We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide
Synonyms
ntn-hydrolase, isoaspartyl dipeptidase, hasrgl1, cpsiada, asparaginase-like protein 1, isoaspartyl peptidase/l-asparaginase, beta-aspartyl peptidase, isoaspartyl peptidase, isoaspartyl aminopeptidase/asparaginase,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
asparaginase-like protein 1
-
asparagine beta-amidohydrolase
-
beta-aspartyl dipeptidase
-
-
-
-
beta-aspartyl peptidase
-
-
-
-
dipeptidase, beta-aspartyl
-
-
-
-
EC 3.4.13.10
-
-
formerly
-
isoaspartyl aminopeptidase
-
isoaspartyl aminopeptidase/asparaginase
isoaspartyl peptidase/L-asparaginase
UniProt
potassium-independent asparaginase
-
CpsIadA
-
IAD
-
isoaspartyl aminopeptidase/asparaginase
-
isoaspartyl aminopeptidase/asparaginase
-
-
isoaspartyl dipeptidase
-
isoaspartyl dipeptidase
-
-
isoaspartyl peptidase
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
hydrolysis of peptide bond
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
alpha-Asp-Leu + H2O
Asp + Leu
-
-
-
?
alpha-Asp-Leu + H2O
L-Asp + L-Leu
-
-
-
?
Asp-Gly-Ala + H2O
Asp + Gly-Ala
-
55% of the activity with beta-aspartylglycine
-
?
Asp-Gly-Val + H2O
Asp + Gly-Val
-
13% of the activity with beta-aspartylglycine
-
?
beta-Ala-Ala + H2O
Ala + Ala
-
-
-
?
beta-Asp-Ala + H2O
Asp + Ala
beta-Asp-Gln + H2O
Asp + Gln
-
-
-
?
beta-Asp-Gly + H2O
Asp + Gly
beta-Asp-Gly-Gly + H2O
Asp + Gly-Gly
-
95% of the activity with beta-aspartylglycine
-
?
beta-Asp-His + H2O
Asp + His
beta-Asp-Ile + H2O
Asp + Ile
-
37% of the activity with beta-aspartylglycine
-
?
beta-Asp-Leu + H2O
Asp + Leu
beta-Asp-Lys + H2O
Asp + Lys
beta-Asp-Met + H2O
Asp + Met
-
82% of the activity with beta-aspartylglycine
-
?
beta-Asp-Phe + H2O
Asp + Phe
beta-Asp-Phe + H2O
L-Asp + L-Phe
-
-
-
-
?
beta-Asp-Ser + H2O
Asp + Ser
beta-Asp-Thr + H2O
Asp + Thr
-
29% of the activity with beta-aspartylglycine
-
?
beta-Asp-Val + H2O
Asp + Val
-
28% of the activity with beta-aspartylglycine
-
?
beta-L-Asp-L-Ala + H2O
L-Asp + L-Ala
-
-
-
?
beta-L-Asp-L-Leu + H2O
L-Asp + L-Leu
-
-
-
?
beta-L-Asp-L-Lys + H2O
L-Asp + L-Lys
-
-
-
?
beta-L-Asp-L-Phe + H2O
L-Asp + L-Phe
-
-
-
?
beta-L-Asp-L-Phe methyl ester + H2O
L-Asp + L-Phe methyl ester
-
-
-
?
beta-L-aspartyl-L-leucine + H2O
?
-
-
-
?
iso-Asp-Gly + H2O
?
-
-
-
?
iso-Asp-Leu + H2O
?
best substrate
-
-
?
L-Asp beta-methyl ester + H2O
L-Asp + methanol
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
?
L-aspartic acid beta-(7-amido-4-methylcoumarin) + H2O
L-aspartic acid + 7-amino-4-methylcoumarin
-
-
-
?
additional information
?
