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Information on EC 3.5.1.1 - asparaginase and Organism(s) Arabidopsis thaliana and UniProt Accession Q8GXG1
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3.5.1.1 asparaginaseSpecify your search results
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- 3.5.1.1
- leukemia
- lymphoblastic
- children
-
remission
- erwinia
- hypersensitivity
- methotrexate
- lymphoma
- vincristine
-
pegylated
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relapse
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- thrombosis
- prednisone
-
high-dose
- venous
-
oncology
-
event-free
-
schedule
- cytarabine
-
consolidation
-
intensification
-
antileukemic
-
intrathecal
- antithrombin
-
l-aspartic
- chrysanthemi
- anthracyclines
- medicine
-
reinduction
- cyclophosphamide
-
pegaspargase
- thromboembolism
- allergy
- acrylamide
-
arabinoside
- mercaptopurine
- daunorubicin
- osteonecrosis
- analysis
-
philadelphia
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extranodal
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fried
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b-precursor
- succinogenes
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standard-risk
- synthesis
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coli-derived
- food industry
- diagnostics
- biotechnology
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dana-farber
- pharmacology
- teniposide
- carotovora
-
multiagent
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-asparaginase
-
-
-
-
asparaginase II
-
-
-
-
colaspase
-
-
-
-
crasnitin
-
-
-
-
DiAsp
-
-
-
-
elspar
-
-
-
-
L-ASNase
-
-
-
-
L-asparaginase
-
-
-
-
L-asparagine amidohydrolase
-
-
-
-
leunase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylic acid amide hydrolysis
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
L-asparagine amidohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY
9015-68-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-asparagine + H2O
L-aspartate + NH3
strictly specific for L-Asn, has no activity towards beta-aspartyl dipeptides
-
-
?
beta-Asp-His + H2O
?
-
substrate of ASPGA1 and ASPGB1, ASPGA1 has a 4fold substrate preference for beta-Asp-His over Asn
-
-
?
additional information
?
-
not active with N-acetylglucosaminyl-L-Asn
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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+
-
potassium-independent asparaginase ASPGA1, and potassium-dependent asparaginase ASPGB1
additional information
-
potassium-independent L-asparaginase (AtA), Arabidopsis thaliana potassium-dependent L-asparaginase (AtAK)
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic parameters of wild-type and chimeric ASPGA1 and -B1, overview
-
2.38
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, wild-type ASPGB1
2.9
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184A
3.13
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, ASPGA1 mutant T166R
3.28
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184Q
3.56
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant S189C
3.9
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant F162W
4.15
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184D
4.91
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant S189A
5.56
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant F162L
5.62
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant R165T
6.65
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant S189T
6.79
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, ASPGA1 mutant L163F
12.6
beta-Asp-His
-
pH 8.0, temperature not specified in the publication, wild-type ASPGA1
3.25
L-asparagine
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant F162L
3.25
L-asparagine
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant S189T
4.11
L-asparagine
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184D
4.23
L-asparagine
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant S189A
4.53
L-asparagine
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184A
4.72
L-asparagine
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant S189C
5.12
L-asparagine
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant F162W
6.83
L-asparagine
-
pH 8.0, temperature not specified in the publication, wild-type ASPGB1
10.5
L-asparagine
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184Q
10.7
L-asparagine
-
pH 8.0, temperature not specified in the publication, ASPGB1 mutant R165T
12.7
L-asparagine
-
pH 8.0, temperature not specified in the publication, ASPGA1 mutant L163F
14.3
L-asparagine
-
pH 8.0, temperature not specified in the publication, ASPGA1 mutant T166R
14.7
L-asparagine
-
pH 8.0, temperature not specified in the publication, wild-type ASPGA1
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
activity is highest in sink tissues, especially in flowers and siliques
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F162L
-
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
-
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
-
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
-
site-directed mutagenesis of ASPGB1, the mutant shows a 3fold decrease in Vmax value with Asn as substrate
N184D
-
site-directed mutagenesis of ASPGB1, the mutant shows altered kinetics with substrate compared to the wild-type enzyme
N184Q
-
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
-
site-directed mutagenesis of ASPGB1, the mutant shows altered kinetics with substrate compared to the wild-type enzyme
S189A
-
site-directed mutagenesis of ASPGB1, the mutant shows a 3fold decrease in Vmax value with Asn as substrate
S189C
-
site-directed mutagenesis of ASPGB1, the mutant shows altered kinetics with substrate compared to the wild-type enzyme
S189T
-
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
-
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
-
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
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)
EXTERNAL LINKS (specific for EC-Number 3.5.1.1)
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