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Information on EC 3.5.1.1 - asparaginase
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3.5.1.1 asparaginaseSpecify your search results
Word Map
- 3.5.1.1
- leukemia
- lymphoblastic
- children
-
remission
- erwinia
- vincristine
-
pediatric
- methotrexate
- lymphoma
- hypersensitivity
-
relapse
- thrombosis
-
pegylated
- prednisone
- pancreatitis
-
consolidation
-
event-free
-
high-dose
- cytarabine
-
intensification
-
oncology
- venous
-
schedule
-
intrathecal
- cyclophosphamide
- chrysanthemi
- mercaptopurine
- medicine
- antithrombin
- daunorubicin
-
prophylaxis
-
arabinoside
-
reinduction
-
antileukemic
- thromboembolism
- allergy
- anthracyclines
-
cranial
-
l-aspartic
-
dana-farber
- pharmacology
- teniposide
-
multiagent
-
extranodal
-
coli-derived
- osteonecrosis
- biotechnology
- analysis
-
nordic
- diagnostics
-
standard-risk
- succinogenes
- food industry
-
b-precursor
- synthesis
-
fried
- carotovora
The enzyme appears in viruses and cellular organisms
Synonyms
asparaginase, l-asnase, asparaginase ii, l-asparaginase ii, asrgl1, erwinase, ecaii, l-asparaginase i, ecaiii, diasp, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
14270 ASNase
AnsA
ansA3
AnsB
ansZ
Asn
ASNase
ASNase1
ASNase3
ASP1
asparaginase
asparaginase II
asparagine amidohydrolase
ASPG II
-
three forms, ASPG I, ASPG II, and ASPG III. ASPG II shows the highest specific activity
ErA
glutamine-(asparagin-)ase
HPA
L-ASNase
L-asparaginase
L-asparaginase II
L-asparaginase III
L-asparagine amidohydrolase
SGR ASNase
type II L-asparaginase
Ypa
L-asparaginase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-asparagine + H2O = L-aspartate + NH3
-
-
-
-
L-asparagine + H2O = L-aspartate + NH3
active site structure involving Thr193, autocatalytic activation mechanism involving Thr193
-
L-asparagine + H2O = L-aspartate + NH3
active site structure with a flexible loop that is stabilized by a beta-hairpin formation and intracellular interaction with the alpha-helical region, modelling
-
L-asparagine + H2O = L-aspartate + NH3
kinetic model, substrate specificity, and catalytic mechanism, active site residues are Asp115 and Glu82, the structural transition of the enzyme is rate-limiting in the reaction, entropy changes are the main determinants for the substrate specificity
-
L-asparagine + H2O = L-aspartate + NH3
kinetic model, substrate specificity, and catalytic mechanism, active site residues are Asp115 and Glu82, the structural transition of the enzyme is rate-limiting in the reaction, entropy changes are the main determinants for the substrate specificity
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
L-asparagine amidohydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
9015-68-3
-
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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
benzyloxycarbonyl-Gly-L-Asn + H2O
benzyloxycarbonyl-Gly-L-Asp
-
-
-
?
beta-Asp-His + H2O
?
-
substrate of ASPGA1 and ASPGB1, ASPGA1 has a 4fold substrate preference for beta-Asp-His over Asn
-
?
beta-aspartoethylamide + H2O
?
-
at 0.4% of the activity with L-Asn
-
?
beta-aspartomethylamide + H2O
L-Asp + ethylamine
-
at 0.5% of the activity with L-Asn
-
?
beta-aspartopropylamide + H2O
?
-
at 0.7% of the activity with L-Asn
-
?
D-aspartic acid beta-hydroxamate + H2O
D-Asp + hydroxylamine
-
59% of the activity with L-Asn
-
?
diazo-4-oxo-L-norvaline + H2O
5-hydroxy-4-oxo-L-norvaline + NH3
-
-
-
?
DL-Ala-DL-Asn + H2O
DL-Ala-DL-Asn + DL-Ala-DL-Asp
-
-
75% Ala-Asp + 25% Ala-Asn
?
L-aspartic acid beta-hydrazide + H2O
L-Asp + hydroxylamine
-
2% of the activity with L-Asn
-
?
L-glutamic acid gamma-hydroxamate + H2O
L-Glu + hydroxylamine
-
1% of the activity with L-Asn
-
?
