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Information on EC 3.5.1.1 - asparaginase and Organism(s) Helicobacter pylori and UniProt Accession Q9ZLB9
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3.5.1.1 asparaginaseSpecify your search results
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- 3.5.1.1
- leukemia
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- children
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remission
- erwinia
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event-free
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intrathecal
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l-aspartic
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philadelphia
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fried
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b-precursor
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standard-risk
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coli-derived
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multiagent
The taxonomic range for the selected organisms is: Helicobacter pylori
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-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
L-glutamine + H2O
L-glutamate + NH3
reaction of EC 3.5.1.2
-
-
?
L-asparagine + H2O
L-aspartate + NH3
strongly preferred substrate
-
-
?
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
strongly preferred substrate
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-Diazo-4-oxo-L-norvaline
-
inhibits L-asparaginase activity and affects broth culture filtrate inhibition of the cell cycle
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.23
L-asparagine
mutant M121C/T169M, cooperative kinetic toward L-Asn, Hill coefficient 1.7, pH 7.5, 37°C
0.25
L-asparagine
mutant M121C, cooperative kinetic toward L-Asn, Hill coefficient 1.5, pH 7.5, 37°C
0.25
L-asparagine
mutant T169M, cooperative kinetic toward L-Asn, Hill coefficient 1.8, pH 7.5, 37°C
46.4
L-glutamine
wild-type, cooperative kinetic toward L-Gln, Hill coefficient 2.0, pH 7.5, 37°C
76.5
L-glutamine
mutant Q63E, cooperative kinetic toward L-Gln, Hill coefficient 2.3, pH 7.5, 37°C
additional information
L-asparagine
kcat/Km: 66.41 1/mM*s, pH7.5, 37°C
additional information
L-glutamine
kcat/Km: 0.48 1/mM*s, pH7.5, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
29.6
L-asparagine
mutant T169M, cooperative kinetic toward L-Asn, Hill coefficient 1.8, pH 7.5, 37°C
30.2
L-asparagine
mutant M121C, cooperative kinetic toward L-Asn, Hill coefficient 1.5, pH 7.5, 37°C
60.7
L-asparagine
mutant M121C/T169M, cooperative kinetic toward L-Asn, Hill coefficient 1.7, pH 7.5, 37°C
0.19
L-glutamine
mutant Q63E, cooperative kinetic toward L-Gln, Hill coefficient 2.3, pH 7.5, 37°C
0.47
L-glutamine
wild-type, cooperative kinetic toward L-Gln, Hill coefficient 2.0, pH 7.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
Helicobacter pylori L-asparaginase is able to inhibit the cell-cycle of fibroblasts and gastric cell lines. Interference with cell-cycle in vitro depends on cell genotype and is related to the expression levels of the concurrent enzyme asparagine synthetase
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
M121C
M121C/T169M
Q63E
T169M
T16D
T95D
replacement of catalytic threonine, depletes the enzyme of its catalytic activities with L-asparagine and L-glutamine
M121C
mutants has nearly 2.5fold reduced catalytic activity compared to the wild type enzyme
M121C/T169M
the mutant has a preserved efficiency versus L-asparagine but is completely unable to carry out L-glutamine hydrolysis
M121C/T169M
mutant has a preserved efficiency vs L-asparagine but is completely unable to carry out L-glutamine hydrolysis. The mutant does not exert any cytotoxic effect on HL-60 cells
Q63E
the mutant endows with a similar catalytic efficiency versus L-asparagine and halved glutaminase efficiency with respect to the wild type enzyme
Q63E
mutant displays similar catalytic efficiency versus asparagine and halved glutaminase efficiency with respect to the wild type enzyme, is able to exert a cytotoxic effect comparable to, or higher than, the one of the wild type enzyme
T169M
mutants has nearly 4fold reduced catalytic activity compared to the wild type enzyme
T16D
replacement of catalytic threonine, depletes the enzyme of its catalytic activities with L-asparagine and L-glutamine
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
absolutely stable up to 50°C (10 min incubation time), 50% activity after 10 min at 53°C
53
the wild type enzyme shows 50% activity after 10 min incubation at 53°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dhavala, P.; Krasotkina, J.; Dubreuil, C.; Papageorgiou, A.C.
Expression, purification and crystallization of Helicobacter pylori L-asparaginase
Acta Crystallogr. Sect. F
64
740-742
2008
Helicobacter pylori
Cappelletti, D.; Chiarelli, L.R.; Pasquetto, M.V.; Stivala, S.; Valentini, G.; Scotti, C.
Helicobacter pylori L-asparaginase: a promising chemotherapeutic agent
Biochem. Biophys. Res. Commun.
377
1222-1226
2008
Helicobacter pylori (B6ZCD8), Helicobacter pylori CCUG 17874 (B6ZCD8)
Scotti, C.; Sommi, P.; Pasquetto, M.V.; Cappelletti, D.; Stivala, S.; Mignosi, P.; Savio, M.; Chiarelli, L.R.; Valentini, G.; Bolanos-Garcia, V.M.; Merrell, D.S.; Franchini, S.; Verona, M.L.; Bolis, C.; Solcia, E.; Manca, R.; Franciotta, D.; Casasco, A.; Filipazzi, P.; Zardini, E.; Vannini, V.
Cell-cycle inhibition by Helicobacter pylori L-asparaginase
PLoS ONE
5
e13892
2010
Helicobacter pylori
Maggi, M.; Chiarelli, L.R.; Valentini, G.; Scotti, C.
Engineering of Helicobacter pylori L-asparaginase: characterization of two functionally distinct groups of mutants
PLoS ONE
10
e0117025
2015
Helicobacter pylori (I0ZIE0), Helicobacter pylori, Helicobacter pylori CCUG 17874 (I0ZIE0)
Maggi, M.; Chiarelli, L.R.; Valentini, G.; Scotti, C.
Engineering of Helicobacter pylori L-asparaginase characterization of two functionally distinct groups of mutants
PLoS ONE
10
e0117025
2015
Helicobacter pylori (A0A2X5A091), Helicobacter pylori, Helicobacter pylori ATCC 43504 (A0A2X5A091)
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