-
beta-Asp-Ala + H2O
Asp + Ala
-
-
-
-
?
beta-Asp-Ala + H2O
Asp + Ala
-
-
-
?
beta-Asp-Ala + H2O
Asp + Ala
-
-
-
?
beta-Asp-Ala + H2O
Asp + Ala
-
-
-
?
beta-Asp-Ala + H2O
Asp + Ala
-
51% of the activity with beta-aspartylglycine
-
?
beta-Asp-Gly + H2O
Asp + Gly
-
-
-
-
?
beta-Asp-Gly + H2O
Asp + Gly
-
-
-
?
beta-Asp-Gly + H2O
Asp + Gly
-
-
-
?
beta-Asp-Gly + H2O
Asp + Gly
-
-
-
?
beta-Asp-Gly + H2O
Asp + Gly
-
-
-
?
beta-Asp-His + H2O
Asp + His
-
-
-
?
beta-Asp-His + H2O
Asp + His
-
-
-
?
beta-Asp-His + H2O
Asp + His
-
-
-
?
beta-Asp-Leu + H2O
Asp + Leu
-
-
-
?
beta-Asp-Leu + H2O
Asp + Leu
-
-
-
?
beta-Asp-Leu + H2O
Asp + Leu
-
-
-
-
?
beta-Asp-Leu + H2O
Asp + Leu
-
-
-
?
beta-Asp-Leu + H2O
Asp + Leu
-
59-65% of the activity with beta-aspartylglycine
-
?
beta-Asp-Lys + H2O
Asp + Lys
-
-
-
?
beta-Asp-Lys + H2O
Asp + Lys
-
-
-
?
beta-Asp-Lys + H2O
Asp + Lys
-
-
-
?
beta-Asp-Phe + H2O
Asp + Phe
-
-
-
?
beta-Asp-Phe + H2O
Asp + Phe
-
-
-
?
beta-Asp-Ser + H2O
Asp + Ser
-
-
-
-
?
beta-Asp-Ser + H2O
Asp + Ser
-
47-56% of the activity with beta-aspartylglycine
-
?
additional information
?
-
-
enzyme additionally acts as an asparaginase, EC 3.5.1.1
-
-
?
additional information
?
-
-
little or no activity towards L-isoaspartyl-glycine or L-isoaspartyl-L-histidine, gamma-L-glutamyl-L-leucine, gamma-L-glutamyl-glycine, gamma-L-glutamyl-L-cysteine, gamma-L-glutamyl-L-histidine
-
-
?
additional information
?
-
-
does not appear to be involved in glutathione metabolism
-
-
?
additional information
?
-
energetics of isoaspartyl dipeptidase reaction. Dispersion is included in the modeling of the enzymatic reaction
-
-
?
additional information
?
-
energetics of isoaspartyl dipeptidase reaction. Dispersion is included in the modeling of the enzymatic reaction
-
-
?
additional information
?
-
the enzyme shows both isoaspartyl dipeptidase and L-asparaginase activities. Identification of Thr193 in enzyme LlA as the catalytic nucleophile and classification of the enzyme as Ntn-hydrolase
-
-
?
additional information
?
-
-
the enzyme shows both isoaspartyl dipeptidase and L-asparaginase activities. Identification of Thr193 in enzyme LlA as the catalytic nucleophile and classification of the enzyme as Ntn-hydrolase
-
-
?
additional information
?
-
no activity with L-glutamine, L-asparagine amide, L-aspartic acid amide, glycyl-L-asparagine, and N4-(beta-N-acetylglucosaminyl)-L-asparagine
-
-
?
additional information
?
-
-
no activity with L-glutamine, L-asparagine amide, L-aspartic acid amide, glycyl-L-asparagine, and N4-(beta-N-acetylglucosaminyl)-L-asparagine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-asparagine + H2O
L-aspartate + NH3
-
-
-
?
additional information
?
-
additional information
?
-
-
does not appear to be involved in glutathione metabolism
-
-
?
additional information
?
-
the enzyme shows both isoaspartyl dipeptidase and L-asparaginase activities. Identification of Thr193 in enzyme LlA as the catalytic nucleophile and classification of the enzyme as Ntn-hydrolase
-
-
?
additional information
?