L-glutamine + H2O
L-glutamate + H2O
-
36% relative activity compared to L-asparagine as substrate
-
?
L-glutamyl hydroxamate + H2O
L-glutamate + hydroxylamine
-
16% relative activity compared to L-asparagine as substrate
-
?
N-acetyl-L-asparagine + H2O
N-acetyl-L-aspartic acid + NH3
-
-
?
N4-ethyl-L-asparagine
L-Asp + propylamine
-
12% of the activity with L-Asn
-
?
N4-methoxy-L-asparagine + H2O
L-Asp + O-methylhydroxylamine
-
154% of the activity with L-Asn
-
?
N4-methyl-L-asparagine
L-Asp + methylamine
-
12% of the activity with L-Asn
-
?
Nalpha-acetyl-L-asparagine + H2O
Nalpha-acetyl-L-aspartate + NH3
-
-
-
?
Nalpha-methyl-L-Asn + H2O
Nalpha-methyl-L-Asp + NH3
-
26% of the activity with L-Asn
-
?
threo-3-hydroxy-L-asparagine + H2O
?
-
36% of the activity with L-Asn
-
?
beta-cyano-L-Ala + H2O
?
-
at 5.7% of the activity with L-Asn
-
?
D-Asn + H2O
D-Asp + NH3
-
at 5% of the activity with L-Asn
-
?
D-asparagine + H2O
D-aspartate + NH3
-
catalytic activity of the recombinant enzyme for L-asparagine is 5fold higher than for D-asparagine
-
?
D-asparagine + H2O
D-aspartate + NH3
-
less than 10% activity compared to L-asparagine
-
?
D-asparagine + H2O
D-aspartate + NH3
negligible activity
-
?
DL-aspartyl hydroxamate + H2O
DL-Asp + hydroxylamine
-
66% of the activity with L-Asn
-
?
L-Asn + H2O
L-Asp + NH3
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
strictly specific for L-Asn, has no activity towards beta-aspartyl dipeptides
-
?
L-asparagine + H2O
L-aspartate + NH3
-
substrate of ASPGA1 and ASPGB1, but ASPGB1 has a 45fold higher specific activity with Asn as substrate than ASPGA1, ASPGA1 has a 4fold substrate preference for beta-Asp-His over Asn
-
?
L-asparagine + H2O
L-aspartate + NH3
-
catalytic activity of the recombinant enzyme for L-asparagine is 5fold higher than for D-asparagine
-
?
L-asparagine + H2O
L-aspartate + NH3
-
highly specific substrate
-
?
L-asparagine + H2O
L-aspartate + NH3
100% activity
-
?
L-asparagine + H2O
L-aspartate + NH3
-
substrate hydrolysis efficiency of L-asparagine is 8fold higher than that of L-glutamine
-
?
L-asparagine + H2O
L-aspartate + NH3
-
the enzyme does not reduce alpha-antiplasmin and plasminogen levels in human patients with acute lymphoblastic leukemia
-
?
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
-
?
L-asparagine + H2O
L-aspartate + NH3
strongly preferred substrate
-
?
L-asparagine + H2O
L-aspartate + NH3
strongly preferred substrate
-
?
L-asparagine + H2O
L-aspartate + NH3
highly specific substrate
-
?
L-asparagine + H2O
L-aspartate + NH3
highly specific substrate
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
highest specificity for L-asparagine
-
?
L-asparagine + H2O
L-aspartate + NH3
highest specificity for L-asparagine
-
?
L-asparagine + H2O
L-aspartate + NH3
best substrate
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
?
L-asparagine + H2O
L-aspartic acid + NH3
-
specificity: free from L-glutaminase activity
-
?
L-asparagine + H2O
L-aspartic acid + NH3
-
specificity: free from L-glutaminase activity
-
?
L-aspartic acid + NH3
?
less than 3% activity compared to L-asparagine
-
?
L-aspartic acid + NH3
?
less than 3% activity compared to L-asparagine
-
?
L-aspartic acid beta-hydroxamate + H2O
L-Asp + hydroxylamine
-
59% of the activity with L-Asn
-
?
L-aspartic acid beta-hydroxamate + H2O
L-Asp + hydroxylamine
-
11% of the activity with L-Asn
-
?
