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Acetate + D-ethionine
N-Acetyl-D-ethionine + H2O
-
-
-
-
?
beta-Lactam PS-5 + H2O
beta-Lactam NS5 + H2O
Formate + D-Met
N-Formyl-D-Met + H2O
-
-
-
-
?
N-Acetyl-D-Ala + H2O
acetate + D-Ala
N-acetyl-D-alanine + H2O
acetate + D-alanine
N-acetyl-D-allylglycine + H2O
acetate + D-allylglycine
Rhodococcus armeniensis
-
moderate activity
-
-
r
N-acetyl-D-arginine + H2O
acetate + D-arginine
Rhodococcus armeniensis
-
low activity
-
-
r
N-Acetyl-D-Asn + H2O
acetate + D-Asn
N-acetyl-D-aspartate + H2O
acetate + D-aspartate
N-acetyl-D-glutamate + H2O
acetate + D-glutamate
N-acetyl-D-Leu + H2O
acetate + D-Leu
N-acetyl-D-leucine + H2O
acetate + D-leucine
N-Acetyl-D-Met + H2O
acetate + D-Met
N-Acetyl-D-Met-Gly + H2O
acetate + D-Met-Gly
-
fair reactivity
-
-
?
N-Acetyl-D-Met-OMe + H2O
acetate + D-Met-OMe
-
fair reactivity
-
-
?
N-acetyl-D-methionine + H2O
acetate + D-methionine
N-Acetyl-D-norleucine + H2O
acetate + D-norleucine
-
-
-
-
?
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-D-Phe + H2O
acetate + D-Phe
N-acetyl-D-phenylalanine + H2O
acetate + D-phenylalanine
N-Acetyl-D-phenylglycine + H2O
acetate + D-phenylglycine
N-Acetyl-D-Trp + H2O
acetate + D-Trp
N-acetyl-D-tryptophan + H2O
acetate + D-tryptophan
N-Acetyl-D-Tyr + H2O
acetate + D-Tyr
-
-
-
-
?
N-acetyl-D-tyrosine + H2O
acetate + D-tyrosine
N-acetyl-D-Val + H2O
acetate + D-Val
N-acetyl-D-valine + H2O
acetate + D-valine
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-acetyl-DL-tyrosine + H2O
acetate + D-tyrosine
Rhodococcus armeniensis
-
low activity
-
-
r
N-acetyl-DL-valine + H2O
acetate + D-valine
Rhodococcus armeniensis
-
low activity
-
-
r
N-Acetyl-Gly + H2O
acetate + Gly
N-acyl-D-amino acid + H2O
a carboxylate + D-amino acid
N-Benzoyl-Ala + H2O
Benzoate + Ala
-
-
-
-
?
N-Benzoyl-D-Leu + H2O
Benzoate + D-Leu
N-Benzoyl-D-Met + H2O
Benzoate + D-Met
N-Benzoyl-D-Phe + H2O
Benzoate + D-Phe
N-Benzoyl-Val + H2O
Benzoate + Val
-
-
-
-
?
N-Benzyloxycarbonyl-D-Leu + H2O
Benzyloxycarbonate + D-Leu
-
fair reactivity
-
-
?
N-Benzyloxycarbonyl-D-Met + H2O
Benzyloxycarbonate + D-Met
-
fair reactivity
-
-
?
N-Butyl-D-Leu + H2O
Butanoate + D-Leu
-
-
-
-
?
N-chloroacetyl-D-phenylalanine + H2O
chloroacetate + D-phenylalanine
N-Chloroacetyl-D-Val + H2O
Chloroacetate + D-Val
N-Formyl-D-Leu + H2O
Formate + D-Leu
-
-
-
-
?
N-Formyl-D-Phe + H2O
Formate + D-Phe
-
-
-
-
?
N-Phenylacetyl-D-Phe + H2O
Phenylacetate + D-Phe
-
-
-
-
?
N-Propionyl-D-Leu + H2O
Propanoate + D-Leu
-
-
-
-
?
additional information
?
-
beta-Lactam PS-5 + H2O
beta-Lactam NS5 + H2O
-
-
-
?
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-Ala + H2O
acetate + D-Ala
-
-
-
-
?
N-Acetyl-D-Ala + H2O
acetate + D-Ala
-
-
-
-
?
N-Acetyl-D-Ala + H2O
acetate + D-Ala
-
-
-
-
?
