3.5.1.81: N-Acyl-D-amino-acid deacylase
This is an abbreviated version!
For detailed information about N-Acyl-D-amino-acid deacylase, go to the full flat file.
Word Map on EC 3.5.1.81
-
3.5.1.81
-
alcaligenes
-
subsp
-
xylosoxydans
-
faecalis
-
synthesis
-
amidohydrolases
-
binuclear
-
l-aminoacylase
-
denitrificans
-
d-hydantoinase
-
n-acylated
-
semi-synthetic
-
dnak-dnaj-grpe
-
d-leucine
-
d-methionine
-
industry
-
biotechnology
- 3.5.1.81
- alcaligenes
-
subsp
- xylosoxydans
- faecalis
- synthesis
-
amidohydrolases
-
binuclear
- l-aminoacylase
- denitrificans
- d-hydantoinase
-
n-acylated
-
semi-synthetic
-
dnak-dnaj-grpe
- d-leucine
- d-methionine
- industry
- biotechnology
Reaction
Synonyms
AcyM, AxD-NAase, D-AAase, D-AGase, D-amidohydrolase, D-Amino acylase, D-Aminoacylase, D-ANase, D-NAase, DAA, dan, N-Acyl-D-amino acid amidohydrolase, N-acyl-D-amino-acid deacylase, N-Acyl-D-aspartate amidohydrolase, N-acyl-D-glutamate amidohydrolase, N-D-AAase
ECTree
3.5.1.81 N-Acyl-D-amino-acid deacylaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.5.1.81 - N-Acyl-D-amino-acid deacylase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-acetyl-D-allylglycine + H2O
acetate + D-allylglycine
Rhodococcus armeniensis
-
moderate activity
-
-
r
N-acetyl-D-oxyvaline + H2O
acetate + D-oxyvaline
Rhodococcus armeniensis
-
activity is 71.2% compared to the activity with N-acetyl-D-methionine
-
-
?
N-acetyl-DL-methionine + H2O
acetate + D-methionine
Rhodococcus armeniensis
-
high activity
-
-
r
N-acetyl-DL-oxyvaline + H2O
acetate + D-oxyvaline
Rhodococcus armeniensis
-
high activity
-
-
r
N-Benzyloxycarbonyl-D-Leu + H2O
Benzyloxycarbonate + D-Leu
-
fair reactivity
-
-
?
N-Benzyloxycarbonyl-D-Met + H2O
Benzyloxycarbonate + D-Met
-
fair reactivity
-
-
?
beta-Lactam PS-5 + H2O
beta-Lactam NS5 + H2O
-
-
i.e. deacetylated PS-5
?
beta-Lactam PS-5 + H2O
beta-Lactam NS5 + H2O
-
-
i.e. deacetylated PS-5
?
N-acetyl-D-alanine + H2O
acetate + D-alanine
16% of the activity with N-acetyl-D-methionine
-
-
?
N-acetyl-D-alanine + H2O
acetate + D-alanine
Rhodococcus armeniensis
-
activity is 30.7% compared to the activity with N-acetyl-D-methionine
-
-
?
N-acetyl-D-aspartate + H2O
acetate + D-aspartate
25% of the activity with N-acetyl-D-methionine
-
-
?
N-acetyl-D-aspartate + H2O
acetate + D-aspartate
25% of the activity with N-acetyl-D-methionine
-
-
?
N-acetyl-D-aspartate + H2O
acetate + D-aspartate
-
substrate of isozyme D-AAase
-
-
?
N-acetyl-D-aspartate + H2O
acetate + D-aspartate
-
substrate of isozyme D-AAase
-
-
?
N-acetyl-D-glutamate + H2O
acetate + D-glutamate
-
substrate of isozyme D-AGase
-
-
?
N-acetyl-D-glutamate + H2O
acetate + D-glutamate
-
substrate of isozyme D-AGase
-
-
?
N-acetyl-D-leucine + H2O
acetate + D-leucine
61% of the activity with N-acetyl-D-methionine
-
-
?
N-acetyl-D-leucine + H2O
acetate + D-leucine
61% of the activity with N-acetyl-D-methionine
-
-
?
N-acetyl-D-leucine + H2O
acetate + D-leucine
59.9% of the activity with N-acetyl-D-phenylalanine
-
-
?
N-acetyl-D-leucine + H2O
acetate + D-leucine
59.9% of the activity with N-acetyl-D-phenylalanine
-
-
?
N-acetyl-D-leucine + H2O
acetate + D-leucine
Rhodococcus armeniensis
-
activity is 6.8% compared to the activity with N-acetyl-D-methionine
-
-
?
