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EC Tree
The taxonomic range for the selected organisms is: Arabidopsis thaliana The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
asparaginase, l-asnase, asrgl1, asparaginase ii, l-asparaginase ii, erwinase, ecaii, l-asparaginase i, ecaiii, diasp,
more
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alpha-asparaginase
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L-asparagine amidohydrolase
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potassium-dependent asparaginase
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potassium-independent asparaginase
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carboxylic acid amide hydrolysis
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L-asparagine amidohydrolase
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L-asparagine + H2O
L-aspartate + NH3
strictly specific for L-Asn, has no activity towards beta-aspartyl dipeptides
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?
L-aspartyl hydroxamate + H2O
L-aspartate + hydroxylamine
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?
beta-Asp-His + H2O
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substrate of ASPGA1 and ASPGB1, ASPGA1 has a 4fold substrate preference for beta-Asp-His over Asn
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?
L-asparagine + H2O
L-aspartate + NH3
additional information
?
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not active with N-acetylglucosaminyl-L-Asn
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?
L-asparagine + H2O
L-aspartate + NH3
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?
L-asparagine + H2O
L-aspartate + NH3
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substrate of ASPGA1 and ASPGB1, but ASPGB1 has a 45fold higher specific activity with Asn as substrate than ASPGA1, ASPGA1 has a 4fold substrate preference for beta-Asp-His over Asn
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?
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L-asparagine + H2O
L-aspartate + NH3
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?
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K+
catalytic activity of At3g16150 is enhanced approximately tenfold in the presence of K+
Na+
monovalent cation preference in order of decreasing efficiency is: K+, Na+, Rb+
Rb+
monovalent cation preference in order of decreasing efficiency is: K+, Na+, Rb+
K+
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potassium-independent asparaginase ASPGA1, and potassium-dependent asparaginase ASPGB1
additional information
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potassium-independent L-asparaginase (AtA), Arabidopsis thaliana potassium-dependent L-asparaginase (AtAK)
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additional information
additional information
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kinetic parameters of wild-type and chimeric ASPGA1 and -B1, overview
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2.38
beta-Asp-His
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pH 8.0, temperature not specified in the publication, wild-type ASPGB1
2.9
beta-Asp-His
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pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184A
3.13
beta-Asp-His
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pH 8.0, temperature not specified in the publication, ASPGA1 mutant T166R
3.28
beta-Asp-His
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pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184Q
3.56
beta-Asp-His
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pH 8.0, temperature not specified in the publication, ASPGB1 mutant S189C
3.9
beta-Asp-His
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pH 8.0, temperature not specified in the publication, ASPGB1 mutant F162W
4.15
beta-Asp-His
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pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184D
4.91
beta-Asp-His
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pH 8.0, temperature not specified in the publication, ASPGB1 mutant S189A
5.56
beta-Asp-His
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pH 8.0, temperature not specified in the publication, ASPGB1 mutant F162L
5.62
beta-Asp-His
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pH 8.0, temperature not specified in the publication, ASPGB1 mutant R165T
6.65
beta-Asp-His
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pH 8.0, temperature not specified in the publication, ASPGB1 mutant S189T
6.79
beta-Asp-His
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pH 8.0, temperature not specified in the publication, ASPGA1 mutant L163F
12.6
beta-Asp-His
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pH 8.0, temperature not specified in the publication, wild-type ASPGA1
3.25
L-asparagine
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pH 8.0, temperature not specified in the publication, ASPGB1 mutant F162L
3.25
L-asparagine
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pH 8.0, temperature not specified in the publication, ASPGB1 mutant S189T
4.11
L-asparagine
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pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184D
4.23
L-asparagine
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pH 8.0, temperature not specified in the publication, ASPGB1 mutant S189A
4.53
L-asparagine
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pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184A
4.72
L-asparagine
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pH 8.0, temperature not specified in the publication, ASPGB1 mutant S189C
5.12
L-asparagine
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pH 8.0, temperature not specified in the publication, ASPGB1 mutant F162W
6.83
L-asparagine
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pH 8.0, temperature not specified in the publication, wild-type ASPGB1
10.5
L-asparagine
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pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184Q
10.7
L-asparagine
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pH 8.0, temperature not specified in the publication, ASPGB1 mutant R165T
12.7
L-asparagine
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pH 8.0, temperature not specified in the publication, ASPGA1 mutant L163F
14.3
L-asparagine
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pH 8.0, temperature not specified in the publication, ASPGA1 mutant T166R
14.7
L-asparagine
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pH 8.0, temperature not specified in the publication, wild-type ASPGA1
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ecotype Columbia
SwissProt
brenda
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activity is highest in sink tissues, especially in flowers and siliques
brenda
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additional information
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a divergent sequence between the two enzymes forms a variable loop at the C-terminal of the alpha subunit, the asparaginase variable loop plays a role in the determination of substrate preference in plants. The variable loop itself spans positions 169-182 of ASPGA1 and 168-194 of ASPGB1, dynamic simulations and comparative protein structure modeling based on the crystal structure of Lupinus luteus LlA, PDB accession number 2GEZ, overview
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ASPGB_ARATH
325
0
34341
Swiss-Prot
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14200
x * 27000 + x * 14200, SDS-PAGE
27000
x * 27000 + x * 14200, SDS-PAGE
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?