N-Acetyl-D-Ala + H2O
acetate + D-Ala
-
-
-
-
?
N-Acetyl-D-Ala + H2O
acetate + D-Ala
-
-
-
-
?
N-Acetyl-D-Ala + H2O
acetate + D-Ala
-
-
-
-
?
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
-
low activity
-
-
r
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-Asn + H2O
acetate + D-Asn
-
-
-
-
?
N-Acetyl-D-Asn + H2O
acetate + D-Asn
-
-
-
-
?
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-Leu + H2O
acetate + D-Leu
-
-
-
-
?
N-acetyl-D-Leu + H2O
acetate + D-Leu
-
-
-
?
N-acetyl-D-Leu + H2O
acetate + D-Leu
-
-
-
-
?
N-acetyl-D-Leu + H2O
acetate + D-Leu
-
-
-
-
?
N-acetyl-D-Leu + H2O
acetate + D-Leu
-
-
-
-
?
N-acetyl-D-Leu + H2O
acetate + D-Leu
-
-
-
-
?
N-acetyl-D-Leu + H2O
acetate + D-Leu
-
-
-
-
?
N-acetyl-D-Leu + H2O
acetate + D-Leu
-
-
-
-
?
N-acetyl-D-Leu + H2O
acetate + D-Leu
-
-
-
-
?
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
-
-
-
-
?
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
-
low activity
-
-
r
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-leucine + H2O
acetate + D-leucine
-
-
-
-
?
N-acetyl-D-leucine + H2O
acetate + D-leucine
-
-
-
-
?
N-Acetyl-D-Met + H2O
acetate + D-Met
-
-
-
-
?
N-Acetyl-D-Met + H2O
acetate + D-Met
-
-
-
-
?
N-Acetyl-D-Met + H2O
acetate + D-Met
-
preferred substrate
-
-
?
N-Acetyl-D-Met + H2O
acetate + D-Met
-
preferred substrate
-
-
?
N-Acetyl-D-Met + H2O
acetate + D-Met
-
-
-
-
?
N-Acetyl-D-Met + H2O
acetate + D-Met
-
-
-
?
N-Acetyl-D-Met + H2O
acetate + D-Met
-
r
-
-
?
N-Acetyl-D-Met + H2O
acetate + D-Met
-
-
-
-
?
N-Acetyl-D-Met + H2O
acetate + D-Met
-
r
-
-
?
N-Acetyl-D-Met + H2O
acetate + D-Met
-
-
-
-
?
N-Acetyl-D-Met + H2O
acetate + D-Met
-
-
-
?
N-Acetyl-D-Met + H2O
acetate + D-Met
-
-
-
-
?
N-Acetyl-D-Met + H2O
acetate + D-Met
-
-
-
-
?
N-Acetyl-D-Met + H2O
acetate + D-Met
-
-
-
-
?
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
-
-
-
-
?
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-methionine + H2O
acetate + D-methionine
-
-
-
?
N-acetyl-D-methionine + H2O
acetate + D-methionine
-
-
-
?
N-acetyl-D-methionine + H2O
acetate + D-methionine
-
-
-
-
?
N-acetyl-D-methionine + H2O
acetate + D-methionine
-
-
-
-
?
N-acetyl-D-methionine + H2O
acetate + D-methionine
-
-
-
?
N-acetyl-D-methionine + H2O
acetate + D-methionine
-
-
-
?
N-Acetyl-D-Phe + H2O
acetate + D-Phe
-
-
-
-
?
N-Acetyl-D-Phe + H2O
acetate + D-Phe
-
-
-
-
?
N-Acetyl-D-Phe + H2O
acetate + D-Phe
-
-
-
-
?
N-Acetyl-D-Phe + H2O
acetate + D-Phe
-
-
-
-
?
N-Acetyl-D-Phe + H2O
acetate + D-Phe
-
-
-
-
?
N-Acetyl-D-Phe + H2O
acetate + D-Phe
-
-
-
-
?
N-Acetyl-D-Phe + H2O
acetate + D-Phe
-
-
-
-
?
N-Acetyl-D-Phe + H2O
acetate + D-Phe
-
-
-
-
?
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-phenylalanine + H2O
acetate + D-phenylalanine
-
-
-
?
N-acetyl-D-phenylalanine + H2O
acetate + D-phenylalanine
-
-
-
-
?
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-phenylglycine + H2O
acetate + D-phenylglycine
-
-
-
-
?