L-aspartic acid beta-hydroxamate + H2O
L-Asp + hydroxylamine
-
11% of the activity with L-Asn
-
?
L-aspartic acid beta-hydroxamate + H2O
L-Asp + hydroxylamine
-
-
-
?
L-aspartyl hydroxamate + H2O
L-aspartate + hydroxylamine
-
60% relative activity compared to L-asparagine as substrate
-
?
L-Gln + H2O
L-Glu + NH3
-
to about the same extent as L-Asn
-
?
L-Gln + H2O
L-Glu + NH3
-
at 10% of the activity with L-Asn
-
?
L-Gln + H2O
L-Glu + NH3
-
at 4% of the activity with L-asparagine
-
?
L-glutamine + H2O
?
58.2% activity compared to L-asparagine
-
?
L-glutamine + H2O
L-glutamate + NH3
-
recombinant enzyme has 4fold higher activity for L-asparagine than for L-glutamine
-
?
L-glutamine + H2O
L-glutamate + NH3
-
less than 1% activity compared to L-asparagine
-
?
L-glutamine + H2O
L-glutamate + NH3
less than 1% activity compared to L-asparagine
-
?
L-glutamine + H2O
L-glutamate + NH3
less than 1% activity compared to L-asparagine
-
?
L-glutamine + H2O
L-glutamate + NH3
reaction of EC 3.5.1.2
-
?
L-glutamine + H2O
L-glutamate + NH3
reaction of EC 3.5.1.2
-
?
L-glutamine + H2O
L-glutamate + NH3
reaction of EC 3.5.1.2
-
?
L-glutamine + H2O
L-glutamate + NH3
-
reaction of EC 3.5.1.2
-
?
L-glutamine + H2O
L-glutamate + NH3
negligible activity
-
?
L-glutamine + H2O
L-glutamate + NH3
reaction of EC 3.5.1.2
-
?
L-glutamine + H2O
L-glutamate + NH3
reaction of EC 3.5.1.2
-
?
L-glutamine + H2O
L-glutamate + NH3
YpA L-glutaminase activity is relatively low and more than 15 times less than specific activity towards L-Asn
-
?
L-glutamine + H2O
L-glutamate + NH3
YpA L-glutaminase activity is relatively low and more than 15 times less than specific activity towards L-Asn
-
?
poly-L-asparagine + H2O
?
-
at 21.7% of the activity with L-Asn
-
?
additional information
?
-
-
the enzyme shows anti-leukemic activity
-
?
additional information
?
-
not active with N-acetylglucosaminyl-L-Asn
-
?
additional information
?
-
no activity with D-asparagine monohydrate and L-glutamic acid
-
?
additional information
?
-
-
no activity with D-asparagine monohydrate and L-glutamic acid
-
?
additional information
?
-
-
no activity with D-glutamine, L-aspartic acid, D-aspartic acid, L-glutamic acid, and ornathine
-
?
additional information
?
-
no activity with D-asparagine monohydrate and L-glutamic acid
-
?
additional information
?
-
-
no activity with D-asparagine monohydrate and L-glutamic acid
-
?
additional information
?
-
-
the recombinant enzyme shows low affinity to L-glutamine
-
?
additional information
?
-
-
the recombinant enzyme shows low affinity to L-glutamine
-
?
additional information
?
-
-
the enzyme requires autocleavage to become active
-
?
additional information
?
-
the enzyme lacks L-glutaminase activity
-
?
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
-
?
additional information
?
-
-
L-asparaginase is cytotoxic, resistance to L-asparaginase in TEL-AML1-negative but not TEL-AML1-positive pediatric acute lymphoblastic cells is due to increased cellular expression of asparagine synthase, overview
-
?
additional information
?
-
to become enzymatically active, ASNase3 must undergo autocleavage between residues Gly167 and Thr168
-
?
additional information
?
-
-
to become enzymatically active, ASNase3 must undergo autocleavage between residues Gly167 and Thr168
-
?
additional information
?
-
-
the enzyme performs autocatalytic activation, overview
-
?
additional information
?
-
no activity with L-glutamine, L-aspartic acid, L-glutamic acid, thiourea, L-histidine, glutathione, L-arginine, and glycine
-
?
additional information
?
