Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
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.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.018 - 0.068
L-asparagine
0.0095
diazo-4-oxo-L-norvaline
-
-
0.0125 - 5.3
L-asparagine
0.011 - 1.9
L-aspartyl-beta-hydroxamate
additional information
additional information
-
the Km of the immobilized enzyme is 8fold lower compared to the free enzyme
-
0.018
L-asparagine
K0.5 value, Hill coefficient 1.5, pH 8.0, 37°C
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
1.6
L-glutamine
K0.5 value, Hill coefficient 1.1, 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
0.0115
Asn
-
-
0.015
Asn
-
pH 7.0, 25°C, wild-type enzyme
0.095
Asn
-
pH 7.0, 25°C, mutant enzyme N248A
0.0125
L-asparagine
-
-
0.3
L-asparagine
pH 8.0, 45°C
0.442
L-asparagine
-
Vmax: 0.0699 mM/min, 37°C, pH not specified in the publication
5.1
L-asparagine
-
37°C, pH 8.0, mutant enzyme D178P
5.3
L-asparagine
-
37°C, pH 8.0, wild-type enzyme
0.011
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme V27L
0.015
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme V27M
0.035
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, wild-type enzyme
0.037
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme Q59E
0.04
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme G88A
0.05
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme G57V
0.05
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme G88I
0.056
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme N248D
0.069
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme G57A
0.07
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme G11V
0.082
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme G57L
0.13
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme G11L
0.14
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme N248W
0.15
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme N248Q
0.19
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme N248A
0.21
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme N248G
1.8
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme Q59G
1.9
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme Q59A
0.035
L-Gln
-
pH 7.0, 25°C, wild-type enzyme
2 - 3
L-Gln
-
pH 7.0, 25°C, mutant enzyme Q59E
2.4
L-Gln
-
pH 7.0, 25°C, mutant enzyme G57V
3.5
L-Gln
-
pH 7.0, 25°C, mutant enzyme N248D
4
L-Gln
-
pH 7.0, 25°C, mutant enzyme V27M
4.4
L-Gln
-
pH 7.0, 25°C, mutant enzyme V27L
5.7
L-Gln
-
pH 7.0, 25°C, mutant enzyme G57A
6
L-Gln
-
pH 7.0, 25°C, mutant enzyme N248G
10
L-Gln
-
pH 7.0, 25°C, mutant enzyme Q59A
16
L-Gln
-
pH 7.0, 25°C, mutant enzyme N248A
21
L-Gln
-
pH 7.0, 25°C, mutant enzyme N248Q
50
L-Gln
-
pH 7.0, 25°C, mutant enzyme Q59G
70
L-Gln
-
pH 7.0, 25°C, mutant enzyme N248E
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0027
L-asparagine
-
37°C, pH 8.0, wild-type enzyme and mutant enzyme D178P
0.004 - 29
L-aspartyl-beta-hydroxamate
additional information
additional information
-
turnover numbers for L-aspartyl-beta-hydroxamate with mutant enzyme G11L and G88I are below 0.01 per sec
-
48
L-asparagine
presence of 8 mM Gln, pH 8.0, 37°C
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
60
L-asparagine
pH 8.0, 37°C
67
L-asparagine
presence of 0.9 mM Gln, pH 8.0, 37°C
72
L-asparagine
presence of 0.3 mM Gln, pH 8.0, 37°C
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
2.2
L-glutamine
pH 8.0, 37°C
7
Asn
-
pH 7.0, 25°C, mutant enzyme N248A
24
Asn
-
pH 7.0, 25°C, wild-type enzyme
0.004
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme G88A
0.11
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme G11V
0.143
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme Q59G
0.2
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme G57L
0.46
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme N248D
0.86
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme G57V
2
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme Q59E
9.7
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme Q59A
10.3
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme V27L
10.8
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme V27M
15.4
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme G57A
21
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme N248Q
23
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme N248G
26
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme N248W
27
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, mutant enzyme N248A
29
L-aspartyl-beta-hydroxamate
-
pH 7.0, 25°C, wild-type enzyme
0.001
L-Gln
-
pH 7.0, 25°C, mutant enzyme Q59A
0.0024
L-Gln
-
pH 7.0, 25°C, mutant enzyme Q59E
0.0029
L-Gln
-
pH 7.0, 25°C, mutant enzyme N248A
0.0046
L-Gln
-
pH 7.0, 25°C, mutant enzyme N248G
0.006
L-Gln
-
pH 7.0, 25°C, mutant enzyme G57V
0.0068
L-Gln
-
pH 7.0, 25°C, mutant enzyme N248D
0.01
L-Gln
-
pH 7.0, 25°C, mutant enzyme G57A
0.01
L-Gln
-
pH 7.0, 25°C, mutant enzyme Q59G
0.019
L-Gln
-
pH 7.0, 25°C, mutant enzyme N248E
0.032
L-Gln
-
pH 7.0, 25°C, mutant enzyme N248Q
0.032
L-Gln
-
pH 7.0, 25°C, mutant enzyme V27M
0.091
L-Gln
-
pH 7.0, 25°C, mutant enzyme V27L
0.33
L-Gln
-
pH 7.0, 25°C, wild-type enzyme
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.
