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Information on EC 3.5.1.1 - asparaginase and Organism(s) Escherichia coli and UniProt Accession P00805
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- 3.5.1.1
- leukemia
- lymphoblastic
- children
-
remission
- erwinia
- hypersensitivity
- methotrexate
- lymphoma
- vincristine
-
pegylated
-
relapse
- pancreatitis
- 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
-
extranodal
-
fried
-
b-precursor
- succinogenes
-
standard-risk
- synthesis
-
coli-derived
- food industry
- diagnostics
- biotechnology
-
dana-farber
- pharmacology
- teniposide
- carotovora
-
multiagent
The taxonomic range for the selected organisms is: Escherichia coli
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
asparaginase II
colaspase
-
-
-
-
crasnitin
-
-
-
-
DiAsp
-
-
-
-
elspar
-
-
-
-
L-ASNase
L-asparaginase
L-asparagine amidohydrolase
-
-
-
-
leunase
-
-
-
-
asparaginase II
-
-
-
-
L-ASNase
-
-
-
-
L-asparaginase
-
-
-
-
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
diazo-4-oxo-L-norvaline + H2O
5-hydroxy-4-oxo-L-norvaline + NH3
-
-
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
reaction of EC 3.5.1.2
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
the enzyme reduces alpha-antiplasmin and plasminogen levels in human patients with acute lymphoblastic leukemia
-
-
?
additional information
?
-
-
the enzyme selectively inhibits rapamycin-targeted signaling pathway in leukemic cell lines, the enzyme suppresses synthesis of ribosomal proteins at the level of mRNA translation
-
-
?
additional information
?
-
-
residues 195RKH197 are critical for enzyme antigenicity
-
-
?
additional information
?
-
-
L-asparaginase from Escherichia coli is more immuno-depressive and immunotoxic than that from Erwinia carotovora
-
-
?
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
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
the enzyme reduces alpha-antiplasmin and plasminogen levels in human patients with acute lymphoblastic leukemia
-
-
?
additional information
?
-
-
residues 195RKH197 are critical for enzyme antigenicity
-
-
?
additional information
?
-
-
L-asparaginase from Escherichia coli is more immuno-depressive and immunotoxic than that from Erwinia carotovora
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Glutaraldehyde
-
inhibits the enzyme during immobilization at concentrations above 0.2%
Trypsin
-
the free enzyme is completely inactivated by trypsin within 10 min, while the immobilized enzyme is stable for 240 min with loss of 30% activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
the Km of the immobilized enzyme is 8fold lower compared to the free enzyme
-
0.021
L-asparagine
K0.5 value, Hill coefficient 1.4, presence of 0.3 mM Gln, pH 8.0, 37°C
0.025
L-asparagine
K0.5 value, Hill coefficient 1.4, presence of 0.9 mM Gln, pH 8.0, 37°C
0.03
L-asparagine
wild-type, pH not specified in the publication, temperature not specified in the publication
0.03
L-asparagine
mutant N24S, pH not specified in the publication, temperature not specified in the publication
0.068
L-asparagine
K0.5 value, Hill coefficient 1.0, presence of 8 mM Gln, pH 8.0, 37°C
3.95
L-glutamine
wild-type, pH not specified in the publication, temperature not specified in the publication
4.14
L-glutamine
mutant N24S, pH not specified in the publication, temperature not specified in the publication
0.442
L-asparagine
-
Vmax: 0.0699 mM/min, 37°C, pH not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0027
L-asparagine
-
37°C, pH 8.0, wild-type enzyme and mutant enzyme D178P
additional information
additional information
-
turnover numbers for L-aspartyl-beta-hydroxamate with mutant enzyme G11L and G88I are below 0.01 per sec
-
58.8
L-asparagine
mutant N24S, pH not specified in the publication, temperature not specified in the publication
59.8
L-asparagine
wild-type, pH not specified in the publication, temperature not specified in the publication
0.51
L-glutamine
wild-type, pH not specified in the publication, temperature not specified in the publication
0.53
L-glutamine
mutant N24S, pH not specified in the publication, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
710
L-asparagine
using K0.5 value, Hill coefficient 1.0, presence of 8 mM Gln, pH 8.0, 37°C
1782
L-asparagine
mutant N24S, pH not specified in the publication, temperature not specified in the publication
1975
L-asparagine
wild-type, pH not specified in the publication, temperature not specified in the publication
2700
L-asparagine
using K0.5 value, Hill coefficient 1.4, presence of 0.9 mM Gln, pH 8.0, 37°C
3300
L-asparagine
using K0.5 value, Hill coefficient 1.5, pH 8.0, 37°C
3400
L-asparagine
using K0.5 value, Hill coefficient 1.4, presence of 0.3 mM Gln, pH 8.0, 37°C
0.13
L-glutamine
wild-type, pH not specified in the publication, temperature not specified in the publication
0.13
L-glutamine
mutant N24S, pH not specified in the publication, temperature not specified in the publication
1400
L-glutamine
using K0.5 value, Hill coefficient 1.1, pH 8.0, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
103