-
no activity with L-glutamine, L-aspartic acid, L-glutamic acid, thiourea, L-histidine, glutathione, L-arginine, and glycine
-
?
additional information
?
-
-
no activity with L-glutamine, L-aspartic acid, L-glutamic acid, thiourea, L-histidine, glutathione, L-arginine, and glycine
-
?
additional information
?
-
enzyme exhibits strict substrate specificity towards L-asparagine, with trace activity towards L-glutamine
-
?
additional information
?
-
-
L-asparaginase from Escherichia coli is more immuno-depressive and immunotoxic than that from Erwinia carotovora
-
?
additional information
?
-
-
no glutaminase activity is observed
-
?
additional information
?
-
-
the hydrolysis efficiency of asparagine is at least 11925fold higher than that of L-glutamine
-
?
additional information
?
-
-
no substrate: D-asparagine, beta-alanine amide
-
?
additional information
?
-
-
poor substrates: D-asparagine, L-aspartic acid, and L-glutamic acid. No substrate: L-glutamine
-
?
additional information
?
-
poor or no substrates: D-asparagine, L-glutamine, D-glutamine, L-histidine, L-ornithine, Boc-L-asapragine, N-alpha-acetyl-L-asparagine, urea, acrylamide
-
?
additional information
?
-
-
poor or no substrates: D-asparagine, L-glutamine, D-glutamine, L-histidine, L-ornithine, Boc-L-asapragine, N-alpha-acetyl-L-asparagine, urea, acrylamide
-
?
additional information
?
-
increased substrate accessibility through the active site loop plays a major role in determining activity, dynamic flipping of a critical Tyr residue is responsible for the activity of thermophilic L-asparaginases, molecular dynamic simulation and reaction mechanism, overview
-
?
additional information
?
-
-
increased substrate accessibility through the active site loop plays a major role in determining activity, dynamic flipping of a critical Tyr residue is responsible for the activity of thermophilic L-asparaginases, molecular dynamic simulation and reaction mechanism, overview
-
?
additional information
?
-
-
the N-terminal domain of L-asparaginase functions as a non-specific, stable, molecular chaperone
-
?
additional information
?
-
enzyme shows negligible activity with both D-asparagine (22 U/mg) and L-glutamine (36 U/mg) as the substrates
-
?
additional information
?
-
the activity against L-glutamine, reaction of EC 3.5.1.2, corresponds to 2.2% of the activity against L-asparagine
-
?
additional information
?
-
-
the activity against L-glutamine, reaction of EC 3.5.1.2, corresponds to 2.2% of the activity against L-asparagine
-
?
additional information
?
-
-
very poor substrate: L-glutamine
-
?
additional information
?
-
-
less than 0.5% of the activity with L-asparagine: L-glutamine, D-asparagine, D-glutamine
-
?
additional information
?
-
-
less than 0.5% of the activity with L-asparagine: L-glutamine, D-asparagine, D-glutamine
-
?
additional information
?
-
-
antiproliferating activity on the breast cancer cell lines T47D, BT20, and MCF-7
-
?
additional information
?
-
-
no activity with D-asparagine as substrate
-
?
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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
D-asparagine + H2O
D-aspartate + NH3
-
less than 10% activity compared to L-asparagine
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
highly specific substrate
-
-
?
L-asparagine + H2O
L-aspartate + NH3
100% activity
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
substrate hydrolysis efficiency of L-asparagine is 8fold higher than that of L-glutamine
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
the enzyme does not reduce alpha-antiplasmin and plasminogen levels in human patients with acute lymphoblastic leukemia
-
-
?
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
-
-
?
L-asparagine + H2O
L-aspartate + NH3
strongly preferred substrate
-
-
?
L-asparagine + H2O
L-aspartate + NH3
strongly preferred substrate
-
-
?
L-asparagine + H2O
L-aspartate + NH3
highly specific substrate
-
-
?
L-asparagine + H2O
L-aspartate + NH3
highly specific substrate
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
-
?
L-asparagine + H2O
L-aspartate + NH3
highest specificity for L-asparagine
-
-
?
L-asparagine + H2O
L-aspartate + NH3
highest specificity for L-asparagine
-
-
?
L-asparagine + H2O
L-aspartate + NH3
best substrate
-
-
?