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.
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.
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.
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.
D90E
active site mutation
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
K196A/H197A
-
investigation of antigenicity, purification of mutant protein
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/R195S
-
activity similar to wild-type
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/H197A
-
investigation of antigenicity, purification of mutant protein
R195A/K196A
-
investigation of antigenicity, purification of mutant protein
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
S58A
-
crystallization of the mutant L-asparaginase II
T162A
-
mutation results in an active enzyme with no cooperativity
T179A
does not undergo autoprocessing
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
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
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.
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.
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.
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
brenda
Handschumacher, R.E.
Active site of L-asparaginase: reaction with diazo-4-oxonorvaline
Methods Enzymol.
46
432-435
1977
Escherichia coli
brenda
Wriston, J.C.; Yellin, T.O.
L-Asparaginase: a review
Adv. Enzymol. Relat. Areas Mol. Biol.
39
185-248
1973
Acinetobacter calcoaceticus, Acinetobacter glutaminasificans, Cupriavidus necator, Aspergillus niger, Aspergillus oryzae, Aspergillus terreus, Azotobacter agilis, Geobacillus stearothermophilus, Clostridium cadaveris, Weizmannia coagulans, Saccharomyces cerevisiae, Brucella abortus, Cavia porcellus, Gallus gallus, Lablab purpureus, Escherichia coli, Erwinia aroidea, Pectobacterium carotovorum, Fusarium tricinctum, Lupinus luteus, Platyrrhini, Mycobacterium tuberculosis, Mycobacterium avium, Mycobacterium tuberculosis variant bovis, Mycolicibacterium phlei, Mycolicibacterium smegmatis, Neurospora crassa, Proteus vulgaris, Pseudomonas sp., [Pseudomonas] boreopolis, Pseudomonas fluorescens, Rattus norvegicus, Salmonella typhosa, Serratia marcescens, Staphylococcus sp., Streptomyces griseus, Escherichia coli EC-I, Pseudomonas sp. P-210, Pseudomonas sp. GG13
brenda
Wriston, J.C.
L-Asparaginase
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
4
101-121
1971
Weizmannia coagulans, Cavia porcellus, Escherichia coli, Erwinia aroidea, Pectobacterium carotovorum, Fusarium tricinctum, Serratia marcescens
-
brenda
Newsted, W.J.; Ramjeesingh, M.; Zywulko, M.; Rothstein, S.J.; Shami, E.Y.
Engineering resistance to trypsin inactivation into L-asparaginase through the production of a chimeric protein between the enzyme and a protective single-chain antibody
Enzyme Microb. Technol.
17
575-764
1995
Escherichia coli
-
brenda
Kozak, M.; Jaskolski, M.
Crystallization and preliminary crystallographic studies of a new crystal form of Escherichia coli L-asparaginase II (Ser58Ala mutant)
Acta Crystallogr. Sect. D
56
509-511
2000
Escherichia coli (P00805), Escherichia coli
brenda
Iiboshi, Y.; Papst, P.J.; Hunger, S.P.; Terada, N.
L-Asparaginase inhibits the rapamycin-targeted signaling pathway
Biochem. Biophys. Res. Commun.
260
534-539
1999
Escherichia coli
brenda
Kozak, M.; Jurga, S.
A comparison between the crystal and solution structures of Escherichia coli asparaginase II
Acta Biochim. Pol.
49
509-513
2002
Escherichia coli
brenda
Sanches, M.; Barbosa, J.A.; de Oliveira, R.T.; Abrahao Neto, J.; Polikarpov, I.
Structural comparison of Escherichia coli L-asparaginase in two monoclinic space groups
Acta Crystallogr. Sect. D
59
416-422
2003
Escherichia coli
brenda
Jaskolski, M.; Kozak, M.; Lubkowski, J.; Palm, G.; Wlodawer, A.
Structures of two highly homologous bacterial L-asparaginases: a case of enantiomorphic space groups
Acta Crystallogr. Sect. D
D57
369-377
2001
Escherichia coli (P00805)
brenda
Derst, C.; Henseling, J.; Rohm, K.H.
