonsporeforming rod-shaped bacterium, B1
-
-
Manually annotated by BRENDA team
i.e. Streptomyces luteoreticuli, strains NBRC/IFO 13819 and 13422
-
-
Manually annotated by BRENDA team
strain NBRC 13819; strain NBRC (IFO) 13819
UniProt
Manually annotated by BRENDA team
olivaeus 62 , tuirus
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-acetylamino-3-((1S,2S)-2-hydroxycyclohexylsulfanyl)-propionic acid + H2O
S-[(1S,2S)-2-hydroxycyclohexyl]cysteine + acetate
show the reaction diagram
-
-
-
-
?
2-acetylamino-3-((3S,4S)-2-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
show the reaction diagram
-
-
-
-
?
2-acetylamino-3-((3S,4S)-2-hydroxycyclooctylsulfanyl)-propionic acid + H2O
S-[(1S,2S)-2-hydroxycyclooctyl]cysteine + acetate
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
3-(2-furyl)acryloyl-L-methionine + H2O
3-(2-furyl)acrylate + L-methionine
show the reaction diagram
-
-
-
-
?
8-methyl-N-vanillyl-6-nonenamide + H2O
?
show the reaction diagram
-
i.e. capsaicin
-
-
?
acetyl-DL-alloisoleucine + H2O
acetate + DL-alloisoleucine
show the reaction diagram
-
-
-
-
?
acetyl-DL-ethionine + H2O
acetate + DL-ethionine
show the reaction diagram
-
-
-
-
?
acetyl-DL-isoleucine + H2O
acetate + DL-isoleucine
show the reaction diagram
-
-
-
-
?
acetyl-L-beta amino acid + H2O
acetate + L-beta amino acid
show the reaction diagram
-
-
-
-
?
acetyl-L-methionine + H2O
acetate + L-methionine
show the reaction diagram
-
-
-
-
?
alpha,beta-dichloroacetyl-DL-diaminopropionic acid + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-DL-alanine + H2O
benzoate + DL-alanine
show the reaction diagram
-
-
-
-
?
benzoyl-DL-leucinamide + H2O
benzoate + DL-leucinamide
show the reaction diagram
-
-
-
-
?
benzoyl-DL-methionine + H2O
benzoate + DL-methionine
show the reaction diagram
-
-
-
-
?
benzoyl-DL-phenylalanine + H2O
benzoate + DL-phenylalanine
show the reaction diagram
-
-
-
-
?
benzoyl-DL-phenylalanine + H2O
benzoate + DL-phenylalanine
show the reaction diagram
-
-
-
-
?
benzoyl-DL-valine + H2O
benzoate + DL-valine
show the reaction diagram
-
-
-
-
?
benzoyl-L-leucine + H2O
benzoate + L-leucine
show the reaction diagram
-
-
-
-
?
benzoyloxycarbonglycyl-L-leucine + H2O
?
show the reaction diagram
-
-
-
-
?
bromoacetyl -DL_alanine + H2O
bromoacetate + DL-alanine
show the reaction diagram
-
-
-
-
?
bromoacetyl-DL-phenylalanine + H2O
bromoacetate + DL-phenylalanine
show the reaction diagram
-
-
-
-
?
cephalosporin C + H2O
7-aminocephalosporanic acid
show the reaction diagram
-
-
-
-
?
chloracetyl-DL-aminoheptylic acid + H2O
chloroacetate + DL-aminoheptanoate
show the reaction diagram
-
-
-
-
?
chloroacetyl-DL-allothreonine + H2O
chloroacetate + DL-allothreonine
show the reaction diagram
-
-
-
-
?
chloroacetyl-DL-serine + H2O
chloroacetate + DL-serine
show the reaction diagram
-
-
-
-
?
chloroacetyl-DL-threonine + H2O
chloroacetate + DL-threonine
show the reaction diagram
-
-
-
-
?
chloroacetyl-L-4-fluorophenylalanine + H2O
chloroacetate + L-4-fluorophenylalanine
show the reaction diagram
-
-
-
-
?
chloroacetyl-L-4-methoxyphenylalanine + H2O
chloroacetate + L-4-methoxyphenylalanine
show the reaction diagram
-
-
-
-
?
chloroacetyl-L-beta amino acid + H2O
chloroacetate + L-beta amino acid
show the reaction diagram
-
-
-
-
?
chloroacetyl-L-leucine + H2O
chloroacetate + L-leucine
show the reaction diagram
-
-
-
-
?
chloroacetyl-L-leucine + H2O
chloroacetate + L-leucine
show the reaction diagram
-
-
-
-
r
chloroacetyl-L-phenylalanine + H2O
chloroacetate + L-phenylalanine
show the reaction diagram
-
-
-
-
?
dichloroacety-DL-phenylalanine + H2O
dichloroacetate + DL-phenylalanine
show the reaction diagram
-
-
-
-
?
dichloroacetyl-DL-alanine + H2O
dichloroacetate + DL-alanine
show the reaction diagram
-
-
-
-
?
dichloroacetyl-DL-ornithine + H2O
dichloroacetate + DL-ornithine
show the reaction diagram
-
-
-
-
?
DL-N-acetyl-D,L-3-(4-thiazolyl)alanine + H2O
L-3-(4-thiazolyl)alanine + D-N-acetyl-D-3-(4-thiazolyl)alanine
show the reaction diagram
-
-
-
-
-
fluoroacetyl-DL-alanine + H2O
fluoroacetate + DL-alanine
show the reaction diagram
-
-
-
-
?
fluoroacetyl-L-phenylalanine + H2O
fluoroacetate + L-phenylalanine
show the reaction diagram
-
-
-
-
?
formyl-DL-alanine + H2O
formate + DL-alanine
show the reaction diagram
-
-
-
-
?
formyl-DL-phenylalanine + H2O
formate + L-phenylalanine
show the reaction diagram
-
-
-
-
?
furylacryloyl-L-methionine + H2O
?
show the reaction diagram
-
-
-
-
?
glycyl-L-methionine + H2O
glycine + L-methionine
show the reaction diagram
-
-
-
-
?
glycyl-L-tyrosine + H2O
glycine + L-tyrosine
show the reaction diagram
-
-
-
-
?
hydroxyacetyl-DL-alanine + H2O
hydroxyacetate + DL-alanine
show the reaction diagram
-
isolated as the barium salt
-
-
?
hydroxyacetyl-DL-phenylalanine + H2O
hydroxyacetate + DL-phenylalanine
show the reaction diagram
-
-
-
-
?
iodoacetyl-DL-alanine + H2O
iodoacetate + DL-alanine
show the reaction diagram
-
-
-
-
?
iodoacetyl-DL-phenylalanine + H2O
iodoacetate + DL-phenylalanine
show the reaction diagram
-
-
-
-
?
L-methionylglycine + H2O
glycine + L-methionine
show the reaction diagram
-
-
-
-
?
m-nitrobenzoyl-DL-alanine + H2O
3-nitrobenzoate + DL-alanine
show the reaction diagram
-
-
-
-
?
methyl-mercaptoacetyl-DL-alanine + H2O
methylmercaptoacetate + DL-alanine
show the reaction diagram
-
-
-
-
?
N-(E)-3-methyl-2-hexenoyl-L-glutamine + H2O
(E)-3-methyl-2-hexenoyl-glutamine + L-glutamine
show the reaction diagram
Corynebacterium striatum, Corynebacterium striatum AX20
-
-
-
-
?
N-2,2-dimethylpropionyl-L-methionine + H2O
propionate + L-methionine
show the reaction diagram
Q03154
-
-
-
?
N-3-methyl-3-hydroxy-hexanoyl-L-glutamine + H2O
3-methyl-3-hydroxy-hexanoate + L-glutamine
show the reaction diagram
Corynebacterium striatum, Corynebacterium striatum AX20
-
-
-
-
?
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-D-Homophenylalanine + H2O
acetate + D-Homophenylalanine
show the reaction diagram
-
-
-
-
?
N-acetyl-DL-aspartate + H2O
acetate + DL-aspartate
show the reaction diagram
-
-
-
-
?
N-acetyl-DL-aspartate + H2O
acetate + DL-aspartate
show the reaction diagram
-
-
-
-
?
N-acetyl-DL-aspartate + H2O
acetate + DL-aspartate
show the reaction diagram
-
-
-
-
?
N-acetyl-DL-aspartate + H2O
acetate + DL-aspartate
show the reaction diagram
-
-
-
-
?
N-acetyl-DL-aspartate + H2O
acetate + DL-aspartate
show the reaction diagram
-
-
-
-
?
N-acetyl-DL-aspartate + H2O
acetate + DL-aspartate
show the reaction diagram
-
D-isomer, N-acetyl-D-aspartate as inducer
-
-
?
N-acetyl-DL-aspartate + H2O
acetate + DL-aspartate
show the reaction diagram
-
pure acylated D-forms hydrolyzed 10000-40000 times more slowly than corresponding pure acylated L-isomers
-
-
-
N-acetyl-DL-methionine + H2O
DL-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-DL-methionine + H2O
DL-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-DL-methionine + H2O
DL-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-DL-methionine + H2O
DL-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-DL-methionine + H2O
DL-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-DL-methionine + H2O
DL-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-DL-methionine + H2O
DL-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-DL-methionine + H2O
DL-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-DL-methionine + H2O
DL-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-DL-methionine + H2O
DL-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-DL-methionine + H2O
DL-methionine + acetate
show the reaction diagram
Aspergillus oryzae No.9
-
-
-
-
?
N-acetyl-DL-methionine + H2O
N-acetyl-D-methionine + L-methionine + acetic acid
show the reaction diagram
-
-
-
-
-
N-acetyl-DL-norleucine + H2O
DL-norleucine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-DL-norleucine + H2O
DL-norleucine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-DL-proline + H2O
acetate + DL-proline
show the reaction diagram
-
-
-
-
?
N-acetyl-DL-serine + H2O
acetate + DL-serine
show the reaction diagram
-
-
-
-
?
N-acetyl-DL-Trp + H2O
acetate + DL-Trp
show the reaction diagram
-
-
-
-
-
N-acetyl-DL-tyrosine + H2O
acetate + DL-tyrosine
show the reaction diagram
-
-
-
-
?
N-acetyl-DL-tyrosine + H2O
acetate + DL-tyrosine
show the reaction diagram
-
prefers D-isomer
-
-
?
N-Acetyl-Gly + H2O
acetate + Gly
show the reaction diagram
C9K2Z6
-
-
-
?
N-acetyl-glycine + H2O
acetate + glycine
show the reaction diagram
-
-
-
-
?
N-acetyl-glycine + H2O
acetate + glycine
show the reaction diagram
-
-
-
-
?
N-acetyl-glycine + H2O
acetate + glycine
show the reaction diagram
-
-
-
-
?
N-acetyl-glycine + H2O
acetate + glycine
show the reaction diagram
-
-
-
-
?
N-acetyl-glycine + H2O
acetate + glycine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-2-aminopentanoate + H2O
acetate + L-2-aminopentanoate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-Ala + H2O
acetate + L-Ala
show the reaction diagram
C9K2Z6
-
-
-
?
N-acetyl-L-alanine + H2O
L-alanine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-alanine + H2O
L-alanine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-alanine + H2O
L-alanine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-alanine + H2O
L-alanine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-alanine + H2O
L-alanine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-alanine + H2O
L-alanine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-alanine + H2O
L-alanine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-alanine + H2O
L-alanine + acetate
show the reaction diagram
Aspergillus oryzae No.9
-
-
-
-
?
N-acetyl-L-alanine + H2O
acetate + L-alanine
show the reaction diagram
C9K2Z6
-
-
-
?
N-acetyl-L-alanine + H2O
acetate + L-alanine
show the reaction diagram
O58754
-
-
-
?
N-acetyl-L-amino acid + H2O
carboxylic acid + L-amino acid
show the reaction diagram
-
highly enantioselective hydrolysis of esters and amides, the L-configuration is preferred, overview
-
-
?
N-acetyl-L-Arg + H2O
acetate + L-Arg
show the reaction diagram
C9K2Z6
-
-
-
?
N-acetyl-L-arginine + H2O
acetate + L-arginine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-arginine + H2O
acetate + L-arginine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-arginine + H2O
acetate + L-arginine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-arginine + H2O
acetate + L-arginine
show the reaction diagram
C9K2Z6
-
-
-
?
N-acetyl-L-Asn + H2O
acetate + L-Asn
show the reaction diagram
C9K2Z6
-
-
-
?
N-acetyl-L-Asp + H2O
acetate + L-Asp
show the reaction diagram
C9K2Z6
-
-
-
?
N-acetyl-L-asparagine + H2O
acetate + L-asparagine
show the reaction diagram
-
-
-
-
-
N-acetyl-L-asparagine + H2O
acetate + L-asparagine
show the reaction diagram
C9K2Z6
-
-
-
?
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-Cys + H2O
acetate + L-Cys
show the reaction diagram
-
-
-
-
?
N-acetyl-L-Cys + H2O
acetate + L-Cys
show the reaction diagram
C9K2Z6
-
-
-
?
N-acetyl-L-Cys + H2O
L-Cys + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-cysteine + H2O
acetate + L-cysteine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-cysteine + H2O
acetate + L-cysteine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-cysteine + H2O
acetate + L-cysteine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-cysteine + H2O
acetate + L-cysteine
show the reaction diagram
C9K2Z6
-
-
-
?
N-acetyl-L-ethionine + H2O
acetate + L-ethionine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-Gln + H2O
acetate + L-Gln
show the reaction diagram
C9K2Z6
-
-
-
?
N-acetyl-L-glutamate + H2O
acetate + L-glutamate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-glutamine + H2O
L-glutamine + acetate
show the reaction diagram
-
-
-
-
-
N-acetyl-L-glutamine + H2O
L-glutamine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-glutamine + H2O
L-glutamine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-glutamine + H2O
L-glutamine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-glutamine + H2O
L-glutamine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-glutamine + H2O
L-glutamine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-glutamine + H2O
L-glutamine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-glutamine + H2O
acetate + L-glutamine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-glutamine + H2O
acetate + L-glutamine
show the reaction diagram
C9K2Z6
-
-
-
?
N-acetyl-L-glycine + H2O
acetate + L-glycine
show the reaction diagram
O58754
weak activity
-
-
?
N-acetyl-L-histidine + H2O
acetate + L-histidine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-histidine + H2O
acetate + L-histidine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-histidine + H2O
acetate + L-histidine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-histidine + H2O
acetate + L-histidine
show the reaction diagram
Q99JW2
-
-
-
?
N-acetyl-L-histidine + H2O
acetate + L-histidine
show the reaction diagram
C9K2Z6
-
-
-
?
N-acetyl-L-Homophenylalanine + H2O
acetate + L-Homophenylalanine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-isoleucine + H2O
acetate + L-isoleucine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-Leu + H2O
acetate + L-Leu
show the reaction diagram
C9K2Z6
-
-
-
?
N-acetyl-L-leucine + H2O
acetate + L-leucine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-leucine + H2O
acetate + L-leucine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-leucine + H2O
acetate + L-leucine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-leucine + H2O
acetate + L-leucine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-leucine + H2O
acetate + L-leucine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-leucine + H2O
acetate + L-leucine
show the reaction diagram
Q6AYS7
-
-
-
?
N-acetyl-L-leucine + H2O
acetate + L-leucine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-leucine + H2O
acetate + L-leucine
show the reaction diagram
C9K2Z6
-
-
-
?
N-acetyl-L-leucine + H2O
acetate + L-leucine
show the reaction diagram
-
immobilised enzyme
-
-
?
N-acetyl-L-Met + H2O
acetate + L-Met
show the reaction diagram
-
-
-
-
?