N-Acetyl-D-phenylglycine + H2O
acetate + D-phenylglycine
-
-
-
-
?
N-Acetyl-D-Trp + H2O
acetate + D-Trp
-
-
-
-
?
N-Acetyl-D-Trp + H2O
acetate + D-Trp
-
poor substrate
-
-
?
N-Acetyl-D-Trp + H2O
acetate + D-Trp
-
poor substrate
-
-
?
N-Acetyl-D-Trp + H2O
acetate + D-Trp
-
-
-
-
?
N-Acetyl-D-Trp + H2O
acetate + D-Trp
-
-
-
-
?
N-Acetyl-D-Trp + H2O
acetate + D-Trp
-
-
-
-
?
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-Val + H2O
acetate + D-Val
-
-
-
-
?
N-acetyl-D-Val + H2O
acetate + D-Val
-
-
-
-
?
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
-
low activity
-
-
r
N-acetyl-D-valine + H2O
acetate + D-valine
Rhodococcus armeniensis
-
activity is 9,3% compared to the activity with N-acetyl-D-methionine
-
-
?
N-acetyl-D-valine + H2O
acetate + D-valine
-
-
-
-
?
N-acetyl-D-valine + H2O
acetate + D-valine
-
-
-
-
?
N-Acetyl-Gly + H2O
acetate + Gly
-
fair reactivity
-
-
?
N-Acetyl-Gly + H2O
acetate + Gly
-
-
-
-
?
N-acyl-D-amino acid + H2O
a carboxylate + D-amino acid
-
-
-
?
N-acyl-D-amino acid + H2O
a carboxylate + D-amino acid
-
-
-
?
N-Benzoyl-D-Leu + H2O
Benzoate + D-Leu
-
-
-
-
?
N-Benzoyl-D-Leu + H2O
Benzoate + D-Leu
-
-
-
-
?
N-Benzoyl-D-Met + H2O
Benzoate + D-Met
-
-
-
-
?
N-Benzoyl-D-Met + H2O
Benzoate + D-Met
-
-
-
-
?
N-Benzoyl-D-Phe + H2O
Benzoate + D-Phe
-
-
-
-
?
N-Benzoyl-D-Phe + H2O
Benzoate + D-Phe
-
-
-
-
?
N-Benzoyl-D-Phe + H2O
Benzoate + D-Phe
-
-
-
-
?
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
-
-
?
N-Chloroacetyl-D-Val + H2O
Chloroacetate + D-Val
-
-
-
-
?
N-Chloroacetyl-D-Val + H2O
Chloroacetate + D-Val
-
-
-
-
?
N-Chloroacetyl-D-Val + H2O
Chloroacetate + D-Val
-
-
-
-
?
N-Chloroacetyl-D-Val + H2O
Chloroacetate + D-Val
-
-
-
-
?
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
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-
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additional information
?
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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
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additional information
?
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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
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0.01
Rhodococcus armeniensis
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substrate: N-acetyl-L-valine, pH 7.8, 30°C
0.22
Rhodococcus armeniensis
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substrate: N-acetyl-L-methionine, pH 7.8, 30°C
1.1
Rhodococcus armeniensis
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substrate: N-acetyl-DL-arginine, pH 7.8, 30°C
1.32
Rhodococcus armeniensis
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substrate: N-acetyl-DL-tryptophane, pH 7.8, 30°C
1.55
Rhodococcus armeniensis
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substrate: N-acetyl-D-leucine, pH 7.8, 30°C
11.9
Rhodococcus armeniensis
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substrate: N-acetyl-DL-allylglycine, pH 7.8, 30°C
16.12
Rhodococcus armeniensis
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substrate: N-acetyl-DL-oxyvaline, pH 7.8, 30°C
2.1
Rhodococcus armeniensis
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substrate: N-acetyl-DL-valine, pH 7.8, 30°C
2.76
Rhodococcus armeniensis
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substrate: N-acetyl-D-valine, pH 7.8, 30°C
204
purified recombinant enzyme, pH 7.8, 37°C
22.41
Rhodococcus armeniensis
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substrate: N-acetyl-DL-methionine, pH 7.8, 30°C
22.63
Rhodococcus armeniensis
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substrate: N-acetyl-D-methionine, pH 7.8, 30°C
51.27
purified recombinant mutant M56L, substrate N-acetyl-D-methionine, pH and temperature not specified in the publication
52.83
purified recombinant mutant M254L, substrate N-acetyl-D-methionine, pH and temperature not specified in the publication
54.42
purified recombinant mutant M352L, substrate N-acetyl-D-methionine, pH and temperature not specified in the publication
6.51
Rhodococcus armeniensis
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substrate: N-acetyl-D-phenylalanine, pH 7.8, 30°C
6.95
Rhodococcus armeniensis
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substrate: N-acetyl-D-alanine, pH 7.8, 30°C
7.34
substrate N-acetyl-D-phenylalanine, pH and temperature not specified in the publication, in presence of Co2+
7.95
Rhodococcus armeniensis
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substrate: N-acetyl-DL-tyrosine, pH 7.8, 30°C
71.06
purified recombinant mutant M39L, substrate N-acetyl-D-methionine, pH and temperature not specified in the publication
76.58
purified recombinant wild-type enzyme, substrate N-acetyl-D-methionine, pH and temperature not specified in the publication
85.78
purified recombinant mutant M221L, substrate N-acetyl-D-methionine, pH and temperature not specified in the publication
9.31
substrate N-acetyl-D-methionine , pH and temperature not specified in the publication, in presence of Co2+