-
-
the enzyme shows both isoaspartyl dipeptidase and L-asparaginase activities. Identification of Thr193 in enzyme LlA as the catalytic nucleophile and classification of the enzyme as Ntn-hydrolase
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Zinc
-
a binuclear zinc center is located in each subunit at the C-terminal end of the (beta,alpha)8-barrel. Ligands to the binuclear metal center include His68, His70, His201, His230, Asp285. The two zincs are bridged by a carboxylated lysine residue Lys162 and a solvent molecule
Zinc
two catalytic zinc ions are surrounded by four His
additional information
the active site consists of a binuclear metal center positioned at the C-terminal end of a (beta/alpha)8-barrel domain
additional information
-
the active site consists of a binuclear metal center positioned at the C-terminal end of a (beta/alpha)8-barrel domain
additional information
the enzyme is potassium-independent
additional information
-
the enzyme is potassium-independent
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
p-hydroxymercuribenzoate
-
-
Zn2+
inhibits autoproteolysis, other divalent cations than Zn2+ have no effect on the process
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-mercaptoethanol
-
slight activation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Endometrial Neoplasms
Asparaginase-like protein 1 expression in curettage independently predicts lymph node metastasis in endometrial carcinoma: a multicentre study.
Endometrial Neoplasms
Asparaginase-like protein 1 is an independent prognostic marker in primary endometrial cancer, and is frequently lost in metastatic lesions.
Lymphatic Metastasis
Asparaginase-like protein 1 expression in curettage independently predicts lymph node metastasis in endometrial carcinoma: a multicentre study.
Neoplasm Metastasis
Asparaginase-like protein 1 expression in curettage independently predicts lymph node metastasis in endometrial carcinoma: a multicentre study.
Neoplasm Metastasis
Structural insights into the function of the catalytically active human Taspase1.
Neoplasms
Increased expression of ASRGL1 in invasive ductal carcinoma and its association with estrogen-progesterone receptor status of tumors.
Neoplasms
Structural insights into the function of the catalytically active human Taspase1.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.93
beta-Ala-Ala
pH 8.0, 30°C
0.8
beta-aspartyl-L-leucine
-
-
0.136
beta-L-aspartyl-L-leucine
pH 7.5, 22°C
5
alpha-Asp-Leu
wild-type enzyme, pH 8.1, 30°C
6.9
alpha-Asp-Leu
pH 8.0, 30°C
1.2
beta-Asp-Ala
pH 8.0, 30°C
3.7
beta-Asp-Ala
wild-type enzyme, pH 8.1, 30°C
4.7
beta-Asp-Gly
pH 8.0, 30°C
18
beta-Asp-Gly
wild-type enzyme, pH 8.1, 30°C
3.7
beta-Asp-His
wild-type enzyme, pH 8.1, 30°C
5.3
beta-Asp-His
pH 8.0, 30°C
0.09
beta-Asp-Leu
Ni/Ni reconstituted enzyme, pH 8.1, 30°C
0.36
beta-Asp-Leu
Cd/Cd reconstituted enzyme, pH 8.1, 30°C
0.5
beta-Asp-Leu
mutant enzyme D285A, pH 8.1, 30°C
0.62
beta-Asp-Leu
Co/Co reconstituted enzyme, pH 8.1, 30°C
0.71
beta-Asp-Leu
pH 8.0, 30°C
0.8
beta-Asp-Leu
mutant enzyme E77Q, pH 8.1, 30°C
