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Information on EC 6.3.5.4 - asparagine synthase (glutamine-hydrolysing)
for references in articles please use BRENDA:EC6.3.5.4
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EC Tree 6 Ligases
6.3 Forming carbon-nitrogen bonds
6.3.5 Carbon-nitrogen ligases with glutamine as amido-N-donor
6.3.5.4 asparagine synthase (glutamine-hydrolysing)
IUBMB Comments
The enzyme from Escherichia coli has two active sites that are connected by an intramolecular ammonia tunnel [5,6]. The enzyme catalyses three distinct chemical reactions: glutamine hydrolysis to yield ammonia takes place in the N-terminal domain. The C-terminal active site mediates both the synthesis of a β-aspartyl-AMP intermediate and its subsequent reaction with ammonia. The ammonia released is channeled to the other active site to yield asparagine .
The enzyme appears in viruses and cellular organisms
- 6.3.5.4
- leukemia
- lymphoblastic
- children
-
remission
- vincristine
- lymphoma
- methotrexate
- l-asparagine
- prednisone
- cyclophosphamide
- marrow
- erwinia
- daunorubicin
- doxorubicin
-
relapsed
- cr
- dexamethasone
-
consolidation
- thrombosis
-
l-aspartic
- chrysanthemi
- etoposide
-
pegylated
-
reinduction
- thromboembolism
- cytarabine
-
antileukemic
- glutaminase
-
intrathecal
-
prophylaxis
-
non-hodgkin
- ifosfamide
-
event-free
-
arabinoside
- antithrombin
- carotovora
- 6-mercaptopurine
-
extranodal
-
philadelphia
- agriculture
- lymphosarcoma
-
smile
- medicine
-
multiagent
-
myelosuppression
- hypofibrinogenemia
-
standard-risk
- pseudocysts
- nutrition
- teniposide
- drug development
- analysis
- daunomycin
- epipodophyllotoxins
- idarubicin
Reaction Schemes
showSynonyms
l-asparaginase, asnase, asparagine synthetase b, glutamine-dependent asparagine synthetase, pvas2, taasn2, osas1, taasn1, ste10, glutamine-dependent amidotransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AS
AS-A
AS-B
AS1
Asn
ASN1
ASN1-S
ASN1-T
Asn1p/Asn2p
ASN2
ASN3
ASN5-S
ASN5-T
AsnA
AsnB
ASNS
AsnS1
AsnS2
Asparagine synthetase
Asparagine synthetase (glutamine hydrolyzing)
-
-
-
-
Asparagine synthetase (glutamine)
-
-
-
-
Asparagine synthetase (glutamine-hydrolysing)
-
-
-
-
asparagine synthetase 2
Asparagine synthetase A
Asparagine synthetase B
At5g10240
bacterial type asparagine synthetase A
Glutamine-dependent asparagine synthetase
-
-
-
-
L-Asparagine synthetase
-
-
-
-
LDBPK_300470
LiAS-A
Synthetase, Asn (glutamine)
-
-
-
-
TS11 cell cycle control protein
-
-
-
-
additional information
AS-B
-
-
-
-
AsnB
-
-
-
-
Asparagine synthetase
-
-
Asparagine synthetase B
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate
uni-uni-bi-ter ping-pong mechanism without abortive complexes. Gln binds first, followed by Glu release, and Asp and ATP bind in order followed by ordered release of diphosphate, AMP and Asn. In the presence of 0.5-2.0 mM excess Mg2+ over ATP the binding of substrates after the release of Glu is in a rapid equilibrium system
-
ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate
NH4+ is bound to the enzyme followed by MgATP causing Asn release
-
ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate
Arg325 is involved in stabilization of a pentacovalent intermediate leading to the formation of beta-aspartyl-AMP
-
ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate
a model for the role of the catalytic triad in transferring nitrogen from Gln to Asp. An alternative catalytic mechanism is proposed, which obviates the participation of a histidine residue in the reaction
-
ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate
hybrid uni uni bi ter ping pong Theorell-Chance mechanism where the glutaminase reaction occurs first and Asp binds to the enzyme before ATP in the sequential segment. Diphosphate is the first product released in the Theorell-Chance reaction, which is followed by the ordered release of AMP and Asn
-
ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate
mechanism
-
ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate
overall ping-pong mechanism
-
-
-
ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate
ping-pong reaction mechanism. Glutamine is the first substrate to bind to the enzyme and Asn is the last product released
-
-
-
ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate
the enzyme forms a crucial beta-aspartyl-AMP-Mg2+ intermediate, which then undergoes a nucleophilic attack of ammonia, forming Asn and releasing AMP and diphosphate. Ammonia can be free or glutamine-derived
ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate
reaction mechanism, structure-function relationship
ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate
reaction mechanism, structure-function relationship
ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate
the enzyme forms a crucial beta-aspartyl-AMP-Mg2+ intermediate, which then undergoes a nucleophilic attack of ammonia, forming Asn and releasing AMP and diphosphate. Ammonia can be free or glutamine-derived
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acid amide hydrolysis
-
-
carboxylic
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
L-asparagine biosynthesis I
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SYSTEMATIC NAME
IUBMB Comments
L-aspartate:L-glutamine amido-ligase (AMP-forming)
The enzyme from Escherichia coli has two active sites [4] that are connected by an intramolecular ammonia tunnel [5,6]. The enzyme catalyses three distinct chemical reactions: glutamine hydrolysis to yield ammonia takes place in the N-terminal domain. The C-terminal active site mediates both the synthesis of a beta-aspartyl-AMP intermediate and its subsequent reaction with ammonia. The ammonia released is channeled to the other active site to yield asparagine [6].
