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Information on EC 3.5.1.1 - asparaginase and Organism(s) Wolinella succinogenes and UniProt Accession P50286

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.1 asparaginase
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This record set is specific for:
Wolinella succinogenes
UNIPROT: P50286 not found.
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The taxonomic range for the selected organisms is: Wolinella succinogenes
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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L-asparagine
+
H2O
=
L-aspartate
+
NH3
+
=
+
Synonyms
asparaginase, l-asnase, asrgl1, asparaginase ii, l-asparaginase ii, erwinase, ecaii, l-asparaginase i, ecaiii, diasp, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-asparaginase
-
-
-
-
asparaginase II
-
-
-
-
colaspase
-
-
-
-
crasnitin
-
-
-
-
DiAsp
-
-
-
-
elspar
-
-
-
-
L-ASNase
-
-
-
-
L-asparaginase
L-asparagine amidohydrolase
-
-
-
-
leunase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic acid amide hydrolysis
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-asparagine amidohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9015-68-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
reaction of EC 3.5.1.2
-
-
?
D-Asn + H2O
D-Asp + NH3
show the reaction diagram
-
6.5% of the activity with L-Asn
-
-
?
L-Asn + H2O
L-Asp + NH3
show the reaction diagram
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
-
-
-
?
L-aspartic acid beta-hydroxamate + H2O
L-Asp + hydroxylamine
show the reaction diagram
-
-
-
-
?
L-Gln + H2O
L-Glu + NH3
show the reaction diagram
-
not hydrolyzed at significant rate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-asparagine + H2O
L-aspartate + NH3
show the reaction diagram
-
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0217 - 0.0236
L-asparagine
0.32 - 0.38
L-glutamine
0.0478
L-asparagine
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
86.7 - 97.8
L-asparagine
1.58 - 11.33
L-glutamine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3700 - 4500
L-asparagine
4.2 - 35.3
L-glutamine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
-
x * 37000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 37000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no modification
-
no carbohydrate and phosphorus detected
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant S121P. Residue 121 impacts the conformation of the conserved tyrosine 27, a component of the catalytically-important flexible N-terminal loop
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S121P
mutant gains L-glutaminase activity, but retains L-asparaginase activity comparable to wild-type
additional information
-
applicated to mice, the enzyme abolishes serum asparagine, but not glutamine, the enzyme does not alter protein synthesis, overview
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for at least 3 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 andadult forms of acute lymphoblastic leukemia, ALL
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
Manually annotated by BRENDA team
Distasio, J.A.; Niederman, R.A.; Kafkewitz, D.; Goodman, D.
Purification and characterization of L-asparaginase with anti-lymphoma activity from Vibrio succinogenes
J. Biol. Chem.
251
6929-6933
1976
Wolinella succinogenes
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Nguyen, H.A.; Durden, D.L.; Lavie, A.
The differential ability of asparagine and glutamine in promoting the closed/active enzyme conformation rationalizes the Wolinella succinogenes L-asparaginase substrate specificity
Sci. Rep.
7
41643
2017
Wolinella succinogenes (P50286), Wolinella succinogenes DSM 1740 (P50286)
Manually annotated by BRENDA team