additional information
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-
additional information
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additional information
0.05-6.32 U/mg, substrate N-acetyl-D-phenylalanine, different lines, pH and temperature not specified in the publication, in absence of Co2+
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H250N
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KM-value for N-acetyl-D-leucine is 6fold higher than the wild-type value, turnover number is 0.0246% of the wild-type value. Below 1% of the relative activity compared with wild-type enzyme.The zinc content of the mutant enzyme is 0.7 gatom per mol, compared to 2.3 gatom per mol for the wild-type enzyme
H251N
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approximately 30% of the activity of wild-type enzyme. KM-value for N-acetyl-D-leucine is 32% of the wild-type value, turnover number is 48% of the wild-type value.
H67I
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no detectable activity
H67N
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KM-value for N-acetyl-D-leucine is 75% of the wild-type value, turnover number is 0.0012% of the wild-type value. The zinc content of the mutant enzyme is 2.2 gatom per mol, compared to 2.3 gatom per mol for the wild-type enzyme
L298F
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the mutant shows rather lower activities toward all substrates tested including N-acetyl-D-Met compared with the wild type enzyme
M346F
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the mutant shows rather lower activities toward all substrates tested including N-acetyl-D-Met compared with the wild type enzyme
R152K
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site-directed mutagenesis, the mutation of isozymes D-AGase and D-AAase leads to increased partitioning of the recombinant protein in Escherichia coli inclusion bodies
R26K
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site-directed mutagenesis, the mutation of isozymes D-AGase and D-AAase leads to increased partitioning of the recombinant protein in Escherichia coli inclusion bodies
R296K
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site-directed mutagenesis, the mutation of isozymes D-AGase and D-AAase leads to increased partitioning of the recombinant protein in Escherichia coli inclusion bodies
R302K
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site-directed mutagenesis, the mutation of isozymes D-AGase and D-AAase leads to increased partitioning of the recombinant protein in Escherichia coli inclusion bodies
R354K
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site-directed mutagenesis, the mutation of isozymes D-AGase and D-AAase does not increase partitioning of the recombinant protein in Escherichia coli inclusion bodies
R377K
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site-directed mutagenesis, the mutation of isozymes D-AGase and D-AAase does not increase partitioning of the recombinant protein in Escherichia coli inclusion bodies
R392K
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site-directed mutagenesis, the mutation of isozymes D-AGase and D-AAase does not increase partitioning of the recombinant protein in Escherichia coli inclusion bodies
V297F
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the mutant shows partially lower activities toward all substrates tested compared with the wild type enzyme
L298F
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the mutant shows rather lower activities toward all substrates tested including N-acetyl-D-Met compared with the wild type enzyme
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M346F
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the mutant shows rather lower activities toward all substrates tested including N-acetyl-D-Met compared with the wild type enzyme
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R152K
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site-directed mutagenesis, the mutation of isozymes D-AGase and D-AAase leads to increased partitioning of the recombinant protein in Escherichia coli inclusion bodies
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R26K
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site-directed mutagenesis, the mutation of isozymes D-AGase and D-AAase leads to increased partitioning of the recombinant protein in Escherichia coli inclusion bodies
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R296K
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site-directed mutagenesis, the mutation of isozymes D-AGase and D-AAase leads to increased partitioning of the recombinant protein in Escherichia coli inclusion bodies
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R302K
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site-directed mutagenesis, the mutation of isozymes D-AGase and D-AAase leads to increased partitioning of the recombinant protein in Escherichia coli inclusion bodies
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R354K