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CAS REGISTRY NUMBER
COMMENTARY
37318-72-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + cysteine sulfinic acid
AMP + diphosphate + cysteine sulfinic acid
-
Substrates: -
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ATP + L-Asp + L-Gln + H2O
AMP + diphosphate + L-Asn + L-Glu
-
Substrates: -
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?
CTP + L-Asp + L-Gln
CMP + diphosphate + Asn + Glu
-
Substrates: weak activity
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?
dATP + L-Asp + L-Gln
dAMP + diphosphate + Asn + Glu
-
Substrates: utilized at a similar rate as ATP
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?
dATP + L-Asp + NH3
dAMP + diphosphate + Asn
-
Substrates: utilized at a similar rate as ATP
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?
L-Glutamic acid gamma-monohydroxamate + H2O
Hydroxylamine + Glu
-
Substrates: -
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?
UTP + L-Asp + L-Gln
UMP + diphosphate + Asn + Glu
-
Substrates: weak activity
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?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
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Substrates: -
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?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
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Substrates: -
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ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
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Substrates: -
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ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
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Substrates: -
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?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
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Substrates: -
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?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
-
Substrates: -
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?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
-
Substrates: -
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ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
-
Substrates: the basic region leucine zipper protein ATF5, a transcriptional activator, stimulates asparagine promoter/reporter gene transcription via the nutrient-sensing response unit
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?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
-
Substrates: resistance to L-asparaginase and relapse risk are associated with high expression of asparagine synthetase in TEL-AML1-negative but not in TEL-AML1-positive B-lineage acute lymphoblastic leukemia
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?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
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Substrates: -
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?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
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Substrates: -
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?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
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Substrates: -
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?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
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Substrates: -
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ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
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Substrates: -
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?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
-
Substrates: the ratio of Gln- to NH4+-dependent activity is 2.5
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?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
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Substrates: -
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ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
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Substrates: -
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ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
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Substrates: -
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?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
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Substrates: -
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ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
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Substrates: -
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?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
Substrates: -
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?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
-
Substrates: TaASN1 is dramatically induced by salinity, osmotic stress and exogenous abscisic acid
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?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
-
Substrates: TaASN2 transcripts are very low in all detected tissues and conditions and are only slightly induced by abscisic acid in roots
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?