0.98
beta-Asp-Leu
mutant enzyme D285N, pH 8.1, 30°C
1.02
beta-Asp-Leu
wild-type enzyme, pH 8.1, 30°C
1.02
beta-Asp-Leu
Zn/Zn reconstituted enzyme, pH 8.1, 30°C
1.4
beta-Asp-Leu
mutant enzyme Y137F, pH 8.1, 30°C
1.7
beta-Asp-Leu
mutant enzyme Y137A, pH 8.1, 30°C
2.7
beta-Asp-Leu
mutant enzyme S289A, pH 8.1, 30°C
6.9
beta-Asp-Leu
mutant enzyme E77D, pH 8.1, 30°C
20
beta-Asp-Leu
mutant enzyme R233K, pH 8.1, 30°C
34
beta-Asp-Leu
mutant enzyme R169K, pH 8.1, 30°C
0.91
beta-Asp-Lys
wild-type enzyme, pH 8.1, 30°C
1.1
beta-Asp-Lys
pH 8.0, 30°C
0.23
beta-Asp-Phe
wild-type enzyme, pH 8.1, 30°C
0.41
beta-Asp-Phe
-
pH 7.5, 37°C
0.49
beta-Asp-Phe
pH 8.0, 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00062 - 164
beta-Asp-Leu
0.813
beta-L-aspartyl-L-leucine
pH 7.5, 22°C
15.7
alpha-Asp-Leu
wild-type enzyme, pH 8.1, 30°C
89
alpha-Asp-Leu
pH 8.0, 30°C
166
beta-Asp-Ala
pH 8.0, 30°C
213
beta-Asp-Ala
wild-type enzyme, pH 8.1, 30°C
0.93
beta-Asp-Gly
wild-type enzyme, pH 8.1, 30°C
181
beta-Asp-Gly
pH 8.0, 30°C
20.8
beta-Asp-His
wild-type enzyme, pH 8.1, 30°C
74
beta-Asp-His
pH 8.0, 30°C
0.00062
beta-Asp-Leu
mutant enzyme D285A, pH 8.1, 30°C
0.0051
beta-Asp-Leu
mutant enzyme E77D, pH 8.1, 30°C
0.0056
beta-Asp-Leu
mutant enzyme E77Q, pH 8.1, 30°C
0.017
beta-Asp-Leu
mutant enzyme D285N, pH 8.1, 30°C
0.18
beta-Asp-Leu
mutant enzyme Y137F, pH 8.1, 30°C
0.19
beta-Asp-Leu
mutant enzyme Y137A, pH 8.1, 30°C
9
beta-Asp-Leu
mutant enzyme R169K, pH 8.1, 30°C
9
beta-Asp-Leu
mutant enzyme S289A, pH 8.1, 30°C
9.2
beta-Asp-Leu
Ni/Ni reconstituted enzyme, pH 8.1, 30°C
11.9
beta-Asp-Leu
Cd/Cd reconstituted enzyme, pH 8.1, 30°C
13
beta-Asp-Leu
mutant enzyme R233K, pH 8.1, 30°C
34
beta-Asp-Leu
Co/Co reconstituted enzyme, pH 8.1, 30°C
104
beta-Asp-Leu
wild-type enzyme, pH 8.1, 30°C
104
beta-Asp-Leu
Zn/Zn reconstituted enzyme, pH 8.1, 30°C
164
beta-Asp-Leu
pH 8.0, 30°C
58
beta-Asp-Lys
wild-type enzyme, pH 8.1, 30°C
256
beta-Asp-Lys
pH 8.0, 30°C
1.98
beta-Asp-Phe
-
pH 7.5, 37°C
16.9
beta-Asp-Phe
wild-type enzyme, pH 8.1, 30°C
145
beta-Asp-Phe
pH 8.0, 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
13
alpha-Asp-Leu
pH 8.0, 30°C
140
beta-Asp-Ala
pH 8.0, 30°C
38
beta-Asp-Gly
pH 8.0, 30°C
14
beta-Asp-His
pH 8.0, 30°C
230.9
beta-Asp-Leu
pH 8.0, 30°C
230
beta-Asp-Lys
pH 8.0, 30°C
5.98
beta-L-aspartyl-L-leucine
pH 7.5, 22°C
4.83
beta-Asp-Phe
-
pH 7.5, 37°C
300
beta-Asp-Phe
pH 8.0, 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7.5 - 8
-
sodium phosphate buffer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7.5 - 9
pH 7.5: about 35% of maximal activity, pH 9.0: about 20% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
22
assay at room temperature
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
30 - 50
30°C: about 60% of maximal activity, 50°C: about 70% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
enzyme from human faeces, present in healthy individuals, absent in antibiotic-treated patients
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
-
Uniprot
brenda
-
UniProt
brenda
yellow lupin with roots infected with Bradyrhizobium sp.