N-acetyl-D-leucine + H2O
acetate + D-leucine
Rhodococcus armeniensis AM6.1
-
low activity
-
-
r
N-acetyl-D-leucine + H2O
acetate + D-leucine
Rhodococcus armeniensis AM6.1
-
activity is 6.8% compared to the activity with N-acetyl-D-methionine
-
-
?
N-Acetyl-D-Met + H2O
acetate + D-Met
-
preferred substrate
-
-
?
N-acetyl-D-methionine + H2O
acetate + D-methionine
best substrate
-
-
?
N-acetyl-D-methionine + H2O
acetate + D-methionine
best substrate
-
-
?
N-acetyl-D-methionine + H2O
acetate + D-methionine
25.1% of the activity with N-acetyl-D-phenylalanine
-
-
?
N-acetyl-D-methionine + H2O
acetate + D-methionine
25.1% of the activity with N-acetyl-D-phenylalanine
-
-
?
N-acetyl-D-methionine + H2O
acetate + D-methionine
Rhodococcus armeniensis
-
high activity, best substrate
-
-
r
N-acetyl-D-methionine + H2O
acetate + D-methionine
Rhodococcus armeniensis AM6.1
-
-
-
-
?
N-acetyl-D-phenylalanine + H2O
acetate + D-phenylalanine
54% of the activity with N-acetyl-D-methionine
-
-
?
N-acetyl-D-phenylalanine + H2O
acetate + D-phenylalanine
54% of the activity with N-acetyl-D-methionine
-
-
?
N-acetyl-D-phenylalanine + H2O
acetate + D-phenylalanine
-
-
-
?
N-acetyl-D-phenylalanine + H2O
acetate + D-phenylalanine
the enzyme purified from the cells of strain TNJL143-2 displays the highest preference for N-acetyl-D-phenylalanine
-
-
?
N-acetyl-D-phenylalanine + H2O
acetate + D-phenylalanine
-
-
-
?
N-acetyl-D-phenylalanine + H2O
acetate + D-phenylalanine
the enzyme purified from the cells of strain TNJL143-2 displays the highest preference for N-acetyl-D-phenylalanine
-
-
?
N-acetyl-D-phenylalanine + H2O
acetate + D-phenylalanine
Rhodococcus armeniensis
-
low activity
-
-
r
N-acetyl-D-phenylalanine + H2O
acetate + D-phenylalanine
Rhodococcus armeniensis
-
activity is 28.8% compared to the activity with N-acetyl-D-methionine
-
-
?
N-acetyl-D-phenylalanine + H2O
acetate + D-phenylalanine
-
-
-
?
N-Acetyl-D-phenylglycine + H2O
acetate + D-phenylglycine
-
-
-
-
?
N-Acetyl-D-phenylglycine + H2O
acetate + D-phenylglycine
-
-
-
-
?
N-acetyl-D-tryptophan + H2O
acetate + D-tryptophan
14% of the activity with N-acetyl-D-methionine
-
-
?
N-acetyl-D-tryptophan + H2O
acetate + D-tryptophan
14.4% of the activity with N-acetyl-D-phenylalanine
-
-
?
N-acetyl-D-tyrosine + H2O
acetate + D-tyrosine
5.0% of the activity with N-acetyl-D-methionine
-
-
?
N-acetyl-D-tyrosine + H2O
acetate + D-tyrosine
Rhodococcus armeniensis
-
activity is 35.1% compared to the activity with N-acetyl-D-methionine
-
-
?
N-acetyl-D-valine + H2O
acetate + D-valine
8.0% of the activity with N-acetyl-D-methionine
-
-
?
N-acetyl-D-valine + H2O
acetate + D-valine
8.0% of the activity with N-acetyl-D-methionine
-
-
?
N-acetyl-D-valine + H2O
acetate + D-valine
Defluvibacter sp.
-
preferred substrate, the enzyme is specific for N-acyl-D-amino acids
-
-
?
N-acetyl-D-valine + H2O
acetate + D-valine
-
preferred substrate, the enzyme is specific for N-acyl-D-amino acids
-
-
?
N-acetyl-D-valine + H2O
acetate + D-valine
6.0% of the activity with N-acetyl-D-phenylalanine
-
-
?
N-acetyl-D-valine + H2O
acetate + D-valine
Rhodococcus armeniensis
-
activity is 9,3% compared to the activity with N-acetyl-D-methionine
-
-
?
N-acyl-D-amino acid + H2O
a carboxylate + D-amino acid
-
-
-
?
N-acyl-D-amino acid + H2O
a carboxylate + D-amino acid
-
-
-
?