ATP + L-Asp + L-Gln
AMP + diphosphate + L-Asn + L-Glu
-
Substrates: -
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?
ATP + L-Asp + L-Gln
AMP + diphosphate + L-Asn + L-Glu
-
Substrates: -
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?
ATP + L-Asp + L-Gln
AMP + diphosphate + L-Asn + L-Glu
-
Substrates: light, carbon and nitrogen availability control asparagine synthesis in sunflower by regulating three aspargine synthetase coding genes. HAS2 expression requires light and is positively affected by sucrose. HAS1 and HAS1.1 expression is dependent on nitrogen availability, while HAS2 transcripts are still found in N-starved plants. High ammonium level induces all three asparagine synthetase genes and partially reverts sucrose repression of HAS1 and HAS1.1
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ATP + L-Asp + L-Gln
AMP + diphosphate + L-Asn + L-Glu
Substrates: -
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?
ATP + L-Asp + NH2OH
AMP + diphosphate + beta-aspartylhydroxamate
-
Substrates: -
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?
ATP + L-Asp + NH2OH
AMP + diphosphate + beta-aspartylhydroxamate
-
Substrates: -
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?
ATP + L-Asp + NH2OH
AMP + diphosphate + beta-aspartylhydroxamate
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Substrates: -
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?
ATP + L-Asp + NH2OH
AMP + diphosphate + beta-aspartylhydroxamate
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Substrates: -
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?
ATP + L-Asp + NH2OH
AMP + diphosphate + beta-aspartylhydroxamate
-
Substrates: -
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?
ATP + L-Asp + NH3
AMP + diphosphate + Asn
-
Substrates: -
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?
ATP + L-Asp + NH3
AMP + diphosphate + Asn
-
Substrates: 30% of the activity relative to Gln
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?
ATP + L-Asp + NH3
AMP + diphosphate + Asn
-
Substrates: the ratio of Gln-dependent to NH4+-dependent activity is 2.5
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?
ATP + L-Asp + NH3
AMP + diphosphate + Asn
-
Substrates: 85% of the activity relative to Gln
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?
ATP + L-Asp + NH3
AMP + diphosphate + Asn
-
Substrates: -
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?
ATP + L-Asp + NH3
AMP + diphosphate + L-Asn
Substrates: -
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?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
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?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
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?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: ATP-dependent, mechanism including an enzyme-ATP-Asp-Gln quarternary complex, AS-B structure, two active sites
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ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
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?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
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?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
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?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: glutamine is the in vivo nitrogen source
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ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: ATP-dependent, the amine group of Gln is transferred directly to Asp
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?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: transfers the amide group of Gln to Asp
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?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
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?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
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?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
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?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: ATP-dependent, the amine group of Gln is transferred directly to Asp
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ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: ATP-dependent, the amine group of Gln is transferred directly to Asp, maximum activity with 1 mM Gln and 3-10 mM ATP in the assay
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?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
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?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
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?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
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ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: the enzyme might play a functional role in nitrogen translocation from root to aerial organs in Phaseolus vulgaris
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ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
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?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: the reaction sequence begins with the ordered addition of ATP and aspartate. Diphosphate is released, followed by the addition of ammonia and the release of asparagine and AMP. Glutamine is simultaneously hydrolyzed at a second site and the ammonia intermediate diffuses through an interdomain protein tunnel from the site of production to the site of utilization. The data are also consistent with the dead-end binding of asparagine to the glutamine binding site and diphosphate with free enzyme. The rate of hydrolysis of glutamine is largely independent of the activation of aspartate and thus the reaction rates at the two active sites are essentially uncoupled from one another
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ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
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?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
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?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
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?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
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?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
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ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: ATP in form of MgATP2-
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?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
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?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
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?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
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ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
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ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
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ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
E9BLE1
Substrates: -
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ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
E9BLE1
Substrates: -
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ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
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ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
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ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
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ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
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ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
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?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
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ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
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ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
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ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
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ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
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ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
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ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
Substrates: -
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ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
-
Substrates: asparagine biosynthesis proceeds by initial reaction of aspartate and ATP to yield a beta-aspartyl-AMP intermediate, in the presence of glutamine, ammonia released in the N-terminal active site reacts with beta-aspartyl-AMP to yield asparagine and AMP
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ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
Substrates: -
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ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
Substrates: -
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ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
E9BLE1
Substrates: also reaction of EC 6.3.1.1
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ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
E9BLE1
Substrates: also reaction of EC 6.3.1.1
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ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
Substrates: -
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ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
-
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
-
Substrates: -
Products: -
Products: -
?