x * 27000 + x * 14200, SDS-PAGE
additional information
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a divergent sequence between the two enzymes forms a variable loop at the C-terminal of the alpha subunit, the variable loop itself spans positions 169-182 of ASPGA1 and 168-194 of ASPGB1
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F162L
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site-directed mutagenesis of ASPGB1, mutation of Phe162 immediately preceding the variable loop in K+-dependent ASPGB1 specifically affects catalytic activity with Asn, the mutant shows an 8.4fold decrease in Vmax value with Asn, whereas the Vmax with beta-Asp-His is similar to that of the wild-type enzyme
F162W
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site-directed mutagenesis of ASPGB1, mutation of Phe162 immediately preceding the variable loop in K+-dependent ASPGB1 specifically affects catalytic activity with Asn, the mutant shows a 4fold decrease in Vmax value with Asn, whereas the Vmax with beta-Asp-His is similar to that of the wild-type enzyme
L163F
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site-directed mutagenesis of ASPGA1, introduction of the more bulky residue in the ASPGA1 mutant only affects Km and Vmax values with beta-Asp-His and not those with Asn, with beta-Asp-His, the Vmax value of the L163F mutant is reduced by approximately fivefold and the Km value by twofold, compared to the wild-type enzyme
N184A
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site-directed mutagenesis of ASPGB1, the mutant shows a 3fold decrease in Vmax value with Asn as substrate
N184D
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site-directed mutagenesis of ASPGB1, the mutant shows altered kinetics with substrate compared to the wild-type enzyme
N184Q
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site-directed mutagenesis of ASPGB1, the mutant shows a Vmax value with Asn as substrate that is similar or slightly higher than that of the wild-type ASPGB1
R165T
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site-directed mutagenesis of ASPGB1, the mutant shows altered kinetics with substrate compared to the wild-type enzyme
S189A
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site-directed mutagenesis of ASPGB1, the mutant shows a 3fold decrease in Vmax value with Asn as substrate
S189C
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site-directed mutagenesis of ASPGB1, the mutant shows altered kinetics with substrate compared to the wild-type enzyme
S189T
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site-directed mutagenesis of ASPGB1, the mutant shows a Vmax value with Asn as substrate that is similar or slightly higher than that of the wild-type ASPGB1
T166R
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site-directed mutagenesis of ASPGA1, introduction of the more bulky residue in the ASPGA1 mutant only affects Km and Vmax values with beta-Asp-His and not those with Asn
additional information
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construction of chimeras of the variable loop at the C-terminal of the alpha subunit of ASPGA1 and ASPGB1, substrate specificities and kinetics compared to the wild-type enzyme, overview
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expression in Escherichia coli as N-terminal His-tagged protein
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Michalska, K.; Jaskolski, M.
Structural aspects of L-asparaginases, their friends and relations
Acta Biochim. Pol.
53
627-640
2006
Arabidopsis thaliana, Lupinus luteus, Pyrococcus horikoshii, Escherichia coli (P00805)
brenda
Bruneau, L.; Chapman, R.; Marsolais, F.
Co-occurrence of both L-asparaginase subtypes in Arabidopsis: At3g16150 encodes a K+-dependent L-asparaginase
Planta
224
668-679
2006
Arabidopsis thaliana (Q8GXG1)
brenda
Gabriel, M.; Telmer, P.G.; Marsolais, F.
Role of asparaginase variable loop at the carboxyl terminal of the alpha subunit in the determination of substrate preference in plants
Planta
235
1013-1022
2012
Arabidopsis thaliana
brenda