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Information on EC 3.5.1.1 - asparaginase and Organism(s) Pseudomonas aeruginosa
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- 3.5.1.1
- leukemia
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remission
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event-free
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antileukemic
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intrathecal
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l-aspartic
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reinduction
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multiagent
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
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
-
-
-
-
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
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
Mg2+
Zn2+
1 mM, 109% of initial activity, 5 mM, 86% of initial activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
glucose, in supplemented culture medium, causes a slight suppression of enzyme expression in wild-type strain NRRL B771
-
Zn2+
1 mM, 109% of initial activity, 5 mM, 86% of initial activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5925
-
pH not specified in the publication, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
solid state, production evaluation and optimization of culture conditions using factorial designs
additional information
-
a pH of 7.9, casein hydrolysate (3.11%) and corn-steep liquor (3.68%) are the most significant factors improving the enzyme production process
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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
160000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
recombinant expression of Vitreoscilla hemoglobin, VHb, in Pseudomonas aeruginosa strain PaJC, the L-asparaginase expression in the recombinant strain is stimulated by glucose, while it is slightly repressed in the wild-type strain NRRL B771, and shows increased enzyme production due to increased oxygen uptake caused by VHb and preference for glucose to other sugars as growth carbon source, optimization of L-asparaginase production, overview
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
20 min, almost 80% residual activity, 30 min, almost 60% residual activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from strain 50071, grown on solid-state fermentation, 106fold to homogeneity by ammonium sulfate fractionation, gel filtration, and ion exchange chromatography
-
recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the maximum amount of L-asparaginase produced is 785U/ml from the optimized medium containing L-asparagine (0.5%), glucose (0.2%), NaCl (0.045%)and K2HPO4 (0.045%)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
pharmacology
-
L-asparaginase is a cancer chemotherapeutically important enzyme
medicine
-
used for treatment of acute lymphoblastic leukemia, pancreatic carcinoma, and bovine lymphosarcoma
medicine
-
purified L-asparaginase does not show hemolysis effect on blood erythrocytes. Recombinant L-asparaginase retains 50% of its initial activity after 90 and 60 min incubation in serum and trypsin separately
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Abdel-Fattah, Y.R.; Olama, Z.A.
L-asparaginase production by Pseudomonas aeruginosa in solid-state culture: evaluation and optimization of culture conditions using factorial designs
Process Biochem.
38
115-122
2002
Pseudomonas aeruginosa, Pseudomonas aeruginosa 50071
-
El-Bessoumy, A.A.; Sarhan, M.; Mansour, J.
Production, isolation, and purification of L-asparaginase from Pseudomonas aeruginosa 50071 using solid-state fermentation
J. Biochem. Mol. Biol.
37
387-393
2004
Pseudomonas aeruginosa, Pseudomonas aeruginosa 50071
Geckil, H.; Gencer, S.; Ates, B.; Ozer, U.; Uckun, M.; Yilmaz, I.
Effect of Vitreoscilla hemoglobin on production of a chemotherapeutic enzyme, L-asparaginase, by Pseudomonas aeruginosa
Biotechnol. J.
1
203-208
2006
Pseudomonas aeruginosa, Pseudomonas aeruginosa NRRL B771
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
Badoei-Dalfard, A.
Purification and characterization of L-asparaginase from Pseudomonas aeruginosa strain SN004 Production optimization by statistical methods
Biocatal. Agricult. Biotechnol.
4
388-397
2015
Pseudomonas aeruginosa, Pseudomonas aeruginosa SN004
-
El-Sharkawy, A.; Farag, A.; Embaby, A.; Saeed, H.; El-Shenawy, M.
Cloning, expression and characterization of aeruginosa EGYII L-asparaginase from Pseudomonas aeruginosa strain EGYII DSM 101801 in E.coli BL21(DE3) pLysS
J. Mol. Catal. B
132
16-23
2016
Pseudomonas aeruginosa (A0A0U3U5E8), Pseudomonas aeruginosa DSM 101801 (A0A0U3U5E8)
-
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