GTP + L-Asp + L-Gln
GMP + diphosphate + Asn + Glu
-
Substrates: 15% of the activity relative to ATP
Products: -
Products: -
?
GTP + L-Asp + L-Gln
GMP + diphosphate + Asn + Glu
-
Substrates: 5.6% of the activity relative to ATP
Products: -
Products: -
?
L-glutamine + H2O
L-glutamate + NH3
E9BLE1
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological roles for asnB in vegetative cells and for asnO in sporulating cells, asnB may be the main gene involved in asparagine biosynthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological roles for asnB in vegetative cells and for asnO in sporulating cells, asnB may be the main gene involved in asparagine biosynthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: comprehensive mechanism has been proposed through which either Gln or NH3 can provide nitrogen for Asn production from Asp
Products: -
Products: -
?
additional information
?
-
-
Substrates: the N74D As-B mutant exhibits very low glutaminase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with ITP or XTP
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is extremly selective, being able to discriminate between metabolites that have similar structures to Asp
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme has inherent glutaminase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: major biosynthetic pathway for asparagine, AS gene expression is down-regulated by light
Products: -
Products: -
?
additional information
?
-
-
Substrates: primary enzyme responsible for asparagine synthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: Helianthus annuus contains three asparagine synthetase genes: HAS1, HAS1.1 and HAS2. Most of the asparagine newly synthesized for germination and cotyledon expansion is due to HAS2 activity, with little contribution of the other asparagine synthetase genes. All three genes work together to synthesize asparagine for leaf senescence
Products: -
Products: -
?
additional information
?
-
Substrates: Helianthus annuus contains three asparagine synthetase genes: HAS1, HAS1.1 and HAS2. Most of the asparagine newly synthesized for germination and cotyledon expansion is due to HAS2 activity, with little contribution of the other asparagine synthetase genes. All three genes work together to synthesize asparagine for leaf senescence
Products: -
Products: -
?
additional information
?
-
Substrates: Helianthus annuus contains three asparagine synthetase genes: HAS1, HAS1.1 and HAS2. Most of the asparagine newly synthesized for germination and cotyledon expansion is due to HAS2 activity, with little contribution of the other asparagine synthetase genes. All three genes work together to synthesize asparagine for leaf senescence
Products: -
Products: -
?
additional information
?
-
Substrates: Helianthus annuus contains three asparagine synthetase genes: HAS1, HAS1.1 and HAS2. Most of the asparagine newly synthesized for germination and cotyledon expansion is due to HAS2 activity, with little contribution of the other asparagine synthetase genes. All three genes work together to synthesize asparagine for leaf senescence
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme has inherent glutaminase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: upregulation of asparagine synthetase fails to avert cell cycle arrest induced by L-asparaginase in TEL/AML1-positive leukaemic cells
Products: -
Products: -
?
additional information
?
-
Substrates: under normal growth conditions HvAS1 gene seems to be important in roots where nitrogen is assimilated into asparagine for long-distance transport within the plant
Products: -
Products: -
?
additional information
?