N-acetyl-L-Met + H2O
acetate + L-Met
show the reaction diagram
C9K2Z6
highest activity
-
-
?
N-acetyl-L-Met + H2O
L-Met + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine
L-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine
L-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine
L-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine
L-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine
L-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine
L-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine
L-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine
L-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine
L-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine
L-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine
L-methionine + acetate
show the reaction diagram
Aspergillus oryzae No.9
-
-
-
-
?
N-acetyl-L-methionine + H2O
acetate + L-methionine
show the reaction diagram
Q03154
-
-
-
?
N-acetyl-L-methionine + H2O
acetate + L-methionine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine + H2O
acetate + L-methionine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine + H2O
acetate + L-methionine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine + H2O
acetate + L-methionine
show the reaction diagram
Q6AYS7
-
-
-
?
N-acetyl-L-methionine + H2O
acetate + L-methionine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine + H2O
acetate + L-methionine
show the reaction diagram
-
-
-
-
r
N-acetyl-L-methionine + H2O
acetate + L-methionine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine + H2O
acetate + L-methionine
show the reaction diagram
O58453
-
-
-
?
N-acetyl-L-methionine + H2O
acetate + L-methionine
show the reaction diagram
C9K2Z6
-
-
-
?
N-acetyl-L-methionine + H2O
acetate + L-methionine
show the reaction diagram
O58754
-
-
-
?
N-acetyl-L-methionine + H2O
acetate + L-methionine
show the reaction diagram
C9K2Z6
preferred substrate
-
-
?
N-acetyl-L-methionine + H2O
acetate + L-methionine
show the reaction diagram
-
immobilised enzyme
-
-
?
N-acetyl-L-methionine + H2O
acetate + L-methionine
show the reaction diagram
-
40.5% of the activity with N-acetyl-L-phenylalanine
-
-
?
N-acetyl-L-methionine + H2O
acetate + L-methionine
show the reaction diagram
Pyrococcus horikoshii OT-3
O58754
-
-
-
?
N-acetyl-L-methionine + H2O
acetic acid + L-methionine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine + H2O
acetic acid + L-methionine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-norleucine + H2O
acetate + L-norleucine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-ornithine + H2O
acetate + L-ornithine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-Phe + H2O
acetate + L-Phe
show the reaction diagram
C9K2Z6
-
-
-
?
N-acetyl-L-Phe methyl ester + H2O
acetate + L-Phe methyl ester
show the reaction diagram
-
the enzyme also shows esterase activity with N-acetyl-L-Phe methyl ester
-
-
?
N-acetyl-L-phenylalanine + H2O
L-phenylalanine + acetate
show the reaction diagram
-
-
-
-
-
N-acetyl-L-phenylalanine + H2O
L-phenylalanine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-phenylalanine + H2O
L-phenylalanine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-phenylalanine + H2O
L-phenylalanine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-phenylalanine + H2O
L-phenylalanine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-phenylalanine + H2O
L-phenylalanine + acetate
show the reaction diagram
-
prefers D-isomer
-
-
?
N-acetyl-L-phenylalanine + H2O
acetate + L-phenylalanine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-phenylalanine + H2O
acetate + L-phenylalanine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-phenylalanine + H2O
acetate + L-phenylalanine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-phenylalanine + H2O
acetate + L-phenylalanine
show the reaction diagram
Q99JW2
-
-
-
?
N-acetyl-L-phenylalanine + H2O
acetate + L-phenylalanine
show the reaction diagram
C9K2Z6
-
-
-
?
N-acetyl-L-phenylalanine + H2O
acetate + L-phenylalanine
show the reaction diagram
O58754
-
-
-
?
N-acetyl-L-phenylalanine + H2O
acetate + L-phenylalanine
show the reaction diagram
-
the reaction is highly stereoselective
-
-
?
N-acetyl-L-phenylalanine + H2O
acetate + L-phenylalanine
show the reaction diagram
-
immobilised enzyme, no activity observed with N-acetyl-L-lysine
-
-
?
N-acetyl-L-phenylalanine + H2O
acetate + L-phenylalanine
show the reaction diagram
-
no activity with N-acetyl-D-phenylalanine
-
-
?
N-acetyl-L-phenylalanine + H2O
acetate + L-phenylalanine
show the reaction diagram
Pyrococcus horikoshii OT-3
O58754
-
-
-
?
N-acetyl-L-phenylalanine methyl ester + H2O
acetate + L-phenylalanine methyl ester
show the reaction diagram
-
-
-
-
?
N-acetyl-L-serine + H2O
acetate + L-serine
show the reaction diagram
-
immobilised enzyme
-
-
?
N-acetyl-L-threonine + H2O
acetate + L-threonine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-tryptophan + H2O
acetate + L-tryptophan
show the reaction diagram
-
-
-
-
?
N-acetyl-L-tryptophan + H2O
acetate + L-tryptophan
show the reaction diagram
-
-
-
-
-
N-acetyl-L-tryptophan + H2O
acetate + L-tryptophan
show the reaction diagram
Q99JW2
-
-
-
?
N-acetyl-L-tryptophan + H2O
acetate + L-tryptophan
show the reaction diagram
O58754
weak activity
-
-
?
N-acetyl-L-tryptophan + H2O
acetate + L-tryptophan
show the reaction diagram
-
immobilised enzyme
-
-
?
N-acetyl-L-tryptophan + H2O
acetate + L-tryptophan
show the reaction diagram
Pyrococcus horikoshii OT-3
O58754
weak activity
-
-
?
N-acetyl-L-tyrosine + H2O
tyrosine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-tyrosine + H2O
acetate + L-tyrosine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-tyrosine + H2O
acetate + L-tyrosine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-tyrosine + H2O
acetate + L-tyrosine
show the reaction diagram
Q99JW2
-
-
-
?
N-acetyl-L-tyrosine + H2O
acetate + L-tyrosine
show the reaction diagram
O58754
-
-
-
?
N-acetyl-L-tyrosine + H2O
acetate + L-tyrosine
show the reaction diagram
-
immobilised enzyme
-
-
?
N-acetyl-L-tyrosine + H2O
acetate + L-tyrosine
show the reaction diagram
Pyrococcus horikoshii OT-3
O58754
-
-
-
?
N-acetyl-L-Val + H2O
acetate + L-Val
show the reaction diagram
C9K2Z6
-
-
-
?
N-acetyl-L-Val + H2O
L-Val + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-valine + H2O
L-valine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-valine + H2O
L-valine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-valine + H2O
L-valine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-valine + H2O
L-valine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-valine + H2O
L-valine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-valine + H2O
L-valine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-valine + H2O
L-valine + acetate
show the reaction diagram
-
favorite substrate
-
-
?
N-acetyl-L-valine + H2O
acetate + L-valine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-valine + H2O
acetate + L-valine
show the reaction diagram
C9K2Z6
-
-
-
?
N-acetyl-O-benzyl-DL-serine + H2O
acetate + O-benzyl-DL-serine
show the reaction diagram
-
no hydrolysis with immobilized enzyme
-
-
?
N-acetyl-phi-DL-glycine + H2O
?
show the reaction diagram
-
only D-isomer hydrolyzed
-
-
?
N-acetyl-S-(1,1,2,2-tetrafluoroethyl)-L-cysteine + H2O
acetate + S-(1,1,2,2-tetrafluoroethyl)-L-cysteine
show the reaction diagram
Q99JW2
-
-
-
?
N-acetyl-S-(1,2,2-trichlorovinyl)-L-cysteine + H2O
acetate + S-(1,2,2-trichlorovinyl)-L-cysteine
show the reaction diagram
Q99JW2
-
-
-
?
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
Q99JW2
-
-
-
?
N-acetyl-S-(1,2-dichlorovinyl)-L-cysteine + H2O
acetate + S-(1,2-dichlorovinyl)-L-cysteine
show the reaction diagram
Q99JW2
-
-
-
?
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
Q99JW2
-
-
-
?
N-acetyl-S-(2,2-dichlorovinyl)-L-cysteine + H2O
acetate + S-(2,2-dichlorovinyl)-L-cysteine
show the reaction diagram
Q99JW2
-
-
-
?
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
Q99JW2
-
-
-
?
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
Q99JW2
-
-
-
?
N-acetyl-S-(2-chlorobenzyl)-L-cysteine + H2O
acetate + S-(2-chlorobenzyl)-L-cysteine
show the reaction diagram
Q99JW2
-
-
-
?
N-acetyl-S-(2-fluorobenzyl)-L-cysteine + H2O
acetate + S-(2-fluorobenzyl)-L-cysteine
show the reaction diagram
Q99JW2
-
-
-
?
N-acetyl-S-(3-fluorobenzyl)-L-cysteine + H2O
acetate + S-(3-fluorobenzyl)-L-cysteine
show the reaction diagram
Q99JW2
-
-
-
?
N-acetyl-S-(4-bromobenzyl)-L-cysteine + H2O
acetate + S-(4-bromobenzyl)-L-cysteine
show the reaction diagram
Q99JW2
-
-
-
?
N-acetyl-S-(4-chlorobenzyl)-L-cysteine + H2O
acetate + S-(4-chlorobenzyl)-L-cysteine
show the reaction diagram
Q99JW2
-
-
-
?
N-acetyl-S-(4-methoxybenzyl)-L-cysteine + H2O
acetate + S-(4-methoxybenzyl)-L-cysteine
show the reaction diagram
Q99JW2
-
-
-
?
N-acetyl-S-1,2-dichlorovinyl-L-cysteine + H2O
acetate + S-1,2-dichlorovinyl-L-cysteine
show the reaction diagram
-
-
-
-
?
N-acetyl-S-benzyl-L-cysteine + H2O
acetate + S-benzyl-L-cysteine
show the reaction diagram
Q99JW2
-
-
-
?
N-acetyl-S-benzyl-L-cysteine + H2O
acetate + S-benzyl-L-cysteine
show the reaction diagram
-
-
-
-
?
N-acetyl-S-DL-benzylcysteine + H2O
acetate + S-DL-benzylcysteine
show the reaction diagram
-
-
-
-
?
N-acetyllysine + H2O
lysine + acetate
show the reaction diagram
-
-
-
-
?
N-acetylmethionine + H2O
acetate + L-methionine
show the reaction diagram
-
preferred substrate
-
-
?
N-acetylpipecolic acid + H2O
acetate + L-piperidine-2-carboxylate
show the reaction diagram
-
-
-
-
?
N-acetylseleno-L-methionine + H2O
acetate + L-selenomethionine
show the reaction diagram
-
-
-
-
?
N-acyl-L-amino acid + H2O
carboxylate + L-amino acid
show the reaction diagram
-
-
-
-
?
N-alpha-acetyl-L-alanine + H2O
acetate + L-alanine
show the reaction diagram
Lactococcus lactis, Lactococcus lactis MG1363
-
-
-
-
?
N-alpha-acetyl-L-aspartate + H2O
acetate + L-aspartate
show the reaction diagram
Lactococcus lactis, Lactococcus lactis MG1363
-
-
-
-
?
N-alpha-acetyl-L-cysteine + H2O
acetate + L-cysteine
show the reaction diagram
Lactococcus lactis, Lactococcus lactis MG1363
-
-
-
-
?
N-alpha-acetyl-L-glutamate + H2O
acetate + L-glutamate
show the reaction diagram
Lactococcus lactis, Lactococcus lactis MG1363
-
-
-
-
?
N-alpha-acetyl-L-isoleucine + H2O
acetate + L-isoleucine
show the reaction diagram
-
-
-
-
?
N-alpha-acetyl-L-leucine + H2O
acetate + L-leucine
show the reaction diagram
-
-
-
-
?
N-alpha-acetyl-L-lysine + H2O
acetate + L-lysine
show the reaction diagram
-
-
-
-
?
N-alpha-acetyl-L-lysine + H2O
acetate + L-lysine
show the reaction diagram
Q99JW2
-
-
-
?
N-alpha-acetyl-L-methionine + H2O
acetate + L-methionine
show the reaction diagram
-
-
-
-
?
N-alpha-acetyl-L-phenylalanine + H2O
acetate + L-phenylalanine
show the reaction diagram
-
-
-
-
?
N-alpha-acetyl-L-proline + H2O
acetate + L-proline
show the reaction diagram
-
-
-
-
?
N-alpha-acetyl-L-serine + H2O
acetate + L-serine
show the reaction diagram
-
-
-
-
?
N-alpha-acetyl-L-threonine + H2O
acetate + L-threonine
show the reaction diagram
-
-
-
-
?
N-alpha-acetyl-L-tryptophan + H2O
acetate + L-tryptophan
show the reaction diagram
-
-
-
-
?
N-alpha-acetyl-L-tyrosine + H2O
acetate + L-tyrosine
show the reaction diagram
-
-
-
-
?
N-alpha-acetyl-L-valine + H2O
acetate + L-valine
show the reaction diagram
-
-
-
-
?
N-alpha-benzoyl-L-phenylalanine + H2O
benzoate + L-phenylalanine
show the reaction diagram
-
-
-
-
?
N-alpha-chloroacetyl-L-phenylalanine + H2O
chloroacetate + L-phenylalanine
show the reaction diagram
-
-
-
-
?
N-benzoyl-L-arginine + H2O
benzoate + L-arginine
show the reaction diagram
-
immobilised enzyme
-
-
?
N-benzoyl-L-isoleucine + H2O
benzoate + L-isoleucine
show the reaction diagram
-
-
-
-
?
N-benzoyl-L-leucine + H2O
benzoate + L-leucine
show the reaction diagram
-
immobilised enzyme
-
-
?
N-benzoyl-L-methionine + H2O
benzoate + L-methionine
show the reaction diagram
Q03154
-
-
-
?
N-benzoyl-L-phenylalanine + H2O
benzoate + L-phenylalanine
show the reaction diagram
-
-
-
-
?
N-benzoyl-L-phenylalanine + H2O
benzoate + L-phenylalanine
show the reaction diagram
-
immobilised enzyme
-
-
?
N-benzoyl-L-phenylalanine + H2O
benzoate + L-phenylalanine
show the reaction diagram
-
735.7% of the activity with N-acetyl-L-phenylalanine
-
-
?
N-benzoyl-L-tert-leucine + H2O
benzoate + L-tert-isoleucine
show the reaction diagram
-
-
-
-
?
N-benzoyl-L-threnine + H2O
benzoate + L-threonine
show the reaction diagram
-
immobilised enzyme
-
-
?
N-benzoyl-L-valine + H2O
benzoate + L-valine
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-L-Phe-Gly + H2O
benzyl hydrogencarbonate + L-Phe-Gly
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-L-phenylalanine + H2O
benzyl hydrogencarbonate + L-phenylalanine
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-L-phenylalanine + H2O
benzyloxycarbonate + L-phenylalanine
show the reaction diagram
-
33.9% of the activity with N-acetyl-L-phenylalanine. no activity with N-benzyloxycarbonyl-D-phenylalanine
-
-
?
N-benzyloxycarbonyl-L-valine + H2O
benzyl hydrogencarbonate + L-valine
show the reaction diagram
-
-
-
-
?
N-butanoyl-L-methionine + H2O
butanoate + L-methionine
show the reaction diagram
Q03154
-
-
-
?
N-butyryl-D-aspartate + H2O
butanoate + D-aspartate
show the reaction diagram
-
-
-
-
?
N-butyryl-L-Met + H2O
butanoate + L-Met
show the reaction diagram
C9K2Z6
-
-
-
?
N-butyryl-L-methionine + H2O
butyrate + L-methionine
show the reaction diagram
C9K2Z6
-
-
-
?
N-carbobenzyloxy-L-glutamine + H2O
?
show the reaction diagram
Corynebacterium striatum, Corynebacterium striatum AX20
-
-
-
-
?