mutant N24S, pH not specified in the publication, temperature not specified in the publication
105
wild-type, pH not specified in the publication, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.6
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
the synthesis of L-asparaginase in Escherichia coli W and Escherichia coli K-12 is almost completely suppressed if glucose is added at a concentration of 0.5% to the growth medium. Organic acids and amino acids such as L-leucine and L-methionine enhance production of L-asparaginase. n-Dodecane at 6% increases cell concentration by 12.7% and production of L-asparaginase by 21% to give 60.8 IU/ml in the fermentation medium
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
L-asparaginase is degraded by leukemic lysosomal cysteine proteases
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33000
SDS-PAGE, intact precursor molecule, 19000 + 14000 (native protein) after autoproteolysis
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
additional information
additional information
-
potential rapid pepscan technique for antigen epitope mapping
additional information
-
residues 195RKH197 are critical for enzyme antigenicity
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant enzyme D90E, hanging drop vapor diffusion method, using 25% PEG MME 550, 100 mM MES pH 6.5, 10 mM ZnSO4 or 30% (w/v) PEG MME 550, 100 mM bicine pH 9.0, 100 mM NaCl or 100 mM HEPES pH 7.5, saturated solution of tribasic sodium citrate mixed with buffer, at citrate:buffer ratio of 9:1
mutant enzyme Y25F, untreated crystals and crystals soaked with L-hydroxylysine. Comparison with previously reported structures. The loop acting as a gate over the active site is very flexible. Its structure in the native enzyme is primarily controlled by the occupancy of the active site
the aspartate product in the crystal structure of L-ASP exists in an unusual alpha-COOH protonation state. The crystal structures may represent intermediate steps rather than initial binding. The substrate's alpha-carboxyl may serve as a proton acceptor and activate one of the catalytic threonines during L-ASP's nucleophilic attack on the amide carbon
hanging-drop vapour-diffusion method, X-ray structure of the enzyme, crystallized in a new form, space group C2 and refined to 1.95 A resolution, is compared with that of the previously determined crystal for, space group P2(1)
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N24S
mutant shows completely preserved asparaginase and glutaminase activities, long-term storage stability, improved thermal parameters, and good resistance to proteases derived from leukaemia cells. The mutant displays a modification in the hydrogen bond network related to residue 24, and a general rigidification of the monomer as compared to wild-type
D178P
-
mutation enhances the thermostability of the enzyme without changing the activity of the enzyme and thus the therapeutical use of L-asparaginase II might be benefit from these result
G11V
-
518fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value
G57A
-
3.8fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 5.2fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value
G57L
-
346fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value
G57V
-
48.8fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 37fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value
G88A
-
8300fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value
N248A
-
5.9fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 4657fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value. Loss in transition state stabilization is 15 kJ per mol for L-glutamine, 4 kJ per mol for L-aspartic beta-hydroxamate and 7 kJ per mol for L-asparagine
N248D
-
10.18fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 49fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value. Loss in transition state stabilization is 10 kJ per mol for L-glutamine and 6 kJ per mol for L-aspartic beta-hydroxamate
N248E
-
4.4fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 34.4fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value. Loss in transition state stabilization is 9 kJ per mol for L-glutamine and 4 kJ per mol for L-aspartic beta-hydroxamate
N248G
-
7.5fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 116fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value. Loss in transition state stabilization is 12 kJ per mol for L-glutamine and 5 kJ per mol for L-aspartic beta-hydroxamate
N248Q
-
5.9fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 6.2fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value. Loss in transition state stabilization is 10 kJ per mol for L-glutamine and 4 kJ per mol for L-aspartic beta-hydroxamate
N24A
-
increase in activity compared to wild-type, a unique hydrogen bond network contributes to higher activity
N24A/Y250L
-
about 75% of wild-type activity. Mutation Y250L is an interface mutation selected to stablize the active tetramer
N24G
-
mutant has a much higher loop flexibility compared with those of wild-type and the other mutants, and a decreased catalytic activity
N24H
-