N-chloroacetyl-D-phenylalanine + H2O
chloroacetate + D-phenylalanine
2.1-fold higher activity compared to N-acetyl-D-Phe
-
-
?
N-chloroacetyl-D-phenylalanine + H2O
chloroacetate + D-phenylalanine
2.1-fold higher activity compared to N-acetyl-D-Phe
-
-
?
additional information
?
-
-
hydrolysis of N-acetyl-L-amino acids is almost negligible
-
-
?
additional information
?
-
-
the best inducers are a poor substrate, N-acetyl-gamma-methyl-D-Leu, and an inhibitor, N-acetyl-D-alloisoleucine
-
-
?
additional information
?
-
-
isozyme D-ANase is specific for N-acyl derivatives of neutral amino acids, while isozymes D-AAase and D-AGase are specific for N-acyl-D-aspartate and N-acyl-D-glutamate, respectively
-
-
?
additional information
?
-
-
isozyme D-ANase is specific for N-acyl derivatives of neutral amino acids, while isozymes D-AAase and D-AGase are specific for N-acyl-D-aspartate and N-acyl-D-glutamate, respectively
-
-
?
additional information
?
-
-
N-acyl-D-amino acid amidohydrolase catalyzes the hydrolysis of N-acyl-D-amino acid to its corresponding D-amino acid and fatty acid from an amino acid mixture or the N-acyl-DL-amino acid directly
-
-
-
additional information
?
-
-
the aza-Markovnikov addition reactions of 4-nitroimidazole to vinyl acetate catalyzed by D-aminoacylase is up to 1260fold faster than the respective non-enzymatic reaction
-
-
?
additional information
?
-
-
the enzyme catalyzes the carbon-carbon bond formation reaction of 1,3-dicarbonyl compounds to methyl vinyl ketone in organic media
-
-
?
additional information
?
-
no activity with N-acetyl-L-amino acids
-
-
?
additional information
?
-
no activity with N-acetyl-L-amino acids
-
-
?
additional information
?
-
-
no activity with N-acetyl-L-amino acids
-
-
?
additional information
?
-
-
the enzyme acts as a peptidase on dipeptides and tripeptides
-
-
?
additional information
?
-
-
the enzyme acts as a peptidase on dipeptides and tripeptides
-
-
?
additional information
?
-
Rhodococcus armeniensis
-
absolute stereospecificity to the D-stereoisomers of N-acetyl-amino acids. The enzyme does practically not react with acidic and hydrophilic N-acetyl-amino acids
-
-
?
additional information
?
-
Rhodococcus armeniensis
-
exhibits absolute stereospecificity to the D-stereoisomers of N-acetyl-amino acids. The enzyme is most active with N-acetyl-D-methionine, as well as with aromatic and hydrophobic N-acetylamino acids and interacts weakly with basic substrates. It is practically not active with acidic and hydrophilic N-acetyl-amino acids. Substrate specificity, overview. No activity with N-acetyl-L-valine, N-acetyl-DL-serine, N-acetyl-DL-threonine, N-acetyl-DL-aspartic acid, and N-acetyl-L-methionine. Only D-enantiomers are produced in the hydrolysis of the racemic substrates
-
-
-
additional information
?
-
Rhodococcus armeniensis AM6.1
-
absolute stereospecificity to the D-stereoisomers of N-acetyl-amino acids. The enzyme does practically not react with acidic and hydrophilic N-acetyl-amino acids
-
-
?
additional information
?
-
Rhodococcus armeniensis AM6.1
-
exhibits absolute stereospecificity to the D-stereoisomers of N-acetyl-amino acids. The enzyme is most active with N-acetyl-D-methionine, as well as with aromatic and hydrophobic N-acetylamino acids and interacts weakly with basic substrates. It is practically not active with acidic and hydrophilic N-acetyl-amino acids. Substrate specificity, overview. No activity with N-acetyl-L-valine, N-acetyl-DL-serine, N-acetyl-DL-threonine, N-acetyl-DL-aspartic acid, and N-acetyl-L-methionine. Only D-enantiomers are produced in the hydrolysis of the racemic substrates
-
-
-
additional information
?
-
the enzyme hydrolyzes various N-acetyl-D-amino acids that have hydrophobic side chains. The activity toward N-chloroacetyl-D-Phe is 2.1-fold higher than that toward N-acetyl-D-Phe, indicating that the structure of N-acylated portion of substrate alters the activity
-
-
?
additional information
?
-
the enzyme hydrolyzes various N-acetyl-D-amino acids that have hydrophobic side chains. The activity toward N-chloroacetyl-D-Phe is 2.1-fold higher than that toward N-acetyl-D-Phe, indicating that the structure of N-acylated portion of substrate alters the activity
-
-
?