UniProt
brenda
-
-
-
brenda
-
-
-
brenda
-
Uniprot
brenda
-
-
-
brenda
-
Uniprot
brenda
-
SwissProt
brenda
-
Uniprot
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
the enzyme belongs to the N-terminal nucleophile hydrolase family
additional information
the enzyme catalyzes the hydrolysis of an isoaspartyl dipeptide-like moiety, which can be inappropriately formed in proteins, between the beta-carboxyl group side chain of Asp and the amino group of the following amino acid
additional information
-
the enzyme catalyzes the hydrolysis of an isoaspartyl dipeptide-like moiety, which can be inappropriately formed in proteins, between the beta-carboxyl group side chain of Asp and the amino group of the following amino acid
additional information
-
the enzyme catalyzes the hydrolysis of an isoaspartyl dipeptide-like moiety, which can be inappropriately formed in proteins, between the beta-carboxyl group side chain of Asp and the amino group of the following amino acid
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
14550
mass spectroscopy, beta-subunit
15000
-
beta-subunit, SDS-PAGE
18000
Western blot, reducing conditions, detected in soluble and insoluble fractions
18500
mass spectroscopy, alpha-subunit
20000
-
alpha-subunit, SDS-PAGE
33020
mass spectroscopy, precursor enzyme
35000
-
inactive precursor, SDS-PAGE
75000
about, recombinant His-tagged enzyme, gel filtration
33000
SDS-PAGE, intact precursor molecule, 19000 + 14000 (native protein) after autoproteolysis
33000
Western blot, reducing conditions, detected in soluble and insoluble fractions
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
heterodimer
alphabeta, 1 * 23000, alpha-subunit + 1 * 14000, beta-subunit, SDS-PAGE, 1 * 22893, His-tagged alpha-subunit + 1 * 13605, beta-subunit, mass spectrometry
tetramer
the enzyme is dimer of heterodimers (alphabeta)2
additional information
the quarternary structure of the enzyme is octameric and can be described as a tetramer od dimers. Each subunit folds into two distinct domains
octamer
crystallographic data, the enzyme forms an octamer with two Zn2+ ions in the active site
octamer
-
crystallographic data, the enzyme forms an octamer with two Zn2+ ions in the active site
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
proteolytic modification
-
inactive precursor undergoes a self-activation process, converting it from an uncleaved precursor of 35000 Da into alpha- and beta-subunits of 20000 and 15000 Da, respectively. Glycine stimulates cleavage in a dose-dependent manner
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
uncleaved (inactive) as well as the cleaved (active), aspartate-bound structures. Cleavage does not greatly alter the overall structure of the enzyme with the exception of the conformational change in the conserved HGG loop that coincides with cleavage
-
structures of the isoaspartyl dipeptidase from Colwellia psychrerythraea, both ligand-free and that complexed with beta-isoaspartyl lysine, at 1.85 A and 2.33 A resolution, respectively. In both structures, the enzyme forms an octamer with two Zn2+ ions in the active site
hanging drop method of vapor diffusion, the best crystals are observed growing at 25°C from 10% poly(ethylene glycol)8000, 100 mM homopipes, pH 5, in the presence of MgCl2
-
hanging drop vapor diffusion method, 1.9 A resolution
hanging drop vapor diffusion method. X-ray crystal structure of the D285N mutant complexed with beta-Asp-His
hanging-drop vapour-diffusion method, crystal structure of EcAIII at 1.65 A resolution
-
sitting drop vapor diffusion method, crystal structure in the absence and presence of the phosphinic inhibitor Asp-PSI[PO2CH2]-LeuOH
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
E166A
the mutant exhibits a complete loss of activity and a considerable decrease in melting temperature
E166K
the mutant exhibits a complete loss of activity and a considerable decrease in melting temperature
E80Q
the mutant has no catalytic activity toward beta-Asp-Leu, but its CD spectra and denaturation temperature are similar to wild-type, indicating that this mutation affects catalytic activity but not the overall folding and integrity of the enzyme