N-CBZ-L-phenylalanine + H2O
? + L-phenylalanine
show the reaction diagram
-
immobilised enzyme
-
-
?
N-chloroacetyl-2-aminobutyrate + H2O
chloroacetate + 2-aminobutyrate
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-chloroacetate + H2O
chloroacetate + acetate
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-chloroacetate + H2O
chloroacetate + acetate
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-chloroacetate + H2O
chloroacetate + acetate
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-DL-alanine + H2O
chloroacetate + alanine
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-DL-alanine + H2O
chloroacetate + alanine
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-DL-aspartate + H2O
chloroacetate + DL-aspartate
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-DL-glutamine + H2O
chloroacetate + DL-glutamine
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-DL-norvaline + H2O
chloroacetate + DL-norvaline
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-DL-phenylalanine + H2O
chloroacetate + phenylalanine
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-DL-phenylalanine + H2O
chloroacetate + phenylalanine
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-DL-phenylalanine + H2O
chloroacetate + phenylalanine
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-DL-phenylalanine + H2O
chloroacetate + phenylalanine
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-DL-proline + H2O
chloroacetate + DL-proline
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-DL-tyrosine + H2O
chloroacetate + DL-tyrosine
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-DL-valine + H2O
chloroacetate + DL-valine
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-DL-valine + H2O
chloroacetate + DL-valine
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-DL-valine + H2O
chloroacetate + DL-valine
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-DL-valine + H2O
chloroacetate + DL-valine
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-L-leucine + H2O
chloroacetate + L-leucine
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-L-leucine + H2O
chloroacetate + L-leucine
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-L-leucine + H2O
chloroacetate + L-leucine
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-L-leucine + H2O
chloroacetate + L-leucine
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-L-leucine + H2O
chloroacetate + L-leucine
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-L-leucine + H2O
chloroacetate + L-leucine
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-L-methionine + H2O
chloroacetate + L-methionine
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-L-methionine + H2O
chloroacetate + L-methionine
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-L-phenylalanine + H2O
chloroacetate + L-phenylalanine
show the reaction diagram
-
-
-
-
?
N-chloroacetyl-L-phenylalanine + H2O
chloroacetate + L-phenylalanine
show the reaction diagram
-
immobilised enzyme
-
-
?
N-chloroacetylaminocaprylate + H2O
chloroacetate + aminocaprylate
show the reaction diagram
-
-
-
-
?
N-chloroacetylaminocyclohexylacetate + H2O
chloroacetate + aminocyclohexylacetate
show the reaction diagram
-
-
-
-
?
N-chloroacetylaminocyclohexylbutyrate + H2O
chloroacetate + aminocyclohexylbutyrate
show the reaction diagram
-
-
-
-
?
N-chloroacetylaminocyclohexylpropionate + H2O
chloroacetate + aminocyclohexylpropionate
show the reaction diagram
-
-
-
-
?
N-chloroacetylaminophenylacetate + H2O
chloroacetate + aminophenylacetate
show the reaction diagram
-
-
-
-
?
N-chloroacetylglutamine-p-aminobenzoate + H2O
?
show the reaction diagram
-
-
-
-
?
N-chloroacetylglutamine-p-aminobenzoate + H2O
?
show the reaction diagram
-
-
-
-
?
N-chloroacetylglycine + H2O
chloroacetate + glycine
show the reaction diagram
-
-
-
-
?
N-chloroacetylglycine + H2O
chloroacetate + glycine
show the reaction diagram
-
N-chloroacetylamino acids are better substrates than N-acetylamino acids
-
-
?
N-chloroacetyltryptophan + H2O
chloroacetate + tryptophan
show the reaction diagram
-
-
-
-
?
N-chloroacetyltryptophan + H2O
chloroacetate + tryptophan
show the reaction diagram
-
-
-
-
?
N-chloroacetyltryptophan + H2O
chloroacetate + tryptophan
show the reaction diagram
-
-
-
-
?
N-cyclohexanoyl-L-methionine + H2O
hexanoate + L-methionine
show the reaction diagram
Q03154
-
-
-
?
N-cyclopentanoyl-L-methionine + H2O
pentanoate + L-methionine
show the reaction diagram
Q03154
-
-
-
?
N-decanoyl-L-glutamine + H2O
decanoate + L-glutamine
show the reaction diagram
Corynebacterium striatum, Corynebacterium striatum AX20
-
-
-
-
?
N-decanoyl-L-Met + H2O
decanoate + L-Met
show the reaction diagram
C9K2Z6
-
-
-
?
N-decanoyl-L-methionine + H2O
decanoate + L-methionine
show the reaction diagram
C9K2Z6
-
-
-
?
N-dichloroacetyl-DL-lysine + H2O
dichloroacetate + DL-lysine
show the reaction diagram
-
-
-
-
?
N-dichloroacetylnorleucine + H2O
dichloroacetate + norleucine
show the reaction diagram
-
-
-
-
?
N-formyl-D-aspartate + H2O
formate + D-aspartate
show the reaction diagram
-
-
-
-
?
N-formyl-L-methionine + H2O
formate + L-methionine
show the reaction diagram
Q03154
-
-
-
?
N-formyl-L-methionine + H2O
formate + L-methionine
show the reaction diagram
-
-
-
-
?
N-formyl-L-methionine + H2O
formate + L-methionine
show the reaction diagram
-
hydrolyzed at 60% rate of N-acetylmethionine
-
-
?
N-formylmethionine + H2O
formate + L-methionine
show the reaction diagram
-
substrate synthesis and purification, overview
-
-
?
N-glycyl-D-aspartate + H2O
glycine + D-aspartate
show the reaction diagram
-
-
-
-
?
N-hexanoyl-L-Met + H2O
hexanoate + L-Met
show the reaction diagram
C9K2Z6
-
-
-
?
N-hexanoyl-L-methionine + H2O
hexanoate + L-methionine
show the reaction diagram
Q03154
-
-
-
?
N-hexanoyl-L-methionine + H2O
hexanoate + L-methionine
show the reaction diagram
-
-
-
-
-
N-hexanoyl-L-methionine + H2O
hexanoate + L-methionine
show the reaction diagram
C9K2Z6
-
-
-
?
N-isobutanoyl-L-methionine + H2O
isobutanoate + L-methionine
show the reaction diagram
Q03154
-
-
-
?
N-isopentanoyl-L-methionine + H2O
pentanoate + L-methionine
show the reaction diagram
Q03154
-
-
-
?
N-lauroyl-Gly + H2O
laurate + Gly
show the reaction diagram
C9K2Z6
-
-
-
?
N-lauroyl-glycine + H2O
laurate + glycine
show the reaction diagram
-
-
-
-
?
N-lauroyl-L-Ala + H2O
laurate + L-Ala
show the reaction diagram
C9K2Z6
-
-
-
?
N-lauroyl-L-alanine + H2O
laurate + L-alanine
show the reaction diagram
-
-
-
-
?
N-lauroyl-L-Arg + H2O
laurate + L-Arg
show the reaction diagram
C9K2Z6
-
-
-
?
N-lauroyl-L-arginine + H2O
laurate + L-arginine
show the reaction diagram
-
-
-
-
?
N-lauroyl-L-Asn + H2O
laurate + L-Asn
show the reaction diagram
C9K2Z6
-
-
-
?
N-lauroyl-L-asparagine + H2O
laurate + L-asparagine
show the reaction diagram
-
-
-
-
?
N-lauroyl-L-aspartate + H2O
laurate + L-aspartate
show the reaction diagram
-
-
-
-
?
N-lauroyl-L-Cys + H2O
laurate + L-Cys
show the reaction diagram
C9K2Z6
-
-
-
?
N-lauroyl-L-glutamate + H2O
laurate + L-glutamate
show the reaction diagram
-
-
-
-
?
N-lauroyl-L-glutamine + H2O
laurate + L-glutamine
show the reaction diagram
-
-
-
-
?
N-lauroyl-L-glutamine + H2O
laurate + L-glutamine
show the reaction diagram
Corynebacterium striatum, Corynebacterium striatum AX20
-
-
-
-
?
N-lauroyl-L-glutaminyl-glycine + H2O
laurate + L-glutaminyl-glycine
show the reaction diagram
-
-
-
-
?
N-lauroyl-L-glutaminyl-L-lysine + H2O
laurate + L-glutaminyl-L-lysine
show the reaction diagram
-
-
-
-
?
N-lauroyl-L-glutamyl-glycine + H2O
laurate + L-glutamyl-glycine
show the reaction diagram
-
-
-
-
?
N-lauroyl-L-His + H2O
laurate + L-His
show the reaction diagram
C9K2Z6
-
-
-
?
N-lauroyl-L-histidine + H2O
laurate + L-histidine
show the reaction diagram
-
-
-
-
?
N-lauroyl-L-isoleucine + H2O
laurate + L-isoleucine
show the reaction diagram
-
-
-
-
?
N-lauroyl-L-leucine + H2O
laurate + L-leucine
show the reaction diagram
-
-
-
-
?
N-lauroyl-L-Lys + H2O
laurate + L-Lys
show the reaction diagram
C9K2Z6
-
-
-
?
N-lauroyl-L-Met + H2O
laurate + L-Met
show the reaction diagram
C9K2Z6
-
-
-
?
N-lauroyl-L-methionine + H2O
laurate + L-methionine
show the reaction diagram
-
-
-
-
?
N-lauroyl-L-phenylalanine + H2O
laurate + L-phenylalanine
show the reaction diagram
-
-
-
-
?
N-lauroyl-L-Ser + H2O
laurate + L-Ser
show the reaction diagram
C9K2Z6
-
-
-
?
N-lauroyl-L-serine + H2O
laurate + L-serine
show the reaction diagram
-
best substrate
-
-
?
N-lauroyl-L-threonine + H2O
laurate + L-threonine
show the reaction diagram
-
-
-
-
?
N-lauroyl-L-tryptophan + H2O
laurate + L-tryptophan
show the reaction diagram
-
-
-
-
?
N-lauroyl-L-tyrosine + H2O
laurate + L-tyrosine
show the reaction diagram
-
-
-
-
?
N-lauroyl-L-valine + H2O
laurate + L-valine
show the reaction diagram
-
-
-
-
?
N-lauryl-glycine + H2O
laurate + glycine
show the reaction diagram
C9K2Z6
-
-
-
?
N-lauryl-L-alanine + H2O
laurate + L-alanine
show the reaction diagram
C9K2Z6
-
-
-
?
N-lauryl-L-cysteine + H2O
laurate + L-cysteine
show the reaction diagram
C9K2Z6
-
-
-
?
N-lauryl-L-lysine + H2O
laurate + L-lysine
show the reaction diagram
C9K2Z6
-
-
-
?
N-lauryl-L-methionine + H2O
laurate + L-methionine
show the reaction diagram
C9K2Z6
-
-
-
?
N-lauryl-L-serine + H2O
laurate + L-serine
show the reaction diagram
C9K2Z6
-
-
-
?
N-linolenoyl-L-glutamine + H2O
linolenic acid + L-glutamine
show the reaction diagram
G8EJ32
-
-
-
?
N-myristoyl-L-Met + H2O
myristate + L-Met
show the reaction diagram
C9K2Z6
-
-
-
?
N-myristoyl-L-methionine + H2O
myristate + L-methionine
show the reaction diagram
C9K2Z6
-
-
-
?
N-octanoyl-L-Met + H2O
octanoate + L-Met
show the reaction diagram
C9K2Z6
-
-
-
?
N-octanoyl-L-methionine + H2O
octanoate + L-methionine
show the reaction diagram
C9K2Z6
-
-
-
?
N-palmitoyl-L-Met + H2O
palmitate + L-Met
show the reaction diagram
C9K2Z6
-
-
-
?
N-palmitoyl-L-methionine + H2O
palmitate + L-methionine
show the reaction diagram
C9K2Z6
-
-
-
?
N-pentanoyl-L-methionine + H2O
pentanoate + L-methionine
show the reaction diagram
Q03154
-
-
-
?
N-propionyl-D-aspartate + H2O
proipionate + D-aspartate
show the reaction diagram
-
-
-
-
?
N-propionyl-L-methionine + H2O
propionate + L-methionine
show the reaction diagram
Q03154
-
-
-
?
N-t-BOC-L-phenylalanine + H2O
? + L-phenylalanine
show the reaction diagram
-
immobilised enzyme
-
-
?
N-tert-butyloxycarbonyl-L-phenylalanine + H2O
N-tert-butyl hydrogencarbonate + L-phenylalanine
show the reaction diagram
-
-
-
-
?
Nalpha-acetylmethionine + H2O
acetate + L-methionine
show the reaction diagram
-
-
-
-
?
Nalpha-lauroyl-L-lysine + H2O
laurate + L-lysine
show the reaction diagram
-
-
-
-
?
Nepsilon-lauroyl-L-lysine + H2O
laurate + L-lysine
show the reaction diagram
-
-
-
-
?
O-methyl-N-acetyl-DL-serine + H2O
acetate + O-methyl-DL-serine
show the reaction diagram
-
-
-
-
?
p-bromobenzoyl-DL-alanine + H2O
4-bromobenzoate + DL-alanine
show the reaction diagram
-
-
-
-
?
p-chlorobenzoyl-DL-alanine + H2O
4-chlorbenzoate + DL-alanine
show the reaction diagram
-
-
-
-
?
p-fluorobenzoyl-DL-alanine + H2O
4-fluorobenzoate + DL-alanine
show the reaction diagram
-
-
-
-
?
p-iodobenzoyl-DL-alanine + H2O
4-iodobenzoate + DL-alanine
show the reaction diagram
-
-
-
-
?
p-nitrobenzoyl-DL-alanine + H2O
4-nitrobenzoate + DL-alanine
show the reaction diagram
-
-
-
-
?
p-tolyl-DL-alanine + H2O
?
show the reaction diagram
-
-
-
-
?
palmitoyl-L-aspartate + H2O
palmitate + L-aspartate
show the reaction diagram
-
-
-
-
?
palmitoyl-L-phenylalanine + H2O
palmitate + L-phenylalanine
show the reaction diagram
-
-
-
-
?
propionyl-DL-alanine + H2O
propanoate + DL-alanine
show the reaction diagram
-
-
-
-
?
S-(1,1,2,2-tetrafluoroethyl)-N-acetyl-L-cysteine + H2O
acetate + S-(-1,1,2,2-terafluoroethyl)-L-cysteine
show the reaction diagram
-
-
-
-
?
S-(2-bromo-1,1,2-trifluoroethyl)-N-acetyl-L-cysteine + H2O
acetate + S-(2-bromo-1,1,2-trifluoroethyl)-L-cysteine
show the reaction diagram
-
-
-
-
?
S-(2-chloro-1,1,2-trifluoroethyl)-N-acetyl-L-cysteine + H2O
acetate + S-(2-chloro-1,1,2-trifluoroethyl)-L-cysteine
show the reaction diagram
-
-
-
-
?
S-ethyl-N-acetyl-L-cysteine + H2O
acetate + S-ethyl-L-cysteine
show the reaction diagram
-
-
-
-
?
S-isobutyl-N-acetyl-L-cysteine + H2O
?
show the reaction diagram
-
-
-
-
?
S-isopropyl-N-acetyl-L-cysteine + H2O
acetate + S-isopropyl-L-cysteine
show the reaction diagram
-
-
-
-
?
S-methyl-N-acetyl-L-cysteine + H2O
acetate + S-methyl-L-cysteine
show the reaction diagram
-
-
-
-
?
S-n-butyl-N-acetyl-L-cysteine + H2O
acetate + S-n-butyl-L-cysteine
show the reaction diagram
-
-
-
-
?