L-asparagine + H2O
L-aspartate + NH3
-
-
-
?
L-aspartic acid + NH3
?
less than 3% activity compared to L-asparagine
-
-
?
L-aspartic acid + NH3
?
less than 3% activity compared to L-asparagine
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
less than 1% activity compared to L-asparagine
-
-
?
L-glutamine + H2O
L-glutamate + NH3
less than 1% activity compared to L-asparagine
-
-
?
L-glutamine + H2O
L-glutamate + NH3
less than 1% activity compared to L-asparagine
-
-
?
additional information
?
-
-
the enzyme shows anti-leukemic activity
-
-
?
additional information
?
-
no activity with D-asparagine monohydrate and L-glutamic acid
-
-
?
additional information
?
-
-
no activity with D-asparagine monohydrate and L-glutamic acid
-
-
?
additional information
?
-
-
no activity with D-glutamine, L-aspartic acid, D-aspartic acid, L-glutamic acid, and ornathine
-
-
?
additional information
?
-
no activity with D-asparagine monohydrate and L-glutamic acid
-
-
?
additional information
?
-
-
no activity with D-asparagine monohydrate and L-glutamic acid
-
-
?
additional information
?
-
-
the enzyme requires autocleavage to become active
-
-
?
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
-
-
?
additional information
?
-
-
L-asparaginase is cytotoxic, resistance to L-asparaginase in TEL-AML1-negative but not TEL-AML1-positive pediatric acute lymphoblastic cells is due to increased cellular expression of asparagine synthase, overview
-
-
?
additional information
?
-
to become enzymatically active, ASNase3 must undergo autocleavage between residues Gly167 and Thr168
-
-
?
additional information
?
-
-
to become enzymatically active, ASNase3 must undergo autocleavage between residues Gly167 and Thr168
-
-
?
additional information
?
-
-
L-asparaginase from Escherichia coli is more immuno-depressive and immunotoxic than that from Erwinia carotovora
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Cu2+
Fe3+
K+
KCl
the catalytic activity of YpA does not vary significantly as a function of ionic strength at 100-3000 mM KCl
Mg2+
Mn2+
Na+
Ni2+
-
5 mM, 37°C, 136% relative activity compared to the activity in absence of metal cations
Rb+
monovalent cation preference in order of decreasing efficiency is: K+, Na+, Rb+
Zn2+
additional information
Co2+
-
5 mM, 37°C, 134% relative activity compared to the activity in absence of metal cations
K+
catalytic activity of At3g16150 is enhanced approximately tenfold in the presence of K+
K+
-
potassium-independent asparaginase ASPGA1, and potassium-dependent asparaginase ASPGB1
K+
-
potassium independent and dependent enzymes appear to be distinct proteins. The proportion of the two enzymes varies with plant species, organ and developmental age
Mg2+
marginal increase in enzyme activity in the presence of 1 mM Mg2+ (less than 15%)
Na+
monovalent cation preference in order of decreasing efficiency is: K+, Na+, Rb+
Na+
-
probably, metal binding loop structure involving Leu59, Glu60, Ile62, Phe65, Ala67, and Ile69, overview
Zn2+
1 mM, 109% of initial activity, 5 mM, 86% of initial activity
additional information
-
potassium-independent L-asparaginase (AtA), Arabidopsis thaliana potassium-dependent L-asparaginase (AtAK)
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Glutaraldehyde
-
inhibits the enzyme during immobilization at concentrations above 0.2%
N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinline
-
no effect up to 1 mM: Mg2+, Mn2+ and Ca2+
phenylmethylsulfonyl fluoride
-
more than 80% residual activity at 10 mM
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
-
5-Diazo-4-oxo-L-norvaline
-
inhibits L-asparaginase activity and affects broth culture filtrate inhibition of the cell cycle
Ba2+
-
5 mM, 37°C, 25% relative activity compared to the activity in absence of metal cations
D-Asn
-
competitive, reverses antiproliferating effect on breast cancer cells
Hg2+
-
5 mM, 37°C, 20% relative activity compared to the activity in absence of metal cations
iodoacetamide
-
at pH 6.0 protection by substrate, at pH 8.0 no protection by substrate
Mn2+
-
5 mM, 37°C, 42% relative activity compared to the activity in absence of metal cations