Information on EC 3.5.1.81 - N-Acyl-D-amino-acid deacylase

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

EC NUMBER
COMMENTARY hide
3.5.1.81
-
RECOMMENDED NAME
GeneOntology No.
N-Acyl-D-amino-acid deacylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N-acyl-D-amino acid + H2O = a carboxylate + D-amino acid
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
N-Acyl-D-amino acid amidohydrolase
The enzyme from Alcaligenes denitrificans subsp. xylosoxydans and Alcaligenes xylosoxydans subsp. xylosoxydans has wide specificity; hydrolyses N-acyl derivative of neutral D-amino acids. Used in separating D- and L-amino acids. Requires zinc.
CAS REGISTRY NUMBER
COMMENTARY hide
65979-42-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Defluvibacter sp.
strain A 131-3
-
-
Manually annotated by BRENDA team
strain A 131-3
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-
Manually annotated by BRENDA team
strain 1158
-
-
Manually annotated by BRENDA team
strain AAA 6029
-
-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
strain SKW-36, isolated from soil, constitutive enzyme
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-
Manually annotated by BRENDA team
strain SKW-36, isolated from soil, constitutive enzyme
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Acetate + D-ethionine
N-Acetyl-D-ethionine + H2O
show the reaction diagram
-
-
-
-
-
beta-Lactam PS-5 + H2O
beta-Lactam NS5 + H2O
show the reaction diagram
Formate + D-Met
N-Formyl-D-Met + H2O
show the reaction diagram
-
-
-
-
-
N-Acetyl-D-Ala + H2O
acetate + D-Ala
show the reaction diagram
N-acetyl-D-alanine + H2O
acetate + D-alanine
show the reaction diagram
16% of the activity with N-acetyl-D-methionine
-
-
?
N-Acetyl-D-Asn + H2O
acetate + D-Asn
show the reaction diagram
N-acetyl-D-aspartate + H2O
acetate + D-aspartate
show the reaction diagram
N-acetyl-D-glutamate + H2O
acetate + D-glutamate
show the reaction diagram
N-acetyl-D-Leu + H2O
acetate + D-Leu
show the reaction diagram
N-acetyl-D-leucine + H2O
acetate + D-leucine
show the reaction diagram
N-Acetyl-D-Met + H2O
acetate + D-Met
show the reaction diagram
N-Acetyl-D-Met-Gly + H2O
acetate + D-Met-Gly
show the reaction diagram
-
fair reactivity
-
-
-
N-Acetyl-D-Met-OMe + H2O
acetate + D-Met-OMe
show the reaction diagram
-
fair reactivity
-
-
-
N-acetyl-D-methionine + H2O
acetate + D-methionine
show the reaction diagram
N-Acetyl-D-norleucine + H2O
acetate + D-norleucine
show the reaction diagram
-
-
-
-
-
N-Acetyl-D-Phe + H2O
acetate + D-Phe
show the reaction diagram
N-acetyl-D-phenylalanine + H2O
acetate + D-phenylalanine
show the reaction diagram
N-Acetyl-D-phenylglycine + H2O
acetate + D-phenylglycine
show the reaction diagram
N-Acetyl-D-Trp + H2O
acetate + D-Trp
show the reaction diagram
N-acetyl-D-tryptophan + H2O
acetate + D-tryptophan
show the reaction diagram
N-Acetyl-D-Tyr + H2O
acetate + D-Tyr
show the reaction diagram
-
-
-
-
-
N-acetyl-D-tyrosine + H2O
acetate + D-tyrosine
show the reaction diagram
5.0% of the activity with N-acetyl-D-methionine
-
-
?
N-acetyl-D-Val + H2O
acetate + D-Val
show the reaction diagram
N-acetyl-D-valine + H2O
acetate + D-valine
show the reaction diagram
N-Acetyl-Gly + H2O
acetate + Gly
show the reaction diagram
N-acyl-D-amino acid + H2O
a carboxylate + D-amino acid
show the reaction diagram
N-Benzoyl-Ala + H2O
Benzoate + Ala
show the reaction diagram
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-
-
-
-
N-Benzoyl-D-Leu + H2O
Benzoate + D-Leu
show the reaction diagram
N-Benzoyl-D-Met + H2O
Benzoate + D-Met
show the reaction diagram
N-Benzoyl-D-Phe + H2O
Benzoate + D-Phe
show the reaction diagram
N-Benzoyl-Val + H2O
Benzoate + Val
show the reaction diagram
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-
-
-
-
N-Benzyloxycarbonyl-D-Leu + H2O
Benzyloxycarbonate + D-Leu
show the reaction diagram
-
fair reactivity
-
-
-
N-Benzyloxycarbonyl-D-Met + H2O
Benzyloxycarbonate + D-Met
show the reaction diagram
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fair reactivity
-
-
-
N-Butyl-D-Leu + H2O
Butanoate + D-Leu
show the reaction diagram
-
-
-
-
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N-chloroacetyl-D-phenylalanine + H2O
chloroacetate + D-phenylalanine
show the reaction diagram
N-Chloroacetyl-D-Val + H2O
Chloroacetate + D-Val
show the reaction diagram
N-Formyl-D-Leu + H2O
Formate + D-Leu
show the reaction diagram
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-
-
-
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N-Formyl-D-Phe + H2O
Formate + D-Phe
show the reaction diagram
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-
-
-
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N-Phenylacetyl-D-Phe + H2O
Phenylacetate + D-Phe
show the reaction diagram
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-
-
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N-Propionyl-D-Leu + H2O
Propanoate + D-Leu
show the reaction diagram
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-
-
-
-
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N-acetyl-D-methionine + H2O
acetate + D-methionine
show the reaction diagram
N-acetyl-D-phenylalanine + H2O
acetate + D-phenylalanine
show the reaction diagram
N-acyl-D-amino acid + H2O
a carboxylate + D-amino acid
show the reaction diagram
additional information
?