S-n-propyl-N-acetyl-L-cysteine + H2O
acetate + S-n-propyl-L-cysteine
show the reaction diagram
-
-
-
-
?
trifluoroacetyl-DL-alanine + H2O
trifluoroacetate + DL-alanine
show the reaction diagram
-
trifluoroacetyl derivatives are most rapidly hydrolyzed
-
-
?
trifluoroacetyl-DL-phenylalanine + H2O
trifluoroacetate + DL-phenylalanine
show the reaction diagram
-
-
-
-
?
methylmercaptoacetyl-DL-phenylalanine + H2O
methylmercaptoacetate + DL-phenylalanine
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
N-acyl-D-alanine is not substrate
-
-
-
additional information
?
-
-
the enzyme is involved in the degradation of chemotactic N-formyl peptides and plays a protective role in degrading bacterial and mitochondrial N-formylated peptide together with the alpha-N-acylpeptide hydrolase, EC 3.4.19.1
-
-
-
additional information
?
-
-
the enzyme is involved in the regulation of oxidative stress, and, by direct interaction, of sphingosine kinase type 1, SphK1, which has a role in cell growth promotion and inhibition of tumor cell apoptosis, Acy1 induces redistribution of SphK1 to the plasma membrane from cytosol, overview
-
-
-
additional information
?
-
-
butanolysis and enantioselective hydrolysis of carboxylic acid esters, the activity of the enzyme is not restricted to N-acyl transfers, other substrates are e.g. L-aminobutyric acid alkyl esters, L-aminobutyric acid amide, L-4-hydroxyphenylglycine, and L-4-hydroxyphenylglycine amide, overview
-
-
-
additional information
?
-
-
no activity with N-formylmethionylalanine, N-formylalanylalanine, N-formylmethionylalanylserine, N-acetylmethionylalanylserine, and N-formylmethionylleucylphenylalanine
-
-
-
additional information
?
-
-
substrate synthesis in an aqueous/n-hexane biphasic system
-
-
-
additional information
?
-
-
the enzyme cataylzes high enantioselective reactions
-
-
-
additional information
?
-
-
the enzyme interacts with sphingosine kinase type 1, SphK1
-
-
-
additional information
?
-
-
AA1 similar to AA3 is involved in deacetylation of N-acetyl-aromatic amino acids and mercapturic acids
-
-
-
additional information
?
-
-
aminoacylase catalyzes the hydrolysis of L-acyl-amino acids to produce the corresponding L-amino acid
-
-
-
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
?
-
C9K2Z6
the enzyme shows high hydrolytic activity towards various N-acetyl-L-amino acids and N-(middle/long)-chain-fatty-acyl-L-amino acids with a preference for the acyl derivatives of L-Met, L-Ala, L-Cys, etc
-
-
-
additional information
?
-
-
AA3 residues Arg63, Asp68, Asn70, Arg71, Glu177 and Tyr287 are potentially involved in catalysis/substrate binding
-
-
-
additional information
?
-
C9K2Z6
no activity towards N-acetyl-L-Lys, N-acetyl-L-Glu, N-acetyl-L-Pro, N-acetyl-L-Trp, N-acetyl-L-Tyr, N-lauroyl-L-Ile, N-lauroyl-L-Leu, N-lauroyl-L-Phe, N-lauroyl-L-Pro, N-lauroyl-L-Trp, N-lauroyl-L-Tyr, and N-lauroyl-L-Val, the enzyme hydrolyzes N-(middle/long)-chain-fatty-acyl-L-amino acids as well as N-short-chain-acyl-L-amino acids. Poor or no activity with N-acetyl-amino acids containing L-Lys, L-Asp, L-Cys, L-Pro, L-Trp, and L-Tyr, as well as with N-leuroyl-amino acids containing L-Arg, L-His, L-Asn, L-Ile, L-Leu, L-Phe, L-Pro, L-Trp, L-Tyr, and L-Val, substrate specificity, overview
-
-
-
additional information
?
-
-
the enzyme hydrolyzes N-(middle/long)-chain-fatty-acyl-L-amino acids as well as N-short-chain-acyl-L-amino acids. Poor or no activity with N-acetyl-amino acids containing L-Lys, L-Asp, L-Cys, L-Pro, L-Trp, and L-Tyr, as well as with N-leuroyl-amino acids containing L-Arg, L-His, L-Asn, L-Ile, L-Leu, L-Phe, L-Pro, L-Trp, L-Tyr, and L-Val, substrate specificity, overview
-
-
-
additional information
?
-
O58754
N-acetyl-D-amino acids are not hydrolyzed
-
-
-
additional information
?
-
-
the enzyme is most specific for substrates containing N-benzoyl- or N-chloroacetyl-amino acids, preferring substrates containing hydrophobic, uncharged, or weakly charged amino acids such as phenylalanine, methionine, and cysteine. It contains esterase activity with 4-nitrophenyl-palmitate and 4-nitrophenyllaurate, but not Phe-ethyl ester at 85C, the enzyme is most specific for substrates containing N-benzoyl- or N-chloroacetyl-amino acids, preferring substrates containing hydrophobic, uncharged, or weakly charged amino acids such as phenylalanine, methionine, and cysteine. No activity with N-benzoyl-D-phenylalanine, N-benzyloxycarbonyl-D-phenylalanine, tert-butyloxycarbonyl-D-phenylalanine, N-acetyl-D-tryptophan
-
-
-
additional information
?
-
Lactococcus lactis MG1363
-
N-acyl-D-alanine is not substrate
-
-
-
additional information
?
-
Pyrococcus horikoshii OT-3
O58754
N-acetyl-D-amino acids are not hydrolyzed
-
-
-
additional information
additional information
-
-
the order of preferred substrates is Phe > Thr > Leu > Arg for N-benzoyl substrates and Phe >> Ser > Leu > Met > Tyr > Trp for N-acetyl substrates
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
?
N-acetyl-L-alanine + H2O
acetate + L-alanine
show the reaction diagram
C9K2Z6
-
-
-
?
N-acetyl-L-amino acid + H2O
carboxylic acid + L-amino acid
show the reaction diagram
-
-
-
-
?
N-acetyl-L-cysteine + H2O
acetate + L-cysteine
show the reaction diagram
C9K2Z6
-
-
-
?
N-acetyl-L-methionine
L-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine
L-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine
L-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine
L-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine
L-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine
L-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine
L-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine
L-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine
L-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine
L-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine
L-methionine + acetate
show the reaction diagram
Aspergillus oryzae No.9
-
-
-
-
?
N-acetyl-L-methionine + H2O
acetate + L-methionine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine + H2O
acetate + L-methionine
show the reaction diagram
-
-
-
-
r
N-acetyl-L-methionine + H2O
acetate + L-methionine
show the reaction diagram
C9K2Z6
-
-
-
?
N-acetyl-L-phenylalanine + H2O
acetate + L-phenylalanine
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme is involved in the degradation of chemotactic N-formyl peptides and plays a protective role in degrading bacterial and mitochondrial N-formylated peptide together with the alpha-N-acylpeptide hydrolase, EC 3.4.19.1
-
-
-
additional information
?
-
-
the enzyme is involved in the regulation of oxidative stress, and, by direct interaction, of sphingosine kinase type 1, SphK1, which has a role in cell growth promotion and inhibition of tumor cell apoptosis, Acy1 induces redistribution of SphK1 to the plasma membrane from cytosol, overview
-
-
-
additional information
?
-
-
AA1 similar to AA3 is involved in deacetylation of N-acetyl-aromatic amino acids and mercapturic acids
-
-
-
additional information
?
-
-
aminoacylase catalyzes the hydrolysis of L-acyl-amino acids to produce the corresponding L-amino acid
-
-
-
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
?
-
C9K2Z6
the enzyme shows high hydrolytic activity towards various N-acetyl-L-amino acids and N-(middle/long)-chain-fatty-acyl-L-amino acids with a preference for the acyl derivatives of L-Met, L-Ala, L-Cys, etc
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
O58754
the enzyme contains 1.22 mol of Zn2+ and 0.17 mol of Ca2+ per mol of monomer enzyme protein
Co2+
-
enzyme strongly activated by Co2+ ions; inhibitory at concentration 1 mM
Co2+
-
enzyme strongly activated by Co2+ ions
Co2+
-
enzyme strongly activated by Co2+ ions
Co2+
-
enzyme strongly activated by Co2+ ions
Co2+
-
enzyme strongly activated by Co2+ ions
Co2+
-
enzyme strongly activated by Co2+ ions
Co2+
-
activates free and immobilized enzyme
Co2+
-
required, activity can be increased significantly by the addition of Co2+
Co2+
-
activates and stabilizes, 148% activity at 0.1 mM, tightly bound to the enzyme
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
Co2+
O58754
when the enzyme is dialyzed against 50 mM EDTA (pH 7.5) for 10 h at 4C and then against 50 mM sodium phosphate buffer (pH 7.5), the aminoacylase activity is decreased to less than 1.0%. The activity is restored by incubation in 50 mM sodium phosphate buffer (pH 7.5) containing ZnCl2, MnCl2, or CoCl2 at 4C for 1 h. The restorative effect is dependent on the concentration of the metal ions. 88%, 23%, and 20% of activities are restored by adding 1.0 mM ZnCl2, 1.0 mM MnCl2, and 0.1 mM CoCl2, respectively
Co2+
-
0.01 mM, 1.1fold activation; 0.01 mM, 1.1fold activation. 0.1 mM, 1.3fold activation
CoCl2
-
activates 2-3fold at 0.1 mM
CoCl2
-
relative activity of ACY is 286.2% when dipicolinic acid is removed; relative activity of ACY is 310% when EDTA is removed, 40.2% with EDTA
CuCl2
-
relative activity of ACY is 22.9% when dipicolinic acid is removed; relative activity of ACY is 26.4% when EDTA is removed
Mn2+
-
inhibitory at concentration 1 mM
Mn2+
-
activity can be increased by the addition of Mn2+
Mn2+
-
Zn2+ substituted by Mn2+: increased activity (substrate: N-acetyl-L-methionine)
Mn2+
-
Mn2+ can substitute for zinc ions in AA1 without a substantial loss of activity
Mn2+
O58754
when the enzyme is dialyzed against 50 mM EDTA (pH 7.5) for 10 h at 4C and then against 50 mM sodium phosphate buffer (pH 7.5), the aminoacylase activity is decreased to less than 1.0%. The activity is restored by incubation in 50 mM sodium phosphate buffer (pH 7.5) containing ZnCl2, MnCl2, or CoCl2 at 4C for 1 h. The restorative effect is dependent on the concentration of the metal ions. 88%, 23%, and 20% of activities are restored by adding 1.0 mM ZnCl2, 1.0 mM MnCl2, and 0.1 mM CoCl2, respectively
Ni2+
-
Zn2+ substituted by Ni2+: increased activity (substrate: N-acetyl-L-methionine)
Ni2+
-
AA3 is a metalloenzyme significantly activated by Co2+ and Ni2+
Ni2+
C9K2Z6
110% relative activity at 0.005 mM
NiCl2
-
activates 2-3fold at 0.1 mM
NiCl2
-
relative activity of ACY is 180.5% when dipicolinic acid is removed; relative activity of ACY is 200.1% when EDTA is removed
Zn2+
-
enzyme contains Zn as prosthetic metal
Zn2+
-
enzyme contains Zn as prosthetic metal
Zn2+
-
-
Zn2+
-
enzyme contains Zn as prosthetic metal
Zn2+
-
enzyme contains Zn as prosthetic metal
Zn2+
-
enzyme contains Zn as prosthetic metal
Zn2+
-
enzyme contains Zn as prosthetic metal
Zn2+
-
required
Zn2+
Q6AYS7
metalloenzyme, required for activity
Zn2+
-
binding site structure, H206 and E146 are involved
Zn2+
-
0.98 Zn2+ per enzyme molecule, tightly bound, involved in cataylsis
Zn2+
-
required
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
Zn2+
C9K2Z6
120% relative activity at 0.0005 mM; activates 57% at 500 nM, 20% at 0.005 mM, but inhibits 61% at 2.5 mM
Zn2+
G8EJ32
restores activity after treatment with EDTA or phenanthroline
Zn2+
O58754
the enzyme contains 1.22 mol of Zn2+ and 0.17 mol of Ca2+ per mol of monomer enzyme protein. When the enzyme is dialyzed against 50 mM EDTA (pH 7.5) for 10 h at 4C and then against 50 mM sodium phosphate buffer (pH 7.5), the aminoacylase activity is decreased to less than 1.0%. The activity is restored by incubation in 50 mM sodium phosphate buffer (pH 7.5) containing ZnCl2, MnCl2, or CoCl2 at 4C for 1 h. The restorative effect is dependent on the concentration of the metal ions. 88%, 23%, and 20% of activities are restored by adding 1.0 mM ZnCl2, 1.0 mM MnCl2, and 0.1 mM CoCl2, respectively
Zn2+
-
0.01 mM, 1.3fold activation; 0.01 mM or 0.1 mM, 1.3fold activation
Zn2+
-
contains one Zn2+ per monomer, zinc-containing enzyme
ZnCl2
-
relative activity of ACY is 113.7% when EDTA is removed; relative activity of ACY is 90.8% when dipicolinic acid is removed
MnCl2
-
relative activity of ACY is 125.3% when dipicolinic acid is removed; relative activity of ACY is 203.5% when EDTA is removed
additional information
-
metalloenzyme
additional information