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site-directed mutagenesis, the mutation of isozymes D-AGase and D-AAase does not increase partitioning of the recombinant protein in Escherichia coli inclusion bodies
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V297F
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the mutant shows partially lower activities toward all substrates tested compared with the wild type enzyme
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C96D
inactive mutant enzymes
D366A
inactive mutant enzymes
H220A
inactive mutant enzymes
C96D
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inactive mutant enzymes
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D366A
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inactive mutant enzymes
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H220A
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inactive mutant enzymes
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M221L
site-directed mutagenesis, the mutant shows 10% enhanced activity and a 44% decreased Km, but a 2.4fold increased kcat/Km compared to the wild-type enzyme, the mutant half-life at 4°C increases up to 6fold compared to the wild-type
M254L
site-directed mutagenesis, the mutant shows 30% reduced activity, but increased half-life compared to the wild-type enzyme
M352L
site-directed mutagenesis, the mutant shows 30% reduced activity, but similar half-life compared to the wild-type enzyme
M39L
site-directed mutagenesis, the mutant shows 10% reduced activity, but increased half-life compared to the wild-type enzyme
M56L
site-directed mutagenesis, the mutant shows 30% reduced activity, but similar half-life compared to the wild-type enzyme
M221L
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site-directed mutagenesis, the mutant shows 10% enhanced activity and a 44% decreased Km, but a 2.4fold increased kcat/Km compared to the wild-type enzyme, the mutant half-life at 4°C increases up to 6fold compared to the wild-type
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M254L
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site-directed mutagenesis, the mutant shows 30% reduced activity, but increased half-life compared to the wild-type enzyme
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M352L
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site-directed mutagenesis, the mutant shows 30% reduced activity, but similar half-life compared to the wild-type enzyme
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M39L
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site-directed mutagenesis, the mutant shows 10% reduced activity, but increased half-life compared to the wild-type enzyme
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M56L
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site-directed mutagenesis, the mutant shows 30% reduced activity, but similar half-life compared to the wild-type enzyme
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F191W
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the catalytic efficiency of the mutant toward N-acetyl-D-Trp and N-acetyl-D-Ala is enhanced by 15.6 and 1.5folds, respectively, compared with that of the wild type enzyme. The mutant retains its catalytic efficiency toward N-acetyl-D-Met compared with that of the wild type enzyme
F191W
site-directed mutagenesis, the catalytic efficiency of the mutant toward N-acetyl-D-Trp and N-acetyl-D-Ala is enhanced by 15.6 and 1.5folds, respectively, compared to the wild-type enzyme, with unaltered other properties, e.g. pH and temperature dependence
L298A
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the catalytic efficiency of the mutant toward N-acetyl-D-Trp is enhanced by 4.4folds compared with that of the wild type enzyme. The catalytic efficiency for N-acetyl-D-Met and N-acetyl-D-Ala decrease to between 2.5 and 5% of that of the wild type enzyme, respectively
L298A
site-directed mutagenesis, the catalytic efficiency of the mutant toward N-acetyl-D-Trp is enhanced by 4.4folds compared to the wild-type enzyme, with unaltered other properties, e.g. pH and temperature dependence
F191W
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the catalytic efficiency of the mutant toward N-acetyl-D-Trp and N-acetyl-D-Ala is enhanced by 15.6 and 1.5folds, respectively, compared with that of the wild type enzyme. The mutant retains its catalytic efficiency toward N-acetyl-D-Met compared with that of the wild type enzyme
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F191W
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site-directed mutagenesis, the catalytic efficiency of the mutant toward N-acetyl-D-Trp and N-acetyl-D-Ala is enhanced by 15.6 and 1.5folds, respectively, compared to the wild-type enzyme, with unaltered other properties, e.g. pH and temperature dependence
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L298A