Y140F
the mutant has a significant reduction rate of catalysis confirming that this tyrosine residue is important for enzymatic catalysis. It shows less than 10% catalytic activity toward beta-Asp-Leu and the CD spectrum is not significantly different to the wild-type enzyme. Unlike the wild-type enzyme and the other mutants Y140F has a tendency to aggregate during purification and storage, but soluble Y140F is the most thermally stable
E166A
-
the mutant exhibits a complete loss of activity and a considerable decrease in melting temperature
-
E166K
-
the mutant exhibits a complete loss of activity and a considerable decrease in melting temperature
-
E80Q
-
the mutant has no catalytic activity toward beta-Asp-Leu, but its CD spectra and denaturation temperature are similar to wild-type, indicating that this mutation affects catalytic activity but not the overall folding and integrity of the enzyme
-
Y140F
-
the mutant has a significant reduction rate of catalysis confirming that this tyrosine residue is important for enzymatic catalysis. It shows less than 10% catalytic activity toward beta-Asp-Leu and the CD spectrum is not significantly different to the wild-type enzyme. Unlike the wild-type enzyme and the other mutants Y140F has a tendency to aggregate during purification and storage, but soluble Y140F is the most thermally stable
-
D285A
kcat/Km for beta-Asp-Leu is 85000fold lower than wild-type value
D285N
kcat/Km for beta-Asp-Leu is 5667fold lower than wild-type value
E77D
kcat/Km for beta-Asp-Leu is 137837fold lower than wild-type value
E77Q
kcat/Km for beta-Asp-Leu is 14571fold lower than wild-type value
R169K
kcat/Km for beta-Asp-Leu is 378fold lower than wild-type value
R169M
kcat/Km for beta-Asp-Leu is 1672131fold lower than wild-type value
R233K
kcat/Km for beta-Asp-Leu is 192fold lower than wild-type value
R233M
kcat/Km for beta-Asp-Leu is 170fold lower than wild-type value
S289A
kcat/Km for beta-Asp-Leu is 30000fold lower than wild-type value
T179A
does not undergo autoprocessing
Y137A
kcat/Km for beta-Asp-Leu is 927fold lower than wild-type value
Y137F
kcat/Km for beta-Asp-Leu is 850fold lower than wild-type value
T168A
mutant does not show enzymatic activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
66
denaturation temperature, mutant enzyme E166K
71
denaturation temperature, mutant enzyme E166A
81
denaturation temperature, wild-type enzyme
85
denaturation temperature, mutant enzyme E80Q
89
denaturation temperature, mutant enzyme Y140F
60
completely inactivated
60
purified recombinant His-tagged enzyme, stable up to
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
stability is dependent on the presence of sodium ions
-
stable to freezing and thawing in 0.01 M sodium phosphate buffer
-
thermostable, probably owing to its octameric structure
unstable to dialysis against water or 0.01 M Tris-HCl buffer, pH 8.0, if 0.01 M NaCl is included in the dialysis solution, 80% of the activity is recovered
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
room temperature, stable for 5 days
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
recombinant His-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography and gel filtration
using Ni-NTA chromatography. hASRGL1 purification by immobilized metal ion affinity chromatography yields 30 mg of protein/l with a purity of more than 90% as determined by SDS-PAGE
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS
expressed as a His-tagged fusion protein in Escherichia coli
expression in Escherichia coli
-
expression in Escherichia coli BL21 (DE3)
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
medicine
-
isoform ASRGL1 is not the asparaginase responsible for the antitumor effects elicited by treatment with guinea pig serum
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Haley, E.E.
beta-Aspartyl peptidase from rat liver
Methods Enzymol.
19
737-741
1970
Rattus norvegicus
-
brenda
van der Leij, F.R.; Welling, G.W.