-
metal removal completely inactivates AA3, whereas addition of Zn2+, Mn2+ or Fe2+ restores initial activity
additional information
-
determination of metal contents, overview. Metal removal completely inactivates AA3, whereas addition of Zn2+, Mn2+ or Fe2+ restores initial activity. A putative metal binding site is formed by His21, Glu24 and His116. No effect on AA3 activity by Zn2+, Mn2+, Fe2+, Cd2+, Mg2+, Ca2+, K+ and Na+
additional information
C9K2Z6
the enzyme activity is not affected by Ca2+ or Mg2+ at 0.5 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
6% inhibition at 10 mM
1,10-phenanthroline
-
24% inhibition
1,10-phenanthroline
C9K2Z6
10% residual activity at 1 mM; 90% inhibition at 1 mM
1,10-phenanthroline
-
1 mM, 54% inhibition
1,3-dichloro-2-propanone
-
-
1-chloro-2-tosylamido-7-amino-2-heptanone
-
25 mM, 7% inhibition
-
2,3-Butanedione
-
-
2-mercaptoethanol
C9K2Z6
20% inhibition at 1 mM; 81% residual activity at 1 mM
4-hydroxymercuribenzoate
-
1 mM, 67% inhibition
Ba2+
-
0.01 mM, 17% inhibition
benzamidine
-
0.1 mM, 7% inhibition
benzyloxycarbonyl-Gly-Gly-Phe
O58754
-
beta-mercaptoethanol
-
0.005 M
beta-mercaptoethanol
-
-
beta-mercaptoethanol
-
competitive, slow reversible inhibition
beta-mercaptoethanol
-
-
Ca2+
C9K2Z6
86% residual activity at 0.005 mM
Ca2+
-
0.01 mM, 45% inhibition
Cd2+
-
50% inhibition at 1 mM
Co2+
-
inhibitory at concentration 1 mM
Co2+
C9K2Z6
82% residual activity at 0.005 mM; slight inhibition at 0.5 mM
Cs+
-
0.01 mM, 47% inhibition
Cu2+
C9K2Z6
93% residual activity at 0.005 mM; slight inhibition at 0.5 mM
Cu2+
-
0.01 mM, 95% inhibition
D-phenylalanine
-
inhibition of benzoyl-L-leucine and benzoyloxycarbonglycyl-L-leucine hydrolysis
diethyldicarbonate
-
-
diethyldicarbonate
-
-
diethyldithiocarbamate
-
-
Diethylpyrocarbonate
-
-
dithiothreitol
-
0.001 M
dithiothreitol
-
-
dithiothreitol
-
-
dithiothreitol
-
-
dithiothreitol
-
1 mM, 22% inhibition; 1 mM, 42% inhibition
DTT
-
85% inhibition at 20 mM
EDTA
-
irreversible inactivation
EDTA
-
10% inhibition at 50 mM
EDTA
-
13% inhibition
EDTA
O58453
inhibits PhoACY activity
EDTA
G8EJ32
-
EDTA
-
1 mM, 45% inhibition
Fe2+
-
-
Fe2+
C9K2Z6
86% residual activity at 0.005 mM; 90% inhibition at 0.5 mM
Fe2+
-
0.01 mM, 33% inhibition
Fe3+
-
0.01 mM, 99% inhibition
Hg2+
-
-
iodoacetamide
-
90% inhibition at 10 mM
iodoacetamide
C9K2Z6
15% inhibition at 1 mM; 85% residual activity at 1 mM
iodoacetate
-
1 mM, 1.1fold activation
iodoacetic acid
-
-
iodoacetic acid
-
-
iodoacetic acid
-
higher inhibitory effect on L-aminoacylase
iodoacetic acid
-
-
Isocaproic acid
-
-
Isopropanol
-
10%
K+
-
0.01 mM, 24% inhibition
L-alpha-fluoro-beta-phenyl-propionate
-
-
L-benzylsuccinate
-
-
-
L-benzylsuccinate
O58754
-
-
L-beta-Phenyllactate
-
-
La3+
-
0.01 mM, 17% inhibition
Li+
-
0.01 mM, 51% inhibition
Mg2+
C9K2Z6
96% residual activity at 0.005 mM
Mg2+
-
0.01 mM, 8% inhibition
Mn2+
-
inhibitory at concentration 1 mM
Mn2+
C9K2Z6
88% residual activity at 0.005 mM; slight inhibition at 0.5 mM
Mn2+
-
0.01 mM, 54% inhibition
N-(4-toluenesulfonyl)-DL-methionine
-
25 mM, 14% inhibition
-
N-(p-toluenesulfonyl)-DL-Met
-
25 mM, 14% inhibition
-
N-acetyl-L-2-aminohexanoic acid
-
-
-
N-alpha-p-Tosyl-L-lysine
-
-
n-butylmalonic acid
-
-
N-ethylmaleimide
-
-
Na+
-
0.01 mM, 19% inhibition
Nepsilon-formyl-Nepsilon-hydroxy-L-lysine
-
IC50: 1.0 mM
Ni2+
-
-
Ni2+
C9K2Z6
slight inhibition at 0.5 mM
Ni2+
-
0.01 mM, 27% inhibition
Nitrilotriacetate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
PCMB
-
inhibits murine AAIII
Phenanthroline
G8EJ32
-
phenylboronic acid
-
-
phenylmethylsulfonyl fluoride
-
1 mM, 22% inhibition
Sn4+
-
0.01 mM, 99% inhibition
Sodium arsenite
-
higher inhibitory effect on L-aminacylase
Tris-(2-amino-ethyl)-amine
-
-
Vinylpyridine
-
-
Zn2+
C9K2Z6
activates 57% at 500 nM, 20% at 0.005 mM, but inhibits 61% at 2.5 mM; slight inhibition at 0.5 mM; the relative remaining activity is decreased to 39% by incubation with 2.5 mM Zn2+
mono-tert-butyl malonate
-
25 mM, 14% inhibition
-
additional information
-
no effects by GSH, L-Cys, (NH4)6Mo7O24, PMSF, PCMB, DTT, MgSO4, AgNO3, CaCl2, FeSO4, ZnCl2, and CuSO4
-
additional information
C9K2Z6
the activity of the recombinant enzyme is not influenced by dithiothreitol, reduced glutathione, EDTA, p-chloromercuribenzoic acid, and L-Cys
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithioerythritol
-
with palmitoylaspartate as substrate
dithiothreitol
-
slight activation of short acyl aminoacylase at 0.2 mM
DTT
-
activates murine AAIII
mercaptoethanol
-
-
mono-benzyl malonate
-
25 mM, activation to 109% of control
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.3
2-acetylamino-3-((1S,2S)-2-hydroxycyclohexylsulfanyl)-propionic acid
-
analysis by HPLC, pH 7.6, 37C
0.5
2-acetylamino-3-((1S,2S)-2-hydroxycyclohexylsulfanyl)-propionic acid
-
analysis by HPLC, pH 7.6, 37C
0.5
2-acetylamino-3-((1S,2S)-2-hydroxycyclohexylsulfanyl)-propionic acid
-
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37C
0.1
2-acetylamino-3-((3S,4S)-2-hydroxy-2,2-dimethyl-chroman-4-ylsulfanyl)-propionic acid
-
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37C
0.15
2-acetylamino-3-((3S,4S)-2-hydroxy-2,2-dimethyl-chroman-4-ylsulfanyl)-propionic acid
-
analysis by HPLC, pH 7.6, 37C
0.2
2-acetylamino-3-((3S,4S)-2-hydroxy-2,2-dimethyl-chroman-4-ylsulfanyl)-propionic acid
-
analysis by HPLC, pH 7.6, 37C
1
2-acetylamino-3-((3S,4S)-2-hydroxycyclooctylsulfanyl)-propionic acid
-
analysis by HPLC, pH 7.6, 37C
-
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, 37C
0.3
2-acetylamino-3-[(S)-1-((R)-hydroxyphenyl-methyl)-2-oxo-2-phenyl-ethylsulfanyl]-propionic acid
-
analysis by HPLC, pH 7.6, 37C
0.4
2-acetylamino-3-[(S)-1-((R)-hydroxyphenyl-methyl)-2-oxo-2-phenyl-ethylsulfanyl]-propionic acid
-
analysis by HPLC, pH 7.6, 37C
0.2
N-(E)-3-methyl-2-hexenoyl-L-glutamine
-
pH 7
168
N-2,2-dimethylpropionyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by hAcy1
585
N-2,2-dimethylpropionyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by pAcy1
0.74
N-3-methyl-3-hydroxy-hexanoyl-L-glutamine
-
pH 7
2.52
N-acetyl-D-aspartate
-
-
12.7
N-acetyl-DL-aspartate
-
-
43.6
N-acetyl-glycine
-
25C, pH 7.4
59.9
N-acetyl-glycine
-
25C, pH7.4
2.32
N-acetyl-L-alanine
-
-
20.1
N-acetyl-L-alanine
-
25C, pH7.4
34.8
N-acetyl-L-arginine
-
25C, pH 7.4
27.7
N-acetyl-L-asparagine
-
25C, pH7.4
0.4
N-acetyl-L-Cys
-
analysis by HPLC, pH 7.6, 37C
0.5
N-acetyl-L-Cys
-
analysis by HPLC, pH 7.6, 37C
0.5
N-acetyl-L-Cys
-
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37C
1.4
N-acetyl-L-cysteine
-
25C, pH7.4
1.5
N-acetyl-L-cysteine
-
25C, pH 7.4
4.4
N-acetyl-L-cysteine
-
-
1.28
N-acetyl-L-ethionine
-
25C, pH7.4
1.87
N-acetyl-L-ethionine
-
25C, pH 7.4
63
N-acetyl-L-glutamate
-
hydrolysis of N-acetyl-L-glutamate substrates by wild-type human Acy1
63
N-acetyl-L-glutamate
-
25C, pH7.4
70
N-acetyl-L-glutamate
-
hydrolysis of N-acetyl-L-glutamate substrates by wild-type human Acy1
102
N-acetyl-L-glutamate
-
hydrolysis of N-acetyl-L-glutamate substrates by Wild-Type porcine Acy1
102
N-acetyl-L-glutamate
-
25C, pH 7.4
5.9
N-acetyl-L-glutamic acid
-
pH 7.0, 30C
7
N-acetyl-L-glutamine
-
hydrolysis in D2O, MOPS/NaOH buffer
10.2
N-acetyl-L-glutamine
-
MOPS/NaOH buffer
57.6
N-acetyl-L-glutamine
-
25C, pH 7.4
62.3
N-acetyl-L-glutamine
-
25C, pH7.4
1.8
N-acetyl-L-histidine
-
37C, pH 7.5
11.9
N-acetyl-L-histidine
-
25C, pH 7.4
22.7
N-acetyl-L-histidine
-
25C, pH7.4
6.72
N-acetyl-L-isoleucine
-
25C, pH 7.4
2.4
N-acetyl-L-leucine
-
25C, pH7.4
3.8
N-acetyl-L-leucine
-
25C, pH 7.4
0.2
N-acetyl-L-Met
-
analysis by HPLC, pH 7.6, 37C
0.3
N-acetyl-L-Met
-
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37C
0.5
N-acetyl-L-Met
-
analysis by HPLC, pH 7.6, 37C
11.3
N-acetyl-L-Met
C9K2Z6
recombinant enzyme, at 37C, pH not specified in the publication
0.013
N-acetyl-L-methionine
-
addition of 0.2 mM Co2+
0.056
N-acetyl-L-methionine
-
addition of 0.2 mM Mn2+
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
0.43
N-acetyl-L-methionine
-
25C, pH7.4
0.76
N-acetyl-L-methionine
-
hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-T347F-mutant
0.964
N-acetyl-L-methionine
-
pH 8.0, 40C, native enzyme
0.99
N-acetyl-L-methionine
-
-
1
N-acetyl-L-methionine
-
-
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
1.4
N-acetyl-L-methionine
-
immobilized enzyme
1.497
N-acetyl-L-methionine
-
pH 8.0, 40C, immobilized, cross-linked enzyme-bovine serum albumin aggregate
1.62
N-acetyl-L-methionine
-
ordinary water, 50 mM MOPS 50 mM bicine buffer
1.72
N-acetyl-L-methionine
-
hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-I177L-mutant
1.87
N-acetyl-L-methionine
-
hydrolysis in D2O, 50 mM MOPS 50 mM bicine buffer
2.1
N-acetyl-L-methionine
-
-
2.72
N-acetyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by pAcy1
2.72
N-acetyl-L-methionine
-
25C, pH 7.4
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
4.18
N-acetyl-L-methionine
O58754
pH 7.5, 85C, wild-type enzyme
4.32
N-acetyl-L-methionine
-
hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-L372G-mutant
5
N-acetyl-L-methionine
-
-
6
N-acetyl-L-methionine
-
soluble enzyme
24.6
N-acetyl-L-methionine
O58453
-
0.44
N-acetyl-L-norleucine
-
25C, pH7.4
1.57
N-acetyl-L-norleucine
-
25C, pH 7.4
1.6
N-acetyl-L-phenylalanine
-
37C, pH 7.5
4.81
N-acetyl-L-phenylalanine
-
25C, pH7.4
5.2
N-acetyl-L-phenylalanine
O58754
pH 7.5, 85C, wild-type enzyme
5.5
N-acetyl-L-phenylalanine
-
ordinary water, MOPS/NaOH buffer
5.6
N-acetyl-L-phenylalanine
-
hydrolysis in D2O, MOPS/NaOH buffer, distinctly inverse deuterium isotope effect
6.2
N-acetyl-L-phenylalanine
O58754
pH 7.5, 85C, mutant enzyme C102S
6.64
N-acetyl-L-phenylalanine
O58754
pH 7.5, 85C, mutant enzyme E367Q
10.3
N-acetyl-L-phenylalanine
-
25C, pH 7.4
30.9
N-acetyl-L-threonine
-
25C, pH 7.4
32.5
N-acetyl-L-threonine
-
25C, pH7.4
1.2
N-acetyl-L-tryptophan
-
37C, pH 7.5
1.4
N-acetyl-L-tyrosine
-
37C, pH 7.5
0.4
N-acetyl-L-Val
-
analysis by HPLC, pH 7.6, 37C
-
0.5
N-acetyl-L-Val
-
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37C
-
2.5
N-acetyl-L-valine
-
-
11.4
N-acetyl-L-valine
-
25C, pH7.4
16.6
N-acetyl-L-valine
-
25C, pH 7.4
0.25
N-acetyl-S-(1,1,2,2-tetrafluoroethyl)-L-cysteine
-
37C, pH 7.5
1.2
N-acetyl-S-(1,2,2-trichlorovinyl)-L-cysteine
-
37C, pH 7.5
1
N-acetyl-S-(1,2,3,4,4-pentachlorobutadienyl)-L-cysteine
-
37C, pH 7.5
0.9
N-acetyl-S-(1,2-dichlorovinyl)-L-cysteine
-
37C, pH 7.5
5.3
N-acetyl-S-(2,2-dichloro-1,1-difluoroethyl)-L-cysteine
-
37C, pH 7.5
0.4
N-acetyl-S-(2,2-dichlorovinyl)-L-cysteine
-
37C, pH 7.5
0.3
N-acetyl-S-(2,2-difluoro-1,1-dichloroethyl)-L-cysteine
-
37C, pH 7.5
0.28
N-acetyl-S-(2-chloro-1,1,2-trifluoroethyl)-L-cysteine
-
37C, pH 7.5
1.45
N-acetyl-S-(2-chlorobenzyl)-L-cysteine
-
37C, pH 7.5
1.3
N-acetyl-S-(2-fluorobenzyl)-L-cysteine
-
37C, pH 7.5
0.6
N-acetyl-S-(3-fluorobenzyl)-L-cysteine
-
37C, pH 7.5
0.5
N-acetyl-S-(4-bromobenzyl)-L-cysteine
-
37C, pH 7.5
0.3
N-acetyl-S-(4-chlorobenzyl)-L-cysteine
-
37C, pH 7.5
0.8
N-acetyl-S-(4-methoxybenzyl)-L-cysteine
-
37C, pH 7.5
1.1
N-acetyl-S-benzyl-L-cysteine
-
37C, pH 7.5
0.3
N-acetylmethionine
-
pH 8.0, 22C
4
N-acetylseleno-L-methionine
-
-
1.2
N-alpha-acetyl-L-alanine
-
pH 7.0, 30C
5
N-alpha-acetyl-L-aspartate
-
pH 7.0, 30C
9.1
N-alpha-acetyl-L-cysteine
-
pH 7.0, 30C
3.1
N-alpha-acetyl-L-isoleucine
-
pH 7.0, 30C
2.3
N-alpha-acetyl-L-leucine
-
pH 7.0, 30C
1.3
N-alpha-acetyl-L-lysine
-
37C, pH 7.5
6.7
N-alpha-acetyl-L-lysine
-
pH 7.0, 30C
0.84
N-alpha-acetyl-L-methionine
-
native porcine enzyme,25°C
1.2
N-alpha-acetyl-L-methionine
-
E309H-mutant, 25°C
1.25
N-alpha-acetyl-L-methionine
-
Wild type Rosetta (DE3),25°C
2.12
N-alpha-acetyl-L-methionine
-
R274A-mutant, 25°C
2.21
N-alpha-acetyl-L-methionine
-
H79A-mutant, 25°C
2.23
N-alpha-acetyl-L-methionine
-
E147A-mutant, 25°C
2.36
N-alpha-acetyl-L-methionine
-
E174A-mutant, 25°C
2.45
N-alpha-acetyl-L-methionine
-
H371A-mutant, 25°C
2.52
N-alpha-acetyl-L-methionine
-
D112A-mutant, 25°C
3.82
N-alpha-acetyl-L-methionine
-
H205L-mutant, 25°C
4.34
N-alpha-acetyl-L-methionine