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the catalytic efficiency of the mutant toward N-acetyl-D-Trp is enhanced by 4.4folds compared with that of the wild type enzyme. The catalytic efficiency for N-acetyl-D-Met and N-acetyl-D-Ala decrease to between 2.5 and 5% of that of the wild type enzyme, respectively
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L298A
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site-directed mutagenesis, the catalytic efficiency of the mutant toward N-acetyl-D-Trp is enhanced by 4.4folds compared to the wild-type enzyme, with unaltered other properties, e.g. pH and temperature dependence
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additional information
construction of mutant AxD-NAases with substrate specificities different from those of wild-type enzyme. The substrate recognition site of the AxD-NAase is rationally manipulated based on computational structural analysis and comparison of its primary structure with other D-aminoacylases with distinct substrate specificities. Mutations of amino acid residues, Phe191, Leu298, Tyr344, and Met346, which interact with the side chain of the substrate, induce marked changes in activities toward each substrate
additional information
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construction of mutant AxD-NAases with substrate specificities different from those of wild-type enzyme. The substrate recognition site of the AxD-NAase is rationally manipulated based on computational structural analysis and comparison of its primary structure with other D-aminoacylases with distinct substrate specificities. Mutations of amino acid residues, Phe191, Leu298, Tyr344, and Met346, which interact with the side chain of the substrate, induce marked changes in activities toward each substrate
additional information
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construction of mutant AxD-NAases with substrate specificities different from those of wild-type enzyme. The substrate recognition site of the AxD-NAase is rationally manipulated based on computational structural analysis and comparison of its primary structure with other D-aminoacylases with distinct substrate specificities. Mutations of amino acid residues, Phe191, Leu298, Tyr344, and Met346, which interact with the side chain of the substrate, induce marked changes in activities toward each substrate
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additional information
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optimization of the enzyme for use on large-scale industrial applications
additional information
Rhodococcus armeniensis
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immobilization of D-aminoacylase of the strain Rhodococcus armeniensis AM6.1 is carried out on the silochrome C-80 with a yield of enzymatic activity of 20%. Aminated silochrome is activated with glutaraldehyde, free aldehyde groups are blocked. The temperature and pH optima, thermal stability, and dependence of thermal stability on pH for free and immobilized enzymes are determined, overview
additional information
Rhodococcus armeniensis AM6.1
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immobilization of D-aminoacylase of the strain Rhodococcus armeniensis AM6.1 is carried out on the silochrome C-80 with a yield of enzymatic activity of 20%. Aminated silochrome is activated with glutaraldehyde, free aldehyde groups are blocked. The temperature and pH optima, thermal stability, and dependence of thermal stability on pH for free and immobilized enzymes are determined, overview
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Wakayama, M.; Katsuno, Y.; Hayashi, S.; Miyamoto, Y.; Sakai, K.; Moriguchi, M.
Cloning and sequencing of a gene encoding D-aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6 and expression of the gene in Escherichia coli
Biosci. Biotechnol. Biochem.
59
2115-2119
1995
Achromobacter xylosoxidans
brenda
Wakayama, M.; Hayashi, S.; Yatsuda, Y.; Katsuno, Y.; Sakai, K.; Moriguchi, M.
Overproduction of D-aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6 in Escherichia coli and its purification
Protein Expr. Purif.
7
395-399
1996
Achromobacter xylosoxidans
brenda
Sugie, M.; Suzuki, H.
Purification and properties of D-aminoacylase of Streptomyces olivaceus
Agric. Biol. Chem.
42
107-133
1978
Streptomyces olivaceus
-
brenda
Yang, Y.B.; Lin, C.S.; Tseng, C.P.; Wang, Y.J.; Tsai, Y.C.
Purification and characterization of D-aminoacylase from Alcaligenes faecalis DA1
Appl. Environ. Microbiol.
57
1259-1260
1991
Alcaligenes faecalis, Alcaligenes faecalis DA1
brenda
Tsai, Y.C.; Tseng, C.P.; Hsiao, K.M.; Chen, L.Y.
Production and purification of D-aminoacylase from Alcaligenes denitrificans and taxonomic study of the strain
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54
984-989
1988
Achromobacter denitrificans
brenda
Chen, H.P.; Wu, S.H.; Wang, K.T.
D-Aminoacylase from Alcaligenes faecalis possesses novel activities on D-methionine
Bioorg. Med. Chem.
2
1-5
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Alcaligenes faecalis, Alcaligenes faecalis DA1
brenda
Tsai, Y.C.; Lin, C.S.; Tseng, T.H.; Lee, H.; Wang, Y.J.