-
Substrates: under normal growth conditions HvAS1 gene seems to be important in roots where nitrogen is assimilated into asparagine for long-distance transport within the plant
Products: -
Products: -
?
additional information
?
-
-
Substrates: under normal growth conditions HvAS1 gene seems to be important in roots where nitrogen is assimilated into asparagine for long-distance transport within the plant
Products: -
Products: -
?
additional information
?
-
Substrates: under normal growth conditions HvAS2 acts as a housekeeping gene in the leaves
Products: -
Products: -
?
additional information
?
-
Substrates: under normal growth conditions HvAS2 acts as a housekeeping gene in the leaves
Products: -
Products: -
?
additional information
?
-
-
Substrates: under normal growth conditions HvAS2 acts as a housekeeping gene in the leaves
Products: -
Products: -
?
additional information
?
-
-
Substrates: Gln-dependent enzyme is essential for Asn synthesis when the nitrogen source is growth rate limiting
Products: -
Products: -
?
additional information
?
-
-
Substrates: primary enzyme responsible for asparagine synthesis
Products: -
Products: -
?
additional information
?
-
E9BLE1
Substrates: asparagine is formed in two steps: the beta-carboxylate group of aspartate is first activated by ATP to form an aminoacyl-AMP before its amidation by a nucleophilic attack with an ammonium ion. LdASNA is active and preferentially utilizes ammonia, although it is also capable of utilizing glutamine as a nitrogen source
Products: -
Products: -
?
additional information
?
-
-
Substrates: asparagine is formed in two steps: the beta-carboxylate group of aspartate is first activated by ATP to form an aminoacyl-AMP before its amidation by a nucleophilic attack with an ammonium ion. LdASNA is active and preferentially utilizes ammonia, although it is also capable of utilizing glutamine as a nitrogen source
Products: -
Products: -
?
additional information
?
-
E9BLE1
Substrates: asparagine is formed in two steps: the beta-carboxylate group of aspartate is first activated by ATP to form an aminoacyl-AMP before its amidation by a nucleophilic attack with an ammonium ion. LdASNA is active and preferentially utilizes ammonia, although it is also capable of utilizing glutamine as a nitrogen source
Products: -
Products: -
?
additional information
?
-
-
Substrates: the primary site of Asn synthesis is the root and subsequently the leaves receive Asn as the principal N-source for amino acid and protein synthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: primary enzyme responsible for asparagine synthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is involved in ammonia assimilation
Products: -
Products: -
?
additional information
?
-
-
Substrates: ATP-diphosphate exchange reaction
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme has inherent glutaminase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: Asn, the end product of the mass action of symbiotic NH4+ synthesis, is the principal N-transport-compound of many temperate legumes
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme has inherent glutaminase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme has inherent glutaminase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: glutamine or glutamine-derived metabolites regulate AS expression in roots
Products: -
Products: -
?
additional information
?
-
-
Substrates: nitrogen metabolism, asparagine synthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: role for hexokinase in the sugar-sensing mechanism that regulates PvNAS2 expression in roots, downregulation of the asparagine synthetase enzyme and concomitantly asparagine production. Thereby a favourable environment is created for the efficient transfer of the amido group of glutamine for the synthesis of purines, and then ureide generation.
Products: -
Products: -
?
additional information
?
-
Substrates: role for hexokinase in the sugar-sensing mechanism that regulates PvNAS2 expression in roots, downregulation of the asparagine synthetase enzyme and concomitantly asparagine production. Thereby a favourable environment is created for the efficient transfer of the amido group of glutamine for the synthesis of purines, and then ureide generation.
Products: -
Products: -
?
additional information
?
-
-
Substrates: ATP-diphosphate exchange reaction
Products: -
Products: -
?
additional information
?
-
-
Substrates: the synthesis of Asn in mammalian tissues proceeds through the intermediate beta-aspartyladenylate
Products: -
Products: -
?
additional information
?