-
E146A-mutant, 25°C
4.57
N-alpha-acetyl-L-methionine
-
N261A-mutant, 25°C
7.7
N-alpha-acetyl-L-methionine
-
pH 7.0, 30C
1.7
N-alpha-acetyl-L-phenylalanine
-
pH 7.0, 30C
2.7
N-alpha-acetyl-L-phenylalanine
-
pH 7.0, 30C
5
N-alpha-acetyl-L-proline
-
pH 7.0, 30C
4.2
N-alpha-acetyl-L-serine
-
pH 7.0, 30C
4
N-alpha-acetyl-L-threonine
-
pH 7.0, 30C
2.4
N-alpha-acetyl-L-tryptophan
-
pH 7.0, 30C
1.9
N-alpha-acetyl-L-tyrosine
-
pH 7.0, 30C
2.5
N-alpha-acetyl-L-valine
-
pH 7.0, 30C
1.4
N-alpha-chloroacetyl-L-phenylalanine
-
pH 7.0, 30C
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
0.41
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
4
N-benzoyl-L-phenylalanine
-
S100T/M106K mutant protein, pH 8.0, 55C
8.5
N-benzoyl-L-phenylalanine
-
wild type protein, pH 8.0, 55C
9.7
N-benzoyl-L-phenylalanine
-
F251K mutant protein, pH 8.0, 55C
5
N-benzoyl-L-valine
-
F251K mutant protein, pH 8.0, 55C
6.7
N-benzoyl-L-valine
-
wild type protein, pH 8.0, 55C
10.7
N-benzoyl-L-valine
-
S100T/M106K mutant protein, pH 8.0, 55C
0.31
N-butanoyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by pAcy1
0.73
N-butanoyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by hAcy1
0.033
N-butyryl-D-aspartate
-
-
4.3
N-CBZ-Gly-Ala
-
-
0.31
N-cyclohexanoyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by pAcy1
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
0.64
N-cyclopentanoyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by pAcy1
7.18
N-cyclopentanoyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by hAcy1
0.08
N-decanoyl-L-glutamine
-
pH 7
12.5
N-formyl-D-aspartate
-
-
16.8
N-formyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by hAcy1
35.4
N-formyl-Lmethionine
-
hydrolysis of N-acyl-L-methionine substrates by pAcy1
3.1
N-formylmethionine
-
pH 8.0, 22C
1.11
N-glycyl-D-aspartate
-
-
0.01
N-hexanoyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by pAcy1
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
15.3
N-isobutanoyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by hAcy1
58.5
N-isobutanoyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by pAcy1
0.54
N-isopentanoyl-L-methionine
-
hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-L372V-mutant
0.9
N-isopentanoyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by pAcy1
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
0.06
N-lauroyl-L-glutamine
-
pH 7
0.03
N-pentanoyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by pAcy1
0.19
N-pentanoyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by hAcy1
0.194
N-propionyl-D-aspartate
-
-
0.34
N-propionyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by hAcy1
0.55
N-propionyl-L-methionine
-
hydrolysis of N-acyl-L-methionine substrates by pAcy1
0.05
N2-[(benzyloxy)carbonyl]-L-glutamine
-
pH 7
0.39
Nalpha-acetylmethionine
-
pH 7.4, 22C, recombinant mutant D274A
0.43
Nalpha-acetylmethionine
-
pH 7.4, 22C, recombinant wild-type enzyme
0.54
Nalpha-acetylmethionine
-
pH 7.4, 22C, recombinant mutant H206A
0.58
Nalpha-acetylmethionine
-
pH 7.4, 22C, recombinant mutant H206K
0.78
Nalpha-acetylmethionine
-
pH 7.4, 22C, recombinant mutant N263D
2.02
Nalpha-acetylmethionine
-
pH 7.4, 22C, recombinant mutant H206N
67.4
Nalpha-acetylmethionine
-
pH 7.4, 22C, recombinant mutant R276A
0.15
palmitoylaspartate
-
-
3.4
S-ethyl-N-acetyl-L-cysteine
-
-
2.1
S-methyl-N-acetyl-L-cysteine
-
-
3.7
S-n-butyl-N-acetyl-L-cysteine
-
-
0.8
S-n-propyl-N-acetyl-L-cysteine
-
-
0.22
furylacryloyl-L-methionine
-
-
additional information
additional information
-
steady-state kinetics of wild-type and mutant enzymes, kinetics of mutants N263D, R276N, and R276Q are not measurable
-
additional information
additional information
-
kinetics of wild-type AA3 in presnece of different metal ions, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
26
2-acetylamino-3-((1S,2S)-2-hydroxycyclohexylsulfanyl)-propionic acid
-
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37C
30
2-acetylamino-3-((1S,2S)-2-hydroxycyclohexylsulfanyl)-propionic acid
-
analysis by HPLC, pH 7.6, 37C
120
2-acetylamino-3-((1S,2S)-2-hydroxycyclohexylsulfanyl)-propionic acid
-
analysis by HPLC, pH 7.6, 37C
45
2-acetylamino-3-((3S,4S)-2-hydroxy-2,2-dimethyl-chroman-4-ylsulfanyl)-propionic acid
-
analysis by HPLC, pH 7.6, 37C
50
2-acetylamino-3-((3S,4S)-2-hydroxy-2,2-dimethyl-chroman-4-ylsulfanyl)-propionic acid
-
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37C
150
2-acetylamino-3-((3S,4S)-2-hydroxy-2,2-dimethyl-chroman-4-ylsulfanyl)-propionic acid
-
analysis by HPLC, pH 7.6, 37C
3
2-acetylamino-3-((3S,4S)-2-hydroxycyclooctylsulfanyl)-propionic acid
-
analysis by HPLC, pH 7.6, 37C
-
19.5
2-acetylamino-3-[(S)-1-((R)-hydroxyphenyl-methyl)-2-oxo-2-phenyl-ethylsulfanyl]-propionic acid
-
analysis by HPLC, pH 7.6, 37C
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, 37C
0.0015
N-2,2-dimethylpropionyl-L-methionine
-
kcat for the hydrolysis of N-acyl-L-methionine substrates by hAcy1
0.0015
N-2,2-dimethylpropionyl-L-methionine
-
kcat for the hydrolysis of N-acetyl-L-methionine substrates by pAcy1
7.6
N-acetyl-glycine
-
25C, pH 7.4
31.7
N-acetyl-glycine
-
25C, pH7.4
0.04 - 1.97
N-acetyl-L-arginine
-
25C, pH 7.4
8.53
N-acetyl-L-arginine
-
25C, pH 7.4
0.1
N-acetyl-L-aspartate
-
E167R mutant protein, pH not specified in the publication, temperature not specified in the publication
9
N-acetyl-L-Cys
-
analysis by HPLC, pH 7.6, 37C
18
N-acetyl-L-Cys
-
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37C
30
N-acetyl-L-Cys
-
analysis by HPLC, pH 7.6, 37C
28.1
N-acetyl-L-cysteine
-
25C, pH7.4
34.7
N-acetyl-L-cysteine
-
25C, pH 7.4
12.4
N-acetyl-L-ethionine
-
25C, pH7.4
68.3
N-acetyl-L-ethionine
-
25C, pH 7.4
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
156
N-acetyl-L-glutamate
-
25C, pH7.4
207
N-acetyl-L-glutamate
-
kcat for the hydrolysis of N-acetyl-L-glutamate substrates by pAcy1
207
N-acetyl-L-glutamate
-
25C, pH 7.4
30.7
N-acetyl-L-glutamine
-
25C, pH7.4
146
N-acetyl-L-glutamine
-
25C, pH 7.4
1.2
N-acetyl-L-histidine
-
25C, pH7.4
2.77
N-acetyl-L-histidine
-
25C, pH 7.4
1.28
N-acetyl-L-isoleucine
-
25C, pH 7.4
55.5
N-acetyl-L-leucine
-
25C, pH7.4
160
N-acetyl-L-leucine
-
25C, pH 7.4
19
N-acetyl-L-Met
-
analysis by HPLC, pH 7.6, 37C
30
N-acetyl-L-Met
-
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37C
65
N-acetyl-L-Met
-
analysis by HPLC, pH 7.6, 37C
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
38.3
N-acetyl-L-methionine
-
25C, pH7.4
45.6
N-acetyl-L-methionine
O58754
pH 7.5, 85C, wild-type enzyme
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
134
N-acetyl-L-methionine
-
kcat for the hydrolysis of N-acetyl-L-methionine substrates by pAcy1
134
N-acetyl-L-methionine
-
25C, pH 7.4
370
N-acetyl-L-methionine
O58453
-
156
N-acetyl-L-norleucine
-
25C, pH7.4
266
N-acetyl-L-norleucine
-
25C, pH 7.4
0.0208
N-acetyl-L-phenylalanine
O58754
pH 7.5, 85C, mutant enzyme C102S
0.14
N-acetyl-L-phenylalanine
-
25C, pH7.4
0.81
N-acetyl-L-phenylalanine
-
25C, pH 7.4
34
N-acetyl-L-phenylalanine
O58754
pH 7.5, 85C, wild-type enzyme
37.3
N-acetyl-L-phenylalanine
O58754
pH 7.5, 85C, mutant enzyme E367Q
1.21
N-acetyl-L-threonine
-
25C, pH 7.4
2.23
N-acetyl-L-threonine
-
25C, pH7.4
0.6
N-acetyl-L-tyrosine
-
E167R mutant protein, pH not specified in the publication, temperature not specified in the publication
1.7
N-acetyl-L-Val
-
analysis by HPLC, pH 7.6, 37C
-
2
N-acetyl-L-Val
-
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37C
-
11.9
N-acetyl-L-valine
-
25C, pH 7.4
14.7
N-acetyl-L-valine
-
25C, pH7.4
2.3
N-acetylmethionine
-
pH 8.0, 22C
0.0101
N-benzoyl-L-glutamate
-
kcat for the hydrolysis of N-acyl-L-glutamate substrates by hAcy1
0.115
N-benzoyl-L-glutamate
-
kcat for the hydrolysis of N-acetyl-L-glutamate substrates by pAcy1
0.158
N-benzoyl-L-methionine
-
kcat for the hydrolysis of N-acyl-L-methionine substrates by hAcy1
1.3
N-benzoyl-L-methionine
-
kcat for the hydrolysis of N-acetyl-L-methionine substrates by pAcy1
20.1
N-benzoyl-L-methionine
-
kcat for the hydrolysis of N-acyl-L-methionine substrates by hAcy1-T347S-mutant
3620
N-benzoyl-L-phenylalanine
-
S100T/M106K mutant protein, pH 8.0, 55C
5900
N-benzoyl-L-phenylalanine
-
F251K mutant protein, pH 8.0, 55C
21300
N-benzoyl-L-phenylalanine
-
wild type protein, pH 8.0, 55C
98.1
N-benzoyl-L-valine
-
F251K mutant protein, pH 8.0, 55C
1760
N-benzoyl-L-valine
-
wild type protein, pH 8.0, 55C
9380
N-benzoyl-L-valine
-
S100T/M106K mutant protein, pH 8.0, 55C
107
N-butanoyl-L-methionine
-
kcat for the hydrolysis of N-acetyl-L-methionine substrates by pAcy1
139
N-butanoyl-L-methionine
-
kcat for the hydrolysis of N-acyl-L-methionine substrates by hAcy1
2 - 8
N-CBZ-Gly-Ala
-
-
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
0.145
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
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
200
N-formyl-Lmethionine
-
kcat for the hydrolysis of N-acetyl-L-methionine substrates by pAcy1
7.9
N-formylmethionine
-
pH 8.0, 22C
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
4.3
N-hexanoyl-L-methionine
-
kcat for the hydrolysis of N-acetyl-L-methionine substrates by pAcy1
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
89.8
N-isobutanoyl-L-methionine
-
kcat for the hydrolysis of N-acetyl-L-methionine substrates by pAcy1
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
0.694
N-isopentanoyl-L-methionine
-
kcat for the hydrolysis of N-acetyl-L-methionine substrates by pAcy1
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
6.08
N-isopentanoyl-L-methionine
-
kcat for the hydrolysis of N-acetyl-L-methionine substrates by pAcy1
16.2
N-pentanoyl-L-methionine
-
kcat for the hydrolysis of N-acyl-L-methionine substrates by hAcy1
18.2
N-pentanoyl-L-methionine
-
kcat for the hydrolysis of N-acetyl-L-methionine substrates by pAcy1
25.7
N-propionyl-L-methionine
-
kcat for the hydrolysis of N-acyl-L-methionine substrates by hAcy1
168
N-propionyl-L-methionine
-
kcat for the hydrolysis of N-acetyl-L-methionine substrates by pAcy1
0.006
Nalpha-acetylmethionine
-
pH 7.4, 22C, recombinant mutant D274A
0.015
Nalpha-acetylmethionine
-
pH 7.4, 22C, recombinant mutant H206N
0.086
Nalpha-acetylmethionine
-
pH 7.4, 22C, recombinant mutant H206A
0.149
Nalpha-acetylmethionine
-
pH 7.4, 22C, recombinant mutant H206K
0.458
Nalpha-acetylmethionine
-
pH 7.4, 22C, recombinant mutant N263D
0.667
Nalpha-acetylmethionine
-
pH 7.4, 22C, recombinant mutant R276A
38.3
Nalpha-acetylmethionine
-
pH 7.4, 22C, recombinant wild-type enzyme
80
2-acetylamino-3-[(S)-1-((R)-hydroxyphenyl-methyl)-2-oxo-2-phenyl-ethylsulfanyl]-propionic acid
-
analysis by HPLC, pH 7.6, 37C
additional information
additional information
-
kinetics of mutants N263D, R276N, and R276Q are not measurable
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
52
2-acetylamino-3-((1S,2S)-2-hydroxycyclohexylsulfanyl)-propionic acid
-
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37C
12221
100
2-acetylamino-3-((1S,2S)-2-hydroxycyclohexylsulfanyl)-propionic acid
-
analysis by HPLC, pH 7.6, 37C
12221
240
2-acetylamino-3-((1S,2S)-2-hydroxycyclohexylsulfanyl)-propionic acid
-
analysis by HPLC, pH 7.6, 37C
12221
300
2-acetylamino-3-((3S,4S)-2-hydroxy-2,2-dimethyl-chroman-4-ylsulfanyl)-propionic acid
-
analysis by HPLC, pH 7.6, 37C
12220
500
2-acetylamino-3-((3S,4S)-2-hydroxy-2,2-dimethyl-chroman-4-ylsulfanyl)-propionic acid
-
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37C
12220
750
2-acetylamino-3-((3S,4S)-2-hydroxy-2,2-dimethyl-chroman-4-ylsulfanyl)-propionic acid
-
analysis by HPLC, pH 7.6, 37C
12220
3
2-acetylamino-3-((3S,4S)-2-hydroxycyclooctylsulfanyl)-propionic acid
-
analysis by HPLC, pH 7.6, 37C
0
49
2-acetylamino-3-[(S)-1-((R)-hydroxyphenyl-methyl)-2-oxo-2-phenyl-ethylsulfanyl]-propionic acid
-
analysis by HPLC, pH 7.6, 37C
12222
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, 37C
12222
270
2-acetylamino-3-[(S)-1-((R)-hydroxyphenyl-methyl)-2-oxo-2-phenyl-ethylsulfanyl]-propionic acid
-
analysis by HPLC, pH 7.6, 37C
12222
23
N-acetyl-L-Cys
-
analysis by HPLC, pH 7.6, 37C