mutant displays low flexibility in the central part of the loop; the C-terminal region of the loop shows high RMSF values that are likely to cause stability problems
N24S/D281E
-
RMSF profile similar to that of WT, with a slight increase in flexibility for residues 20-24
N24T
-
increase in activity compared to wild-type. Mutant has very stable lid-loops, resulting in a tightly locked substrate molecule in the active site, stabilized for the catalytic reaction
N24T/R195S
-
about 85% of wild-type activity. Mutation R195S is an interface mutation selected to stablize the active tetramer
N24T/Y250L
-
about 70% of wild-type activity. Mutation Y250L is an interface mutation selected to stablize the active tetramer
Q59A
-
163fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 930fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value. Loss in transition state stabilization is 17 kJ per mol for L-glutamine and 13 kJ per mol for L-aspartic beta-hydroxamate
Q59E
-
15.4fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 93fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value. Loss in transition state stabilization is 7 kJ per mol for L-glutamine and 11 kJ per mol for L-aspartic beta-hydroxamate
Q59G
-
105fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 465fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value. Loss in transition state stabilization is 15 kJ per mol for L-glutamine and 12 kJ per mol for L-aspartic beta-hydroxamate
R195A/K196A/H197A
R240A
-
mutation increases the [S]0.5 value to 5.9 mM, presumably by reducing the affinity of the site for L-asparagine, although the enzyme retains cooperativity
V27L
-
1.13fold increase in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 4.4fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value
V27M
-
1.5fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 11.6fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value
additional information
R195A/K196A/H197A
-
alanine-scanning mutagenesis for determination of amino acid residues critical for antigenicity, construction of four mutants, the mutants' antigenicity is greatly reduced
R195A/K196A/H197A
-
investigation of antigenicity, purification of mutant protein
additional information
-
applicated to mice, the enzyme abolishes serum asparagine and glutamine, and reduces protein synthesis in liver, and spleen, but not in pancreas via increase dephosphorylation of the translation factor eIF2, overview
additional information
-
construction of a chimeric enzyme composed of asparaginase, a tetanus toxin peptide spacer, fragment 831-854, and the foreign cholesteryl ester transfer protein C-terminal fragment, targeting to and expression in the periplasm of Escherichia coli
additional information
-
covalent immobilization of L-asparaginase on poorly soluble microparticles of the natural silk sericin protein, MW 50-200 kDa, from Bomby mori, best at 0.15% glutaraldehyde in 50 mM citrate buffer, pH 8.6, method optimization and biochemical properties of the enzyme-conjugate, overview
additional information
-
reduction of the allergenic potential of the enzyme as therapeutic agent by chemical modification of the enzyme with 2,4-bis(O-methoxypolyethyleneglycol)-6-chloro-S-triazine, mPEG2, in presence of L-asparagine, optimally with a mPEG2/-NH2 molar ratio of 10, the modified enzyme retains 33% of initial enzymatic activity with complete abolishment of immunogenicity, in vitro half-life increments from 4.6 h to 33 h is obtained, method overview
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
activities of wild-type and mutant enzyme D178P are stable for 0-4 h. Thereafter, the residual activity of wild type decreases rapidly. After 6 h incubation, wild type enzyme loses 35% activity. The mutant D178P loses 19% activity
45
-
60 min, 97% of activity of mutant enzyme D178P remains, 79% of wild-type activity remains
50
55
-
60 min, 72% of activity of mutant enzyme D178P remains, 56% of wild-type activity remains
60
additional information
-
D178P mutation enhances the thermostability of the enzyme without changing the activity of the enzyme and thus the therapeutical use of L-asparaginase II might be benefit from these result
50
-
60 min, 90% of activity of mutant enzyme D178P remains, 71% of wild-type activity remains
60
-
60 min, 52% of activity of mutant enzyme D178P remains, 43% of wild-type activity remains
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the trypsin sensitive enzyme can be rendered trypsin resistant by genetically fusing its gene with that of a single-chain antibody derived from a preselected monoclonal antibody capable of providing protection against trypsin. The chimeric L-asparaginase retains 75% of its original activity upon exposure to trypsin, the native unprotected enzyme is totally inactivated
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, after 3 weeks, the residual activity of wild-type enzyme decreases more rapidly compared to the D178P. After 5 weeks, wild-type enzyme loses 80% of its activity, the mutant enzyme D178P loses 58% of its activity
-
5°C, sterile enzyme solution with high specific activity, several weeks, no loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