Production and immobilization of D-aminoacylase of Alcaligenes faecalis DA1 for optimal resolution of N-acyl-DL-amino acids
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14
384-389
1992
Alcaligenes faecalis, Alcaligenes faecalis DA1
brenda
Kubo, K.; Ishikura, T.; Fukagawa, Y.
Deacetylation of PS-5, a new beta-lactam compound. II. Separation and purification of L- and D-amino acid acylases from Pseudomonas sp. 1158
J. Antibiot.
33
550-555
1980
Pseudomonas sp., Pseudomonas sp. 1158
brenda
Kameda, Y.; Hase, T.; Kanatomo, S.; Kita, Y.
Studies on acylase activity and micro-organisms. XXVL. Purification and properties of D-acylase (N-acyl-D-amino-acid amidohydrolase) from AAA 6029 (Pseudomonas sp.)
Chem. Pharm. Bull.
26
2698-2704
1978
Pseudomonas sp., Pseudomonas sp. AAA 6029
brenda
Moriguchi, M.; Sakai, K.; Miyamoto, Y.; Wakayama, M.
Production, purification, and characterization of D-aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6
Biosci. Biotechnol. Biochem.
57
1149-1152
1993
Achromobacter xylosoxidans
brenda
Yang, Y.B.; Hsiao, K.M.; Li, H.; Yano, H.; Tsugita, A.; Tsai, Y.C.
Characterization of D-aminoacylase from Alcaligenes denitrificans DA181
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56
1392-1395
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Achromobacter denitrificans
brenda
Kubo, K.; Ishikura, T.; Fukagawa, Y.
Deacetylation of PS-5, a new beta-lactam compound. III. Enzymological characterization of L-amino acid acylase and D-amino acid acylase from Pseudomonas sp. 1158
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33
556-565
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Pseudomonas sp., Pseudomonas sp. 1158
brenda
Wakayama, M.; Yada, H.; Kanda, S.; Hayashi, S.; Yatsuda, Y.; Sakai, K.; Moriguchi, M.
Role of conserved histidine residues in D-aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6
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64
1-8
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Achromobacter xylosoxidans
brenda
Liaw, S.H.; Chen, S.J.; Ko, T.P.; Hsu, C.S.; Chen, C.J.; Wang, A.H.; Tsai, Y.C.
Crystal structure of D-aminoacylase from Alcaligenes faecalis DA1. A novel subset of amidohydrolases and insights into the enzyme mechanism
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278
4957-4962
2003
Alcaligenes faecalis (Q9AGH8), Alcaligenes faecalis, Alcaligenes faecalis DA1 (Q9AGH8), Alcaligenes faecalis DA1
brenda
Lai, W.L.; Chou, L.Y.; Ting, C.Y.; Kirby, R.; Tsai, Y.C.; Wang, A.H.; Liaw, S.H.
The functional role of the binuclear metal center in D-aminoacylase: one-metal activation and second-metal attenuation
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279
13962-13967
2004
Alcaligenes faecalis (Q9AGH8), Alcaligenes faecalis DA1 (Q9AGH8), Alcaligenes faecalis DA1
brenda
Liu, J.; Nakayama, T.; Hemmi, H.; Asano, Y.; Tsuruoka, N.; Shimomura, K.; Nishijima, M.; Nishino, T.
Microbacterium natoriense sp. nov., a novel D-aminoacylase-producing bacterium isolated from soil in Natori, Japan
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55
661-665
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Microbacterium natoriense
brenda
Yoshimune, K.; Ninomiya, Y.; Wakayama, M.; Moriguchi, M.
Molecular chaperones facilitate the soluble expression of N-acyl-D-amino acid amidohydrolases in Escherichia coli
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31
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Achromobacter xylosoxidans, Achromobacter xylosoxidans A-6
brenda
Kumagai, S.; Kobayashi, M.; Yamaguchi, S.; Kanaya, T.; Motohashi, R.; Isobe, K.
A new D-aminoacylase from Defluvibacter sp. A 131-3
J. Mol. Catal. B
30
159-165
2004
Defluvibacter sp., Defluvibacter sp. A 131-3
-
brenda
Wakayama, M.; Kitahata, S.; Manoch, L.; Tachiki, T.; Yoshimune, K.; Moriguchi, M.
Production, purification and properties of D-aminoacylase from a newly isolated Trichoderma sp. SKW-36
Process Biochem.