3827
36
N-acetyl-L-Cys
-
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37C
3827
60
N-acetyl-L-Cys
-
analysis by HPLC, pH 7.6, 37C
3827
95
N-acetyl-L-Met
-
analysis by HPLC, pH 7.6, 37C
6635
100
N-acetyl-L-Met
-
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37C
6635
130
N-acetyl-L-Met
-
analysis by HPLC, pH 7.6, 37C
6635
4
N-acetyl-L-Val
-
analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37C
0
4.3
N-acetyl-L-Val
-
analysis by HPLC, pH 7.6, 37C
0
608
N-benzoyl-L-phenylalanine
-
F251K mutant protein, pH 8.0, 55C
12223
904
N-benzoyl-L-phenylalanine
-
S100T/M106K mutant protein, pH 8.0, 55C
12223
2500
N-benzoyl-L-phenylalanine
-
wild type protein, pH 8.0, 55C
12223
19.6
N-benzoyl-L-valine
-
F251K mutant protein, pH 8.0, 55C
9474
263
N-benzoyl-L-valine
-
wild type protein, pH 8.0, 55C
9474
874
N-benzoyl-L-valine
-
S100T/M106K mutant protein, pH 8.0, 55C
9474
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.93
benzyloxycarbonyl-Gly-Gly-Phe
O58754
pH 7.5, 85C
0.001
L-benzylsuccinate
O58754
pH 7.5, 85C
-
0.025
L-benzylsuccinate
-
pH not specified in the publication, temperature not specified in the publication
-
247
Nac-L-Met
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
Nepsilon-formyl-Nepsilon-hydroxy-L-lysine
-
IC50: 1.0 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00000028
G8EJ32
substrate N-linolenoyl-L-glutamine, protein partially purified from frass, pH 8.0, 20C
0.0006
-
S100T/M106K mutant protein, substrate N-acetylpipecolic acid, pH 8.0, 55C
0.003
-
F251K mutant protein, substrate N-acetylpipecolic acid, pH 8.0, 55C; S100T/M106K mutant protein, substrate N-benzoyl-L-tert-leucine, pH 8.0, 55C
0.0042
-
transformant 1 with plasmid pSACY2
0.0045
-
transformant 2 with plasmid pSACY2
0.005
-
F251K mutant protein, substrate N-benzoyl-L-isoleucine, pH 8.0, 55C
0.008
-
F251K mutant protein, substrate N-benzoyl-L-tert-leucine, pH 8.0, 55C
0.0092
-
pH 8.0, temperature not specified in the publication, substrate: acetyl-DL-Trp
0.012
-
transformant 1 with pMACY2
0.02
-
transformant 2 with pMACY2
0.024
-
wild type protein, substrate N-acetylpipecolic acid, pH 8.0, 55C
0.025
-
transformant 3 with pMACY2
0.026
-
S100T/M106K mutant protein, substrate N-benzoyl-L-isoleucine, pH 8.0, 55C
0.075
-
wild type protein, substrate N-benzoyl-L-tert-leucine, pH 8.0, 55C
0.112
-
F251K mutant protein, substrate N-benzoyl-L-valine, pH 8.0, 55C
0.12
-
N-acetyl-D-Phe 8 mM
0.19
-
wild type protein, substrate N-benzoyl-L-isoleucine, pH 8.0, 55C
0.37
-
N-CBZ-Ile-Pro 6 mM
0.55
-
for DR_ACY/CP; N-acetyl-L-Trp 8 mM
0.89
C9K2Z6
native wild-type enzyme, culture supernatant, substrate N-acetyl-L-methionine, pH 7.5, 37C; recombinant wild-type enzyme, culture supernatant, substrate N-acetyl-L-methionine, pH 7.5, 37C
1.16
-
N-CBZ-Ala-Glu 6 mM
1.256
-
F251K mutant protein, substrate N-acetyl-L-phenylalanine, pH 8.0, 55C
1.405
-
S100T/M106K mutant protein, substrate N-acetyl-L-phenylalanine, pH 8.0, 55C
1.55
-
S100T/M106K mutant protein, substrate N-benzoyl-L-phenylalanine, pH 8.0, 55C
1.679
-
wild type protein, substrate N-benzoyl-L-valine, pH 8.0, 55C
1.74
-
N-acetyl-L-homophenylalanine 8 mM
2.15
-
F251K mutant protein, substrate N-benzoyl-L-phenylalanine, pH 8.0, 55C
2.2
-
purified enzyme
2.49
-
N-CBZ-L-Ser 6 mM
2.52
-
N-acetyl-L-Leu 8 mM
2.9
-
recombinant wild-type enzyme, substrate L-methionine, synthesis reaction, pH 6.0, 25C
2.95
-
N-CBZ-L-Phe 6 mM
3.32
-
S100T/M106K mutant protein, substrate N-benzoyl-L-valine, pH 8.0, 55C
4
C9K2Z6
using N-lauroyl-L-Arg as substrate, at 37C, pH not specified in the publication
5.27
-
N-CBZ-Gly-Gly-Phe 6 mM
5.32
-
N-CBZ-L-Glu 6 mM
5.555
-
wild type protein, substrate N-acetyl-L-phenylalanine, pH 8.0, 55C
5.58
-
N-CBZ-L-His 6 mM
5.73
-
for ACY; N-acetyl-L-Met 8 mM
6
C9K2Z6
using N-lauroyl-L-Asn as substrate, at 37C, pH not specified in the publication; using N-lauroyl-L-His as substrate, at 37C, pH not specified in the publication
6.4
-
H79A-mutant, 25°C
6.8
-
wild type protein, substrate N-benzoyl-L-phenylalanine, pH 8.0, 55C
6.84
-
N-chloroacetyl-L-Phe 8 mM
8
C9K2Z6
using N-acetyl-Gly as substrate, at 37C, pH not specified in the publication; using N-acetyl-L-Asp as substrate, at 37C, pH not specified in the publication
8.07
-
N-CBZ-Gly-Leu 6 mM
8.33
-
pH 8.0, 37C
8.4
-
N-acetyl-L-Phe 8 mM
8.54
-
N-CBZ-Ala-Met 6 mM
9.2
-
N261A-mutant, 25°C
9.4
-
activity of the dimer toward S-benzyl-N-acetyl-L-cysteine
9.4
-
D112A-mutant, 25°C
10.3
-
Wild type BL21 (DE3), 25°C
10.7
-
N-CBZ-Gly-Tyr 6 mM
11.26
-
N-acetyl-L-His 8 mM
11.7
-
activity of the tetramer toward S-benzyl-N-acetyl-L-cysteine
13.6
-
E146A-mutant, 25°C
14
C9K2Z6
using N-acetyl-L-Gln as substrate, at 37C, pH not specified in the publication; using N-lauroyl-L-Lys as substrate, at 37C, pH not specified in the publication
15.1
-
N-CBZ-Gly-Ala 6 mM
17
C9K2Z6
using N-lauroyl-L-Cys as substrate, at 37C, pH not specified in the publication
19
C9K2Z6
using N-acetyl-L-Phe as substrate, at 37C, pH not specified in the publication
22
-
purified enzyme, substrate N-lauroyl-L-tryptophan
24
C9K2Z6
using N-acetyl-L-Val as substrate, at 37C, pH not specified in the publication
25
-
purified enzyme, substrate N-lauroyl-L-phenylalanine
25.7
-
E147A-mutant, 25°C
31
C9K2Z6
using N-acetyl-L-Asn as substrate, at 37C, pH not specified in the publication
32.6
-
H371A-mutant, 25°C
34
C9K2Z6
using N-lauroyl-Gly as substrate, at 37C, pH not specified in the publication
36
C9K2Z6
using N-lauroyl-L-Ser as substrate, at 37C, pH not specified in the publication
53.6
-
E174A-mutant, 25°C
59
C9K2Z6
using N-acetyl-L-His as substrate, at 37C, pH not specified in the publication
60
C9K2Z6
using N-acetyl-L-Leu as substrate, at 37C, pH not specified in the publication
66
C9K2Z6
using N-acetyl-L-Arg as substrate, at 37C, pH not specified in the publication
70
-
purified enzyme, substrate N-lauroyl-L-glutaminyl-L-lysine
72
C9K2Z6
using 3 mM N-lauroyl-L-Met as substrate, at 37C, pH not specified in the publication
77
-
recombinant wild-type enzyme, substrate N-acetyl-L-methionine, hydrolytic reaction, pH 6.0, 25C
78.5
-
H205L-mutant, 25°C
87
-
purified enzyme, substrate N-lauroyl-L-valine
89
C9K2Z6
using 3 mM N-decanoyl-L-Met as substrate, at 37C, pH not specified in the publication
90
-
purified enzyme, substrate N-lauroyl-L-glutamyl-glycine; purified enzyme, substrate N-lauroyl-L-isoleucine
96
C9K2Z6
purified recombinant wild-type enzyme, substrate N-lauryl-L-alanine, pH 7.5, 37C; using N-lauroyl-L-Ala as substrate, at 37C, pH not specified in the publication
105
C9K2Z6
using 3 mM N-palmitoyl-L-Met as substrate, at 37C, pH not specified in the publication
106
C9K2Z6
using 3 mM N-myristoyl-L-Met as substrate, at 37C, pH not specified in the publication
110
-
purified enzyme, substrate N-lauroyl-L-glutaminyl-glycine
118
-
purified enzyme, substrate N-lauroyl-L-histidine
129
-
purified enzyme, substrate N-lauroyl-L-leucine
138
-
purified enzyme, substrate N-lauroyl-L-aspartic acid
145
-
purified enzyme, substrate N-lauroyl-L-tyrosine
169
C9K2Z6
using 3 mM N-butyryl-L-Met as substrate, at 37C, pH not specified in the publication
173
C9K2Z6
using 3 mM N-acetyl-L-Met as substrate, at 37C, pH not specified in the publication
175
C9K2Z6
using 3 mM N-hexanoyl-L-Met as substrate, at 37C, pH not specified in the publication
177
-
purified enzyme, substrate N-lauroyl-L-methionine
194
-
purified enzyme, substrate N-lauroyl-L-arginine
194
C9K2Z6
using N-acetyl-L-Ala as substrate, at 37C, pH not specified in the publication
196
-
purified enzyme, substrate N-lauroyl-L-glutamic acid
197
-
R274A-mutant, 25°C
203
-
E309H-mutant, 25°C
210
-
purified enzyme, substrate capsaicin
220
-
Wild type Rosetta (DE3), 25°C
221
-
purified enzyme, substrate N-lauroyl-L-glutamine
222
-
purified enzyme, substrate N-lauroyl-glycine
227
-
purified enzyme, substrate N-lauroyl-L-asparagine
230
-
purified enzyme, substrate N-lauroyl-L-threonine
236
-
purified enzyme, substrate N-lauroyl-L-alanine
244
-
purified enzyme, substrate N-lauroyl-L-lysine
251
C9K2Z6
using 3 mM N-octanoyl-L-Met as substrate, at 37C, pH not specified in the publication
287
-
native porcine enzyme, 25°C
295
-
purified enzyme, substrate N-lauroyl-L-serine
412
C9K2Z6
purified recombinant wild-type enzyme, substrate N-acetyl-L-cysteine, pH 7.5, 37C; using N-acetyl-L-Cys as substrate, at 37C, pH not specified in the publication
440
C9K2Z6
purified native wild-type enzyme, substrate N-acetyl-L-methionine, pH 7.5, 37C
530
C9K2Z6
purified recombinant wild-type enzyme, substrate N-acetyl-L-methionine, pH 7.5, 37C; using 15 mM N-acetyl-L-Met as substrate, at 37C, pH not specified in the publication
additional information
-
maximum specific activity 22.25-27.75 U/ml at 40C and pH 7
additional information
Q6AYS7
-
additional information
-
-
additional information
-
1.74 U/mg in phosphate buffer and 0.88 U/mg in 0.1M Tris-HCl buffer
additional information
C9K2Z6
substrate specificities of recombinant and native enzyme, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.6 - 7.2
-
different optima for various substrates
5.7
-
with palmitoylaspartate as substrate
6
-
synthesis of N-acetyl-L-methionine
7
-
soluble enzyme
7
-
N-chloroacetyl-alanine as substrate, Co2+ enzyme
7.2
-
hydrolysis of 3-(2-furyl)acryloyl-L-methionine
7.3 - 7.6
-
immobilized enzyme
7.4
-
assay at
7.5 - 8
-
-
7.5
-
immobilized enzyme
7.5
-
assay at
7.5
-
assay at
7.5
-
-
7.5
-
assay at
7.5
-
with Mes buffer
7.7 - 7.8
-
assay at
8
Q6AYS7
assay at
8
-
assay at; with Tris-HCl or phosphate buffers
8.5
-
-
8.5
-
N-chloroacetyl-alanine as substrate, Zn2+ enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.7 - 10.8
-
using different buffers containing N-acetyl-D-Homophenylalanine or N-acetyl-L-Homophenylalanine
4 - 6.5
-
-
4.5 - 7.2
-
activity range, substrate N-acetyl-L-methionine
6 - 10.3
-
90% activity
6 - 8.5
O58453
-
6.5 - 9.5
-
at least 70% of the activity is present between pH 6.5 and 9.5
7.5 - 7.7
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
-
assay at room temperature
22
-
assay at room temperature
25
-
assay at
25
-
assay at
25
-
assay at
37
Q6AYS7
assay at
37.5
-
assay at
40
-
assay at
50
C9K2Z6
; at pH 7.5
60
-
soluble enzyme
65
-
immobilized enzyme
65
-
immobilized enzyme
85
-
1 h, Tris-HCl at pH 8.0; at pH 8.0
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 80
-
-
25 - 75
-
-
60 - 100
O58453
-
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Bacillus subtilis (strain 168)
Staphylococcus aureus (strain COL)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26000
-
SDS-PAGE
664342
37000
-
-
288863
37000
-
subunit, SDS-PAGE
288863
40000
-
gel filtration, long acyl aminoacylase, hydrolysis of N-long chain fatty acyl amino acids
288855
42000
-
-
678901
42500
-
calculated from amino acid composition
288863
43000
-
bifunctional DR_ACY/CP is purified by SDS-PAGE
680973
44000
-
gel filtration
658227
45000
-
gel filtration
667685
50000
C9K2Z6
SDS-PAGE
711509
55000
C9K2Z6
; blue native PAGE
711509
56000
-
gel filtration
31930
57000
-
SDS-PAGE
664342
73200
-
-
288857
74000
-
-
288867
75000
-
gel filtration
669031
80000
-
gel filtration
288860
80000
-
gel filtration
288867
85500
-
amino acid composition estimation
288856
85500
-
-
288857
86000
-
gel filtration
288856
88000
-
gel filtration, short acyl aminoacylase
288855
90000
-
gel filtration
288870
90000
-
gel filtration chromatography
657988
108000
-
gel filtration, native enzyme
288872
125000
-
gel filtration
658227
135000
-
gel filtration
288857
140000
-
expressed in HEK293T cells
679474
165000
O58453
under native conditions, homotetrameric structure
679801
168000
-
gel filtration, low glutaraldehyde concentration, native tetrameric form
288866
170000
-
gel filtration
724947, 726571
175000
-
gel permeation
288863
175000
-
-
288867
180000
-
gel filtration
288866
197000
G8EJ32
gel filtration
719598
950000
-
native-PAGE
695818
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
O58754
x * 43000, SDS-PAGE
?
Q6AYS7
x * 45000, SDS-PAGE
?
G8EJ32
x * 64000, recombinant protein about 50000, SDS-PAGE
?