Engineering the substrate specificity of Escherichia coli asparaginase. II. Selective reduction of glutaminase activity by amino acid replacements at position 248
Protein Sci.
9
2009-2017
2000
Escherichia coli
brenda
Roberts, J.; Burson, G.; Hill, J.M.
New procedures for purification of L-asparaginase with high yield from Escherichia coli
J. Bacteriol.
95
2117-2123
1968
Escherichia coli, Escherichia coli HAP
brenda
Zhang, Y.Q.; Tao, M.L.; Shen, W.D.; Zhou, Y.Z.; Ding, Y.; Ma, Y.; Zhou, W.L.
Immobilization of L-asparaginase on the microparticles of the natural silk sericin protein and its characters
Biomaterials
25
3751-3759
2004
Escherichia coli
brenda
Zhang, J.F.; Shi, L.Y.; Wei, D.Z.
Chemical modification of L-asparaginase from Escherichia coli with a modified polyethyleneglycol under substrate protection conditions
Biotechnol. Lett.
26
753-756
2004
Escherichia coli
brenda
Appel, I.M.; Hop, W.C.; Pieters, R.
Changes in hypercoagulability by asparaginase: a randomized study between two asparaginases
Blood Coagul. Fibrinolysis
17
139-146
2006
Escherichia coli, Dickeya chrysanthemi
brenda
Reinert, R.B.; Oberle, L.M.; Wek, S.A.; Bunpo, P.; Wang, X.P.; Mileva, I.; Goodwin, L.O.; Aldrich, C.J.; Durden, D.L.; McNurlan, M.A.; Wek, R.C.; Anthony, T.G.
Role of glutamine depletion in directing tissue-specific nutrient stress responses to L-asparaginase
J. Biol. Chem.
281
31222-31233
2006
Escherichia coli, Wolinella succinogenes
brenda
Gaofu, Q.; Jie, L.; Rongyue, C.; Xin, Y.; Dan, M.; Jie, W.; Xiangchun, S.; Qunwei, X.; Roque, R.S.; Xiuyun, Z.; Jingjing, L.
Asparaginase display of polypeptides in the periplasm of Escherichia coli: potential rapid pepscan technique for antigen epitope mapping
J. Immunol. Methods
299
9-19
2005
Escherichia coli
brenda
Jianhua, C.; Yujun, W.; Ruibo, J.; Min, W.; Wutong, W.
Probing the antigenicity of E. coli L-asparaginase by mutational analysis
Mol. Biotechnol.
33
57-65
2006
Escherichia coli
brenda
Khushoo, A.; Pal, Y.; Singh, B.N.; Mukherjee, K.J.
Extracellular expression and single step purification of recombinant Escherichia coli L-asparaginase II
Protein Expr. Purif.
38
29-36
2004
Escherichia coli
brenda
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
Michalska, K.; Borek, D.; Hernandez-Santoyo, A.; Jaskolski, M.
Crystal packing of plant-type L-asparaginase from Escherichia coli
Acta Crystallogr. Sect. D
64
309-320
2008
Escherichia coli
brenda
Verma, N.; Kumar, K.; Kaur, G.; Anand, S.
L-asparaginase: a promising chemotherapeutic agent
Crit. Rev. Biotechnol.
27
45-62
2007
Aliivibrio fischeri, Enterobacter cloacae, Aspergillus niger, Aspergillus tamarii, Aspergillus terreus, Saccharomyces cerevisiae, Saccharomyces cerevisiae (P38986), Cyberlindnera jadinii, Escherichia coli, Erwinia aroidea, Pectobacterium carotovorum, Erwinia sp., Thermus thermophilus, Lupinus angustifolius, Lupinus arboreus, Mycolicibacterium phlei, Nocardia asteroides, Photobacterium leiognathi, Photobacterium phosphoreum, Pseudomonas aeruginosa, Pseudomonas putida, Pseudomonas fluorescens, Rhodotorula toruloides, Rhodotorula mucilaginosa, Serratia marcescens, Sphagnum fallax, Staphylococcus sp., Tetrahymena pyriformis, Vibrio harveyi, Erwinia aroidea NRR LB-138, Pseudomonas aeruginosa 50071
brenda
Li, L.; Xie, T.; Li, H.; Qing, C.; Zhang, G.; Sun, M.
Enhancing the thermostability of Escherichia coli L-asparaginase II by substitution with Pro in predicted hydrogen-bonded turn structures
Enzyme Microb. Technol.
41
523-527
2007
Escherichia coli
-
brenda
Fu, C.H.; Sakamoto, K.M.
PEG-asparaginase
Expert. Opin. Pharmacother.
8
1977-1984
2007
Escherichia coli
brenda
Yun, M.K.; Nourse, A.; White, S.W.; Rock, C.O.; Heath, R.J.