Determination of beta-aspartylpeptidase activity in human faeces by high-performance liquid chromatography using pre-column derivatization with phenyl isothiocyanate
J. Chromatogr.
383
35-42
1986
Bacteria
brenda
Gary, J.D.; Clarke, S.
Purification and characterization of an isoaspartyl dipeptidase from Escherichia coli
J. Biol. Chem.
270
4076-4087
1995
Escherichia coli
brenda
Jozic, D.; Kaiser, J.T.; Huber, R.; Bode, W.; Maskos, K.
X-ray Structure of isoaspartyl dipeptidase from E. coli: a dinuclear zinc peptidase evolved from amidohydrolases
J. Mol. Biol.
332
243-256
2003
Escherichia coli (P39377)
brenda
Thoden, J.B.; Marti-Arbona, R.; Raushel, F.M.; Holden, H.M.
High-resolution X-ray structure of isoaspartyl dipeptidase from Escherichia coli
Biochemistry
42
4874-4882
2003
Escherichia coli
brenda
Prahl, A.; Pazgier, M.; Hejazi, M.; Lockau, W.; Lubkowski, J.
Structure of the isoaspartyl peptidase with L-asparaginase activity from Escherichia coli
Acta Crystallogr. Sect. D
D60
1173-1176
2004
Escherichia coli
brenda
Marti-Arbona, R.; Fresquet, V.; Thoden, J.B.; Davis, M.L.; Holden, H.M.; Raushel, F.M.
Mechanism of the reaction catalyzed by isoaspartyl dipeptidase from Escherichia coli
Biochemistry
44
7115-7124
2005
Escherichia coli (P39377), Escherichia coli
brenda
Michalska, K.; Brzezinski, K.; Jaskolski, M.
Crystal structure of isoaspartyl aminopeptidase in complex with L-aspartate
J. Biol. Chem.
280
28484-28491
2005
Escherichia coli (P37595), Escherichia coli
brenda
Michalska, K.; Hernandez-Santoyo, A.; Jaskolski, M.
The mechanism of autocatalytic activation of plant-type L-asparaginases
J. Biol. Chem.
283
13388-13397
2008
Escherichia coli (P37595)
brenda
Cantor, J.R.; Stone, E.M.; Chantranupong, L.; Georgiou, G.
The human asparaginase-like protein 1 hASRGL1 is an Ntn hydrolase with beta-aspartyl peptidase activity
Biochemistry
48
11026-11031
2009
Homo sapiens (Q7L266), Homo sapiens
brenda
Schalk, A.M.; Lavie, A.
Structural and kinetic characterization of guinea pig L-asparaginase type III
Biochemistry
53
2318-2328
2014
Cavia porcellus
brenda
Borek, D.; Michalska, K.; Brzezinski, K.; Kisiel, A.; Podkowinski, J.; Bonthron, D.; Krowarsch, D.; Otlewski, J.; Jaskolski, M.
Expression, purification and catalytic activity of Lupinus luteus asparagine beta-amidohydrolase and its Escherichia coli homolog
Eur. J. Biochem.
271
3215-3226
2004
Lupinus luteus (Q9ZSD6), Lupinus luteus
brenda
Zhang, H.M.; Chen, S.L.
Include dispersion in quantum chemical modeling of enzymatic reactions the case of isoaspartyl dipeptidase
J. Chem. Theory Comput.
11
2525-2535
2015
Escherichia coli (P39377), Escherichia coli K12 (P39377)
brenda
Park, S.H.; Lee, C.W.; Lee, S.G.; Shin, S.C.; Kim, H.J.; Park, H.; Lee, J.H.
Crystal structure and functional characterization of an isoaspartyl dipeptidase (CpsIadA) from Colwellia psychrerythraea strain 34H
PLoS ONE
12
e0181705
2017
Colwellia psychrerythraea (Q484B6), Colwellia psychrerythraea, Colwellia psychrerythraea ATCC BAA-681 (Q484B6)
brenda
Select items on the left to see more content.
html completed