Pyrococcus horikoshii OT-3
-
x * 43000, SDS-PAGE
-
dimer
-
-
dimer
-
2 * 40000, SDS-PAGE
dimer
-
2 * 40000, SDS-PAGE
dimer
-
2 * 42000, SDS-PAGE
dimer
-
2 * 43000, SDS-PAGE
dimer
-
2 * 43000, SDS-PAGE
dimer
-
2 * 43000, SDS-PAGE
dimer
-
dissociable enzyme, monomer and dimer forms
dimer
-
2 * 36600, SDS-PAGE
dimer
-
2 * 45000, denaturated intestinal mucosa enzyme, SDS-PAGE
dimer
-
2 * 50000, native enzyme SDS-PAGE
dimer
-
2 * 44147, deduced from nucleotide sequence
dimer
-
2 * 45216, gel filtration and calculated from DNA sequence, 2 * 45260, gel filtration and ESI-MS following a desalting step on a RP-HPLC column
dimer
-
1 * 26000 + 1 * 57000, SDS-PAGE
dimer
-
1 * 61000 + 1 * 19000, SDS-PAGE, the enzyme is active only as complete heterodimer
dimer
Aspergillus oryzae No.9
-
-
-
dimer
Lactococcus lactis MG1363
-
2 * 42000, SDS-PAGE, 2 * 44147, deduced from nucleotide sequence
-
homodimer
-
2 * 45000 Da, SDS-PAGE
homotetramer
-
4 * 43000, SDS-PAGE
homotetramer
-
PAGE
homotetramer
-
SDS-PAGE before and after boiling with beta-mercaptoethanol
homotetramer
-
4 * 43000, SDS-PAGE, sedimentation studies, 4 * 43814, calculated from sequence, 4 * 43815, calculated from sequence
monomer
-
1 * 54000, SDS-PAGE
monomer
-
1 * 45000, SDS-PAGE
monomer
-
1 * 44000, denaturing and reducing gels
monomer
C9K2Z6
1 * 55000, 1 * 55000, purified wild type enzyme, SDS-PAGE
tetramer
-
-
tetramer
-
4 * 42000, SDS-PAGE
tetramer
-
4 * 43000, 4gatom Zn per mol enzyme, SDS-PAGE
tetramer
O58453
4* 42000 SDS-PAGE, recombinant enzyme
trimer
-
3 * 44000, gel filtration and SDS-PAGE, 3 * 45847, deduced from deduced aminacid sequence
monomer
-
1 * 55000, purified wild type enzyme, SDS-PAGE
additional information
-
dimerization domain residues play important roles in binding and catalysis, overview
additional information
Q6AYS7
structure molecular modelling
additional information
-
structural homology modeling, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1.5 A resolution
-
hanging drops at pH 5.6 by the vapour-diffusion method using 30% polyethyleneglycol as precipitant
-
hanging drop vapor diffusion technique
-
the enzyme is crystallized from ammonium sulfate using the sitting-drop vapour-diffusion method. The crystals diffract to 2.8 A resolution and belong to the rhombohedral space group R32, with unit-cell parameters a = b = 102.4, c = 178.5 A, gamma = 120 in a hexagonal lattice setting. The asymmetric unit contains one enzyme monomer, containing a single zinc ion
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8
-
stable in wide pH-range, 5-8 at 30C and 7-7.5 at 55C
288872
5 - 8
-
50 mm Tris, 0.5 mM Co2+, 37C, stable
669031
5 - 9
-
-
288867
5.5 - 8.5
-
stable in 0.1 M potassium phosphate buffer at 55, 60 and 70C, maximum stability from pH 6.5-6.6, immobilized enzyme at pH 7.2
288859
6 - 11.5
-
no activity lost at 37C for 1h
288863
7 - 8.5
-
gradually inactivated below pH 7 or above pH 8.5, all activity lost below pH 4 and above pH 10
288870
8
-
most stable in borate buffer
31930
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
most stable at this temperature
657573
45
-
up to apoenzyme is less heat sensitive than the active holoenzyme
288862
45
-
thermostable up to, 60% activity remains at 50C
31930
50 - 65
-
retains 80% initial activity up to 50C, becomes rapidly inactive above 65C
288870
55
-
1 h, pH 7.8, stable, above 55C the enzyme is stable only in presence of Co2+
669031
60
-
denaturation at 60C
288857
60
-
retains 80% activity after 1 h at 60C
288867
70 - 80
-
retains full activity on heating at 70C for 10 min, 90% of the original activity after heating at 80%, much activity lost on 30 min at 80C
288863
70
-
immobilized enzyme more thermally stable, preserved during prolonged incubation at 70C, soluble enzyme completely inactivated in 10 min under same conditions
288859, 288873
70
-
half-life: 25 h
724947
85
-
half-life: 1.7 h
724947
90
-
no loss of activity during 12 h (Zn2+)-enzyme, half-life time: 4 h (Mn2+)-enzyme, 12 h (Ni2+)-enzyme
696896
100
-
half activity after 1 h (Zn2+)-enzyme
696896
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
very active and physically stable, resistant to urea, 85% activity retained with 8 M urea at 37C for 30 min
-
Co2+ activates and stabilizes
-
relatively stable, urea causes marked activation of the immobilized enzyme, immobilized enzyme resistant against denaturation by guanidinium hydrochloride
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DMSO
-
20% decrease in activity of immobilised enzyme at 5% (v/v) DMSO
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
47C, pH 8.0, 0.2% w/v, 0.1 M sodium phosphate buffer, no and 23% remaining activity for the free aminoacylase and the immobilized, cross-linked enzyme-bovine serum albumin aggregate, respectively, after 24 h
-
4C, 0.03 M phosphate buffer, 0.4 M NaCl, pH 7.3 may be stored for several months with negligible loss of activity
-
4C, relatively stable when stored in presence of Zn2+, loses less than 20% activity per month
-
-20C, 0.2 mM DTT buffer, pH 6.8, retains its acivity for 6 months
-
4C for at least 2 weeks with little loss of activity
-
4C, immobilized enzyme stable for more than 2 months without significant loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using either Ni-NTA (Qiagen), Fractogel HW-50S and HiTrap Q (Pharmacia Biotech) columns or an NiNTA (Quiagen) column only
-
recombinant protein, expressed in Escherichia coli
-
purified by a method that includes DEAE-Sepharose CL-6B anion exchange resin, phenyl-Sepharose hydrophobic interaction resin, Mono Q strong anion exchange column and Mono P weak anion exchange column
-
from frass: ion exchange chromatography (Q-Sepharose), gel filtration, ion exchange chromatography (Mono-Q, gel filtration), recombinant protein from inclusion bodies: immobilized metal ion affinity chromatography (Co2+)
G8EJ32
commercial preparation
-
recombinant GST-tagged C-terminal fragment from an in vitro expression system by glutathione affinity chromatography
-
StrepTactin Sepharose
-
both short acyl aminoacylase and long acyl aminoacylase
-
in 50 mM Tris/HCl-buffer, pH 8 and disrupted by ultrasonication
O58453
by a method that includes DEAE-Sepharose column, Chelating-Sepharose column, Amicon PM 30 membrane and Sephacryl-S200 column
-
native enzyme from intestinal epithelial mucosa, 1833fold to homogeneity, by acid precipitation, two steps of anion exchange chromatography, hydrophobic interaction chromatography, gel filtration and concanavalin A afinity chromatography
-
recombinant GST-tagged wild-type and mutant enzymes from bacteria by solubilization with Triton X-100 and 10% sarcosyl, glutathione affinity chromatography, and tag removal by thrombin
Q6AYS7
ammonium sulfate precipitation, octyl-Sepharose column chromatography, HiTrap chelating column chromatography, and DEAE Sephadex A-50 ion exchange chromatography; Streptomyces lividans strain TK24, native enzyme 494fold from by ammonium sulfate fractionation, anion exchange chromatography, and hydrophobic interaction chromatography
C9K2Z6
native enzyme 1300fold by ammonium sulfate fractionation, dialysis, ion exchange chromatography, hydroxyapatite chromatography, and a second step of dialysis
-
partially
-
commercial preparation
-
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
-
anion exchange chromatography, hydrophobic interaction chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
genomic DNA fragment encoding aminoacylase cloned, sequenced and expressed in Escherichia coli
-
expressed in Escherichia coli
-
expression in Escherichia coli
-
expression in Baculovirus
-
expression of His6-tagged AA3 in HEK-293 cells
-
expressed in Escherichia coli
-
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
-
expression in HEK293T cells
-
expression in Acremonium chrysogenum IS-5, transformants with pSACY2 or pMACY2
-
expression in Escherichia coli
O58453
ACYI, DNA and amino acid sequence determination and analysis, comparison with the porcine intestinal enzyme
Q6AYS7
expressed in Escherichia coli strain BL21(DE3)
-
expression of GST-tagged wild-type and mutant enzymes in bacteria
Q6AYS7
DNA and amino acid sequence determination and analysis, sequence comparisons, subcloning in Escherichia coli strain DH5alpha, expression in Streptomyces lividans strain TK24 resulting in 42fold higher activity compared to the native wild-type Streptomyces mobaraensis strain; expressed in Streptomyces lividans strain TK24
C9K2Z6
ACYI, DNA and amino acid sequence determination and analysis, comparison with the rat kidney enzyme
-
expression in Baculovirus
-
expression in E. coli
-
expression of pAcy1 in Escherichia coli strain BL21 (DE3)
-
expressed in Escherichia coli
-
overexpressed in Escherichia coli; overexpressed in Escherichia coli, modification of N-terminal residues of the recombinant enzyme to enhance expression in Escherichia coli using the vector pUCcer11. The recombinant enzyme has an insertion of four amino acids (Glu-Pro-Leu-Phe) between the N-terminal methionine and the second residue lysine of the wild type
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
I177A
-
2.7fold increased KM-value compared to the wildtype with N-acetyl-L-methionine moiety, 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, 5.2fold increased KM-value compared to the wildtype with N-hexanoyl-L-methionine moiety
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
-
1,7fold increased KM-value compared to the wildtype with N-isopentanoyl-L-methionine moiety, 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, 7.9fold decreased KM-value compared to the wildtype with N-isopentanoyl-L-methionine moiety
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
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
-
1.1fold decreased KM-value compared to the wildtype with N-acetyl-L-methionine moiety, 5.3fold decreased KM-value compared to the wildtype with N-cyclohexanoyl-L-methionine moiety
D68A
-
site-directed mutagenesis of AA3, the mutant is inactive
E167R
-
involved in substrate specificity
E177A
-
site-directed mutagenesis of AA3, the mutant is inactive
E177A
-
catalytically inactive but maintained the structural integrity of active site
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
C102A
O58754
no hydrolytic activity
C102S
O58754
Km-values are similar to those of wild-type enzyme
E367Q
O58754
the kcat-value increases slightly, whereas the Km value does not change for N-acetyl-L-phenylalanine as substrates. Substrate inhibition of aminoacylase activity is also observed. The temperature-dependent activity and pH profile of the activity of E367Q are similar to those of wild-type enzyme
C102A
Pyrococcus horikoshii OT-3
-
no hydrolytic activity
-
C102S
Pyrococcus horikoshii OT-3
-
Km-values are similar to those of wild-type enzyme
-
E367Q
Pyrococcus horikoshii OT-3
-
the kcat-value increases slightly, whereas the Km value does not change for N-acetyl-L-phenylalanine as substrates. Substrate inhibition of aminoacylase activity is also observed. The temperature-dependent activity and pH profile of the activity of E367Q are similar to those of wild-type enzyme
-
C23A
Q6AYS7
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
C272A
Q6AYS7
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
C294A
Q6AYS7
site-directed mutagenesis, the mutation causes a conformational change of the 3D-structure, the mutant shows highly reduced activity compared to the wild-type enzyme
C331A
Q6AYS7
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
C49A
Q6AYS7
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
D82E
Q6AYS7
site-directed mutagenesis, the mutant shows highly reduced activity and loss of zinc coordination compared to the wild-type enzyme
D82N
Q6AYS7
site-directed mutagenesis, nearly inactive mutant
E147A
-
completely inactive
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
D212Y
-
lower temperature stability than wild type protein
E336A
-
total knockout
E336I
-
total knockout
E336S
-
partial activity
F251K
-
impaired activity towards N-benzoyl-L-valine but not towards N-benzoyl-L-phenylalanine
F251R
-
impaired activity towards N-benzoyl-L-valine but not towards N-benzoyl-L-phenylalanine
F251Y
-
32% increase in activity towards N-benzoyl-L-valine, activity towards N-benzoyl-L-phenylalanine unaffected, tetrameric form retained after 1 h at 55C like wild type protein
G246E/I274K
-
decreased activity on N-benzoyl-L-phenylalanine at higher temperature
H169N
-
lower activity than mutant protein H169R
H169Q
-
lower activity than mutant protein H169R
H169R
-
low activity
K226R/P234H/F251Y/I254N
-
37% increase in activity towards N-benzoyl-L-phenylalanine, lower temperature stability than wild type protein
L187F
-
may be involved in altering the relative flexibility or conformation
P237S
-
tetrameric form retained after 1 h at 55C like wild type protein
S100T/M106K
-
51% increase in activity towards N-benzoyl-L-valine, activity towards N-benzoyl-L-phenylalanine unaffected
S100T/M106K/F251Y
-
no further improvement in activity (non-additive interaction between the mutated sites)
S217T/S244I/T250I
-
tetrameric form retained after 1 h at 55C like wild type protein, decreased activity on N-benzoyl-L-phenylalanine at higher temperature
T299H
-
about 50% activity
T299K
-
about 50% activity
T306V
-
may be involved in altering the relative flexibility or conformation
V242D
-
32% increase in activity towards N-benzoyl-L-phenylalanine, lower temperature stability than wild type protein
additional information
-
preparation of cross-linked aggregates of aminoacylase by using bovine serum albumin as an inert additive, cross-linking is conducted at varying glutaraldehyde to enzyme ratio. Cross-linked enzyme aggregates retain 82% of maximal activity in presence of bovine serum albumin, and 24% in its absence
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 4C, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
biocatalytic production of optically active amino acids and their derivatives, which are broadly used as physiologically active compounds, chiral auxiliaries or synthons and as intermediates in pharmaceutical, food and agrochemistry
synthesis
-
production of L-3-(4-thiazolyl)alanine and D-N-acetyl-D-3-(4-thiazolyl)alanine, which are used as a component of antihypertensive inhibitors of the enzyme renin
synthesis
-
enzyme used for production of L-amino acids
synthesis
-
production of L-amino acids, which are used for parental nutrition, feed and food additives, cosmetics, pesticides, and as intermediates for pharmaceuticals as well as chiral synthons for organic synthesis
synthesis
-
the enzyme can be used for production of optically pure L-Phe and D-Phe by usage of N-acetylated DL-Phe, which is hydrolyzed stereospecifically to L-Phe, the remaining N-acetyl-D-Phe can be chemically hydrolyzed to D-Phe. The method can also be applied to racemic Trp and Tyr
synthesis
Aspergillus oryzae No.9
-
-
-
synthesis
-
-
synthesis
-
thermostable enzyme useful for industrial production, optical resolution of DL-amino acids on an industrial scale, utilization in industrial production of stereoisomers from racemates
synthesis
O58754
because of its thermostability, the enzyme is expected to be useful for the production of L-amino acid derivatives from racemates at temperatures over 90C
synthesis
Pyrococcus horikoshii OT-3
-
because of its thermostability, the enzyme is expected to be useful for the production of L-amino acid derivatives from racemates at temperatures over 90C
-
medicine
-
N-acetyl-L-cysteine used for drugs against lung disorders and HIV infections, test of potential antitumor agents
synthesis
-
thermostable enzyme useful for industrial production, optical resolution of DL-amino acids on an industrial scale, utilization in industrial production of stereoisomers from racemates
medicine
-
preparation of commercially important amino acids as components for semisynthetic penicillins and cephalosporins
synthesis
-
thermostable enzyme useful for industrial production, optical resolution of DL-amino acids on an industrial scale, utilization in industrial production of stereoisomers from racemates
analysis
-
enzyme widely used as reagent to resolve amino acid racemates
synthesis
-
industrial applications
synthesis
-
aminoacylase-catalyzed enantioselective synthesis of aromatic beta-amino acids
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