Crystal structure and allosteric regulation of the cytoplasmic Escherichia coli L-asparaginase I
J. Mol. Biol.
369
794-811
2007
Escherichia coli
brenda
Bunpo, P.; Murray, B.; Cundiff, J.; Brizius, E.; Aldrich, C.J.; Anthony, T.G.
Alanyl-glutamine consumption modifies the suppressive effect of L-asparaginase on lymphocyte populations in mice
J. Nutr.
138
338-343
2008
Escherichia coli
brenda
Yong, W.; Zheng, W.; Zhu, J.; Zhang, Y.; Wang, X.; Xie, Y.; Lin, N.; Xu, B.; Lu, A.; Li, J.
L-Asparaginase in the treatment of refractory and relapsed extranodal NK/T-cell lymphoma, nasal type
Ann. Hematol.
88
647-652
2008
Escherichia coli
brenda
Nath, C.E.; Dallapozza, L.; Eslick, A.E.; Misra, A.; Carr, D.; Earl, J.W.
An isocratic fluorescence HPLC assay for the monitoring of L-asparaginase activity and L-asparagine depletion in children receiving E. coli L-asparaginase for the treatment of acute lymphoblastic leukaemia
Biomed. Chromatogr.
23
152-159
2009
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), Escherichia coli
brenda
Wei, Y.; Chen, J.; Jia, R.; Wang, M.; Wu, W.
Purification of Escherichia coli L-asparaginase mutants by a native polyacrylamide gel electrophoresis
J. Chromatogr. Sci.
46
556-559
2008
Escherichia coli
brenda
Teodor, E.; Litescu, S.C.; Lazar, V.; Somoghi, R.
Hydrogel-magnetic nanoparticles with immobilized L-asparaginase for biomedical applications
J. Mater. Sci. Mater. Med.
20
1307-1314
2009
Escherichia coli
brenda
Appel, I.M.; Hop, W.C.; van Kessel-Bakvis, C.; Stigter, R.; Pieters, R.
L-Asparaginase and the effect of age on coagulation and fibrinolysis in childhood acute lymphoblastic leukemia
Thromb. Haemost.
100
330-337
2008
Escherichia coli
brenda
Qiao, J.; Qi, L.; Ma, H.; Chen, Y.; Wang, M.; Wang, D.
Study on amino amides and enzyme kinetics of L-asparaginase by MCE
Electrophoresis
31
1565-1571
2010
Escherichia coli
brenda
Offman, M.N.; Krol, M.; Patel, N.; Krishnan, S.; Liu, J.; Saha, V.; Bates, P.A.
Rational engineering of L-asparaginase reveals importance of dual activity for cancer cell toxicity
Blood
117
1614-1621
2011
Escherichia coli
brenda
Borek, D.; Kozak, M.; Pei, J.; Jaskolski, M.
Crystal structure of active site mutant of antileukemic L-asparaginase reveals conserved zinc-binding site
FEBS J.
281
4097-4111
2014
Escherichia coli (P00805)
brenda
Kim, S.K.; Min, W.K.; Park, Y.C.; Seo, J.H.
Application of repeated aspartate tags to improving extracellular production of Escherichia coli L-asparaginase isozyme II
Enzyme Microb. Technol.
79-80
49-54
2015
Escherichia coli (P00805), Escherichia coli
brenda
Agrawal, S.; Kango, N.
Development and catalytic characterization of L-asparaginase nano-bioconjugates
Int. J. Biol. Macromol.
135
1142-1150
2019
Escherichia coli
brenda
Anishkin, A.; Vanegas, J.M.; Rogers, D.M.; Lorenzi, P.L.; Chan, W.K.; Purwaha, P.; Weinstein, J.N.; Sukharev, S.; Rempe, S.B.
Catalytic role of the substrate defines specificity of therapeutic L-asparaginase
J. Mol. Biol.
427
2867-2885
2015
Escherichia coli (P00805)
brenda
Zhang, Y.; Li, D.; Li, Y.
Expression and purification of L-asparaginase from Escherichia coli and the inhibitory effects of cyclic dipeptides
Nat. Prod. Res.
31
2099-2106
2017
Escherichia coli (C0KWF5)
brenda
Maggi, M.; Mittelman, S.D.; Parmentier, J.H.; Colombo, G.; Meli, M.; Whitmire, J.M.; Merrell, D.S.; Whitelegge, J.; Scotti, C.
A protease-resistant Escherichia coli asparaginase with outstanding stability and enhanced anti-leukaemic activity in vitro
Sci. Rep.
7
14479
2017
Escherichia coli (P00805), Escherichia coli
brenda