further purification of the commercial preparation by gel filtration to remove endotoxin
-
native wild-type and recombinant mutant chimeric enzyme from the periplasm of strain BL21(DE3) by periplasm preparation through osmotic shock, and anion exchange chromatography
-
recombinant enzyme 3.3fold from strain BLR(DE3) culture supernatant by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the mutant chimeric enzyme in the periplasm of strain BL21(DE3)
-
expression of the N-terminally His-tagged enzyme fused to the pelB leader sequence under control of the T7lac promoter in strain BLR(DE3), the recombinant enzyme is secreted to the cell culture medium
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
the enzyme is an important drug in the treatment of childhood acute lymphoblastic leukemia
synthesis
recombinant asparaginase isozyme AnsB fused with the pelB signal sequence and a five aspartate tag is secreted efficiently into culture medium at 34.6 U/mg cell of specific activity. By batch fermentation, recombinant Escherichia coli produces 40.8 U/ml asparaginase isozyme II in the medium. Deletion of the gspDE gene reduces extracellular production of asparaginase isozyme II
analysis
-
direct measurement of L-asparagine in human plasma samples through the use of Escherichia coli Lasparaginase in the soluble form is a major clinical application of this system
biotechnology
-
development of a MCE method (micellar electrokinetic electrophoresis) that is sufficiently sensitive and selective for the separation of amino amides and determination of enzyme kinetic constants of L-Asnase
medicine
medicine
-
the use of asparaginase II as a drug for the treatment of acute lymphoblastic leukemia is complicated by the significant glutaminase side activity of the enzyme. Selective reduction in glutaminase activity in variant B248A and other N248 variants
medicine
-
potent antineoplastic agent in animals which has given complete remission in some human leukemias
medicine
-
L-asparaginase is important in the induction regimen for treating human acute lymphoblastic leukemia, cytotoxic complications are clinically significant problems lacking mechanistic insight, the enzyme is used in the treatment of both pediatric and adult forms of acute lymphoblastic leukemia, ALL
medicine
-
the enzyme is a potential therapeutic agent in acute lymphocytic leukemia, acute lymphoblastic leukemia, and chromic myelogenyous leukemia, but causes high allergic reactions
medicine
-
the enzyme is used for acute lymphoblastic leukemia treatment, the enzyme reduces alpha-antiplasmin and plasminogen levels in human patients, this together with the elevated level of thrombin activity in the patients lead to an enhanced risk for thrombosis due to delay in fibrin elimination in Escherichia coli L-asparaginase-treated patients, overview
medicine
-
asparaginase is used in the treatment of acute lymphoblastic leukemia. It depletes plasma asparagine and glutamine, killing leukemic lymphoblasts but also causing immunosuppression. Asparaginase reduces maturing populations of normal B and T cells in thymus, bone marrow, and spleen of mice. Oral consumption of alanyl-glutamine mitigates metabolic stress in spleen, supporting the peripheral immune system and cell-mediated immunity during asparaginase chemotherapy
medicine
-
the enzyme is important to the treatment of acute lymphoblastic leukemia. Intravenous PEG-asparaginase (L-asparaginase covalently linked to polyethylene glycol) will eliminate painful injection, and achieve rapid peak levels and asparagine depletion
medicine
-
covalent immobilization of enzyme on functionalized aluminium oxide nanoparticles (AONP) and titanium oxide nanoparticles (TONP) for anticancer therapy. The nano-bioconjugates are optimally active at pH 7.0 and 40°C. TONP-asparaginase activity is enhanced in the presence of NH4+ (160%) and Mn2+ (165%) while AONP-asparaginase bioconjugates show increased relative activity with ethyl acetate (142%) and toluene (160%). The nano-bioconjugates display good reusability and maintain over 90% average activity after nine successive cycles. Maximum cytotoxicity (61%) is noticed with AONP-asparaginase against human leukemia MOLT-4 cells. AONP-asparaginase shows better affinity to L-asparagine as compared to free enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wriston, J.C.
Asparaginase
Methods Enzymol.
113
608-618
1985
Azotobacter vinelandii, Acinetobacter calcoaceticus, Klebsiella aerogenes, Saccharomyces cerevisiae, Cavia porcellus, Chlamydomonas sp., Citrobacter freundii, Escherichia coli, Pectobacterium carotovorum, Fusarium tricinctum, Lupinus angustifolius, Lupinus arboreus, Lupinus polyphyllus, Pisum sativum, Proteus vulgaris, Stenotrophomonas geniculata, Serratia marcescens, Wolinella succinogenes
Handschumacher, R.E.
Active site of L-asparaginase: reaction with diazo-4-oxonorvaline
Methods Enzymol.
46
432-435
1977
Escherichia coli
Wriston, J.C.; Yellin, T.O.
L-Asparaginase: a review
Adv. Enzymol. Relat. Areas Mol. Biol.
39
185-248
1973
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