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-
the best inducers are a poor substrate, N-acetyl-gamma-methyl-D-Leu, and an inhibitor, N-acetyl-D-alloisoleucine
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-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide
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16% inhibition at 1 mM, 45% inhibition at 10 mM
2,4,6-trinitrobenzeno-1-sulfonate
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40% inhihition at 1 mM, 86% inhibition at 10 mM
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3-Bromopyruvate
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10 mM, 28% inhibition
4-(2-aminoethyl)benzenesulfonyl fluoride hydrochloride
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17% inhibition at 1 mM, 42% inhibition at 10 mM
5,5'-dithiobis(2-nitrobenzoic acid)
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10 mM, 41% inhibition
CoCl2
Defluvibacter sp.
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-
CuCl2
93% inibition at 1 mM
diethyl dicarbonate
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93% inhibition by 93 mM, complete inhibition by 10 mM
HgCl2
99% inibition at 1 mM
iodoacetate
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10 mM, 37% inhibition
MnCl2
Defluvibacter sp.
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monoiodoacetate
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N-acetimidazole
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88% inhibition at 1 mM, 96% inhibition at 10 mM
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N-Acetyl-D-allosoleucine
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-
N-acetyl-D-phenylalanine
substrate inhibition at high concentrations
NiCl2
Defluvibacter sp.
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-
Phenylglyoxal
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55% inhibition at 1 mM, 98% inhibition at 10 mM
Sn2+
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slightly
ZnCl2
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-Cys
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slight stimulation
additional information
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the enzyme is not inducible by N-acyl-D-amino acids and D-amino acid
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
38.61 - 330
N-Acetyl-D-Ala
0.14 - 9.8
N-Acetyl-D-Leu
0.61 - 11.6
N-acetyl-D-leucine
0.22 - 56.4
N-Acetyl-D-Met
0.0137 - 1.89
N-acetyl-D-methionine
0.27 - 2.95
N-Acetyl-D-Phe
2.5
N-acetyl-D-phenylalanine
pH 7.0, 37°C
1.13
N-Acetyl-D-phenylglycine
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-
2.9 - 6.36
N-Acetyl-D-Trp
0.13
N-Chloroacetyl-D-Val
-
-
additional information
additional information
Michaelis-Menten kinetics
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.97 - 330
N-Acetyl-D-Ala
468
N-Acetyl-D-Leu
Achromobacter denitrificans
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-
0.0147 - 1225
N-acetyl-D-leucine
438 - 1826
N-Acetyl-D-Met
25.2 - 76.08
N-acetyl-D-methionine
877
N-Acetyl-D-Phe
Achromobacter denitrificans
-
-
41
N-acetyl-D-phenylalanine
Microbacterium natoriense
I7HFV7
pH 7.0, 37°C
89.5 - 669
N-Acetyl-D-Trp
382
N-Chloroacetyl-D-Val
Achromobacter denitrificans
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-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02 - 8.56
N-Acetyl-D-Ala
9338
8.21 - 407
N-Acetyl-D-Met
5645
2.06 - 9.58
N-acetyl-D-methionine
10717
14.4 - 225
N-Acetyl-D-Trp
9339
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3 - 10
N-acetyl-D-phenylalanine
Microbacterium natoriense
I7HFV7
pH 7.0, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.34
substrate N-acetyl-D-phenylalanine, pH and temperature not specified in the publication, in presence of Co2+
9.31
substrate N-acetyl-D-methionine , pH and temperature not specified in the publication, in presence of Co2+
42.1
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purified enzyme
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
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
204
purified recombinant enzyme, pH 7.8, 37°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
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N-acetyl-D-Phe, N-formyl-D-Phe
10.5
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N-phenylacetyl-D-Phe
additional information
-
optimal growth at pH 5.0-7.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
6 - 9.5
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pH 6.0: about 35% of maximal activity, pH 9.5: about 45% of maximal activity
6.3 - 9.3
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pH 6.3: about 30% of maximal activity, pH 9.3: about 70% of maximal activity
additional information
-
growth range pH 5.0-9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
Defluvibacter sp.