39
1119-1124
2004
Trichoderma sp., Trichoderma sp. SKW-36
-
brenda
Yoshimune, K.; Kanda, M.; Wakayama, M.; Kanda, S.; Sato, A.; Sakai, K.; Moriguchi, M.
Role of arginine residues of D-aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6
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12
289-294
2005
Achromobacter xylosoxidans, Achromobacter xylosoxidans A-6
brenda
Wu, W.; Xu, J.; Wu, Q.; Lu, D.; Lin, X.
Promiscuous acylase-catalyzed Markovnikov addition of N-heterocycles to vinyl esters in organic media
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348
487-492
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Escherichia coli
-
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Xu, J.; Zhang, F.; Liu, B.; Wu, Q.; Lin, X.
Promiscuous zinc-dependent acylase-mediated carbon-carbon bond formation in organic media
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20
2078-2080
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Escherichia coli
-
brenda
Yano, S.; Haruta, H.; Ikeda, T.; Kikuchi, T.; Murakami, M.; Moriguchi, M.; Wakayama, M.
Engineering the substrate specificity of Alcaligenes D-aminoacylase useful for the production of D-amino acids by optical resolution
J. Chromatogr. B
879
3247-3252
2011
Achromobacter xylosoxidans, Achromobacter xylosoxidans A-6
brenda
Liu, J.; Asano, Y.; Ikoma, K.; Yamashita, S.; Hirose, Y.; Shimoyama, T.; Takahashi, S.; Nakayama, T.; Nishino, T.
Purification, characterization, and primary structure of a novel N-acyl-D-amino acid amidohydrolase from Microbacterium natoriense TNJL143-2
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114
391-397
2012
Microbacterium natoriense (I7HFV7), Microbacterium natoriense TNJL143-2 (I7HFV7), Microbacterium natoriense TNJL143-2
brenda
Wang, W.; Xi, H.; Bi, Q.; Hu, Y.; Zhang, Y.; Ni, M.
Cloning, expression and characterization of D-aminoacylase from Achromobacter xylosoxidans subsp. denitrificans ATCC 15173
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168
360-366
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Achromobacter denitrificans (S4T8N6), Achromobacter denitrificans, Achromobacter denitrificans ATCC 15173 (S4T8N6)
brenda
Peng, I.; Lo, K.; Hsu, C.; Lee, C.
Increasing the storage and oxidation stabilities of N-acyl-D-amino acid amidohydrolase by site-directed mutagenesis of critical methionine residues
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47
1785-1790
2012
Variovorax paradoxus (Q6EMR8), Variovorax paradoxus Iso1 (Q6EMR8)
-
brenda
Arima, J.; Isoda, Y.; Hatanaka, T.; Mori, N.
Recombinant production and characterization of an N-acyl-D-amino acid amidohydrolase from Streptomyces sp. 64E6
World J. Microbiol. Biotechnol.
29
899-906
2013
Streptomyces sp. (S0AUN2), Streptomyces sp. 64E6 (S0AUN2)
brenda
Hambardzumyan, A.; Mkhitaryan, A.; Paloyan, A.; Dadayan, S.; Saghyan, A.
Catalytic properties of aminoacylase of strain Rhodococcus armeniensis AM6.1
Appl. Biochem. Microbiol.
52
250-255
2016
Rhodococcus armeniensis, Rhodococcus armeniensis AM6.1
-
brenda
Hambardzumyan, A.; Mkhitaryan, A.; Paloyan, A.; Dadayan, S.
Covalent immobilization of D-aminoacylase of strain Rhodococcus armeniensis AM6.1 and the characteristics of the biocatalyst
Appl. Biochem. Microbiol.
53
20-24
2017
Rhodococcus armeniensis, Rhodococcus armeniensis AM6.1
-
brenda
Gao, X.; Ma, Q.; Zhu, H.
Distribution, industrial applications, and enzymatic synthesis of D-amino acids
Appl. Microbiol. Biotechnol.
99
3341-3349
2015
Alcaligenes sp.
brenda
Yano, S.; Haruta, H.; Ikeda, T.; Kikuchi, T.; Murakami, M.; Moriguchi, M.; Wakayama, M.
Engineering the substrate specificity of Alcaligenes D-aminoacylase useful for the production of D-amino acids by optical resolution
J. Chromatogr. B
879
3247-3252
2011
Achromobacter xylosoxidans (P72349), Achromobacter xylosoxidans, Achromobacter xylosoxidans A-6 (P72349)
brenda