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-
77
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activity increases up to 77 C
additional information
-
optimal growth at 30°C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 55
activity range, profile overview
25 - 50
activity range, recombinant enzyme, the activity decreased rapidly above 50°C
30 - 60
-
30°C: about 50% of maximal activity, 60°C: about 30% of maximal activity
additional information
-
growth range 10-40°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3
Defluvibacter sp.
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-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51918
-
x * 51918, calculation from nucleotide sequence
100000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of the inactive H220A mutant displays that the endogenous Zn2+ shifts to alpha3 subsite coordinated by His67, His69, Cys96 and Asp366
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structure determined at 1.5 A resolution. The protein comprises a small beta-barrel and a catalytic (betaalpha)8-barrel with a 63-residue insertion. Crystal structure reveals that the enzyme belongs to the alpha/beta barrel amidohydrolase superfamily
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 11
-
stable between pH 5.0 and pH 11.0, soluble enzyme
31915, 31918
5 - 9
-
stable between pH 5 and pH 9, immobilized enzyme
31918
5 - 10
purified enzyme, over 60% activity remaining within this range
734334
5
-
5°C, 20 h, complete loss of activity
31914
5.5
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5°C, 20 h, about 50% loss of activity
31914
5.5 - 9
purifed recombinant enzyme, stable at
735339
6 - 11
-
stable
31922
6
-
5°C, 20 h, stable
31914
6.5 - 8.5
purified recombinant enzyme, 37°C, 30 min, stable at
734635
6.5
-
optimal stability
31923
7 - 8
-
optimal stability between pH 7 and pH 8
31912
7.4
-
50°C, 10 min, 5% loss of activity
31921
7.5
-
5°C, 20 h, about 40% loss of activity
31914
8.1
-
50°C, 10 min, optimal stability at
31921
8.3
-
50°C, 10 min, 17% loss of activity
31921
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 45
purified enzyme, over 60% activity remaining within this range
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
CoCl2 protects from denaturation
-
immobilized enzyme retains 90% of the initial activity after 17 days of continous operation
-
not stabilized in presence of 10% glycerol
-
the recombinant enzyme is unstable during protein purification and storage at 4°C probably due to methionine oxidation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 0.02% NaN3, immobilized enzyme is stable for more than 2 months
-
the recombinant enzyme is unstable during protein purification and storage at 4°C probably due to methionine oxidation
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-Toyopearl column chromatography and butyl-Cellulofine column chromatography
-
native enzyme 77fold to homogeneity by dialysis, several steps of anion exchange chromatography and one step of hydrophobic interaction chromatography, followed by gel filtration
native enzyme to homogeneity
Defluvibacter sp.
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native enzyme to homogeneity by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography, and gel filtration
-
partial
recombinant enzyme
-
recombinant His-tagged enzyme 8.5fold from Escherichia coli strain BL21(DE3) by nickel affinity chhromatography and ultrafiltration to homogeneity
recombinant wild-type and mutant enzymes from Escherichia coli strain JM109 by ammonium sulfate fractionation, anion exchange chromatography, hydrophobic interaction chromatography, and ultrafiltration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning by sequence-based screening, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli and Streptomyces lividans
DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis
expression in Escherichia coli
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expression of wild-type and mutant enzymes in Escherichia coli
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gene ADdan, DNA and amino acid sequence determination and analysis, sequence comparison, recombinant expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3) using pET-28a with a T7 promoter
ovoerproduction in Escherichia coli
-
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain JM109
three isozymes D-ANase, D-AGase, and D-AAase, soluble expression of the enzyme in Escherichia coli facilitated by molecular chaperones, overview
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wild type and mutant enzymes are expressed in Escherichia coli JM109 cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F191W
-
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
H250N
-
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
-
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
-
no detectable activity
H67N
-
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
L298A
-
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
L298F
-
the mutant shows rather lower activities toward all substrates tested including N-acetyl-D-Met compared with the wild type enzyme
M346F
-
the mutant shows rather lower activities toward all substrates tested including N-acetyl-D-Met compared with the wild type enzyme
R152K
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
the mutant shows partially lower activities toward all substrates tested compared with the wild type enzyme
F191W
-
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
-
L298A
-
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
-
L298F
-
the mutant shows rather lower activities toward all substrates tested including N-acetyl-D-Met compared with the wild type enzyme
-
M346F
-
the mutant shows rather lower activities toward all substrates tested including N-acetyl-D-Met compared with the wild type enzyme
-
R152K
-
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
-
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
-
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
-
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
-
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
-
the mutant shows partially lower activities toward all substrates tested compared with the wild type enzyme
-
C96D
-
inactive mutant enzymes
D366A
-
inactive mutant enzymes
H220A
-
inactive mutant enzymes
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
-
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
-
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
60 min preincubation with 1 mM Na2EDTA at 30°C causes irreversible inactivation
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
Show AA Sequence (572 entries)
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