-
-
Substrates: importance of asparagine synthetase in cell proliferation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme continues to produce glutamate even when the synthesis of asparagine has ceased due to a lack of aspartate
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme continues to produce glutamate even when the synthesis of asparagine has ceased due to a lack of aspartate
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme continues to produce glutamate even when the synthesis of asparagine has ceased due to a lack of aspartate
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme continues to produce glutamate even when the synthesis of asparagine has ceased due to a lack of aspartate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-Asp + L-Gln
AMP + diphosphate + L-Asn + L-Glu
-
Substrates: light, carbon and nitrogen availability control asparagine synthesis in sunflower by regulating three aspargine synthetase coding genes. HAS2 expression requires light and is positively affected by sucrose. HAS1 and HAS1.1 expression is dependent on nitrogen availability, while HAS2 transcripts are still found in N-starved plants. High ammonium level induces all three asparagine synthetase genes and partially reverts sucrose repression of HAS1 and HAS1.1
Products: -
Products: -
?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
-
Substrates: the basic region leucine zipper protein ATF5, a transcriptional activator, stimulates asparagine promoter/reporter gene transcription via the nutrient-sensing response unit
Products: -
Products: -
?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
-
Substrates: TaASN1 is dramatically induced by salinity, osmotic stress and exogenous abscisic acid
Products: -
Products: -
?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
-
Substrates: TaASN2 transcripts are very low in all detected tissues and conditions and are only slightly induced by abscisic acid in roots
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: glutamine is the in vivo nitrogen source
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: the enzyme might play a functional role in nitrogen translocation from root to aerial organs in Phaseolus vulgaris
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
E9BLE1
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
E9BLE1
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
-
Substrates: asparagine biosynthesis proceeds by initial reaction of aspartate and ATP to yield a beta-aspartyl-AMP intermediate, in the presence of glutamine, ammonia released in the N-terminal active site reacts with beta-aspartyl-AMP to yield asparagine and AMP
Products: -
Products: -
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
E9BLE1
Substrates: also reaction of EC 6.3.1.1
Products: -
Products: -
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
E9BLE1
Substrates: also reaction of EC 6.3.1.1
Products: -
Products: -
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
Substrates: -
Products: -
Products: -
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
-
Substrates: -
Products: -
Products: -
?
L-glutamine + H2O
L-glutamate + NH3
E9BLE1
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological roles for asnB in vegetative cells and for asnO in sporulating cells, asnB may be the main gene involved in asparagine biosynthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological roles for asnB in vegetative cells and for asnO in sporulating cells, asnB may be the main gene involved in asparagine biosynthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: comprehensive mechanism has been proposed through which either Gln or NH3 can provide nitrogen for Asn production from Asp
Products: -
Products: -
?
additional information
?
-
-
Substrates: major biosynthetic pathway for asparagine, AS gene expression is down-regulated by light
Products: -
Products: -
?
additional information
?
-
-
Substrates: primary enzyme responsible for asparagine synthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: Helianthus annuus contains three asparagine synthetase genes: HAS1, HAS1.1 and HAS2. Most of the asparagine newly synthesized for germination and cotyledon expansion is due to HAS2 activity, with little contribution of the other asparagine synthetase genes. All three genes work together to synthesize asparagine for leaf senescence
Products: -
Products: -
?
additional information
?
-
Substrates: Helianthus annuus contains three asparagine synthetase genes: HAS1, HAS1.1 and HAS2. Most of the asparagine newly synthesized for germination and cotyledon expansion is due to HAS2 activity, with little contribution of the other asparagine synthetase genes. All three genes work together to synthesize asparagine for leaf senescence
Products: -
Products: -
?
additional information
?
-
Substrates: Helianthus annuus contains three asparagine synthetase genes: HAS1, HAS1.1 and HAS2. Most of the asparagine newly synthesized for germination and cotyledon expansion is due to HAS2 activity, with little contribution of the other asparagine synthetase genes. All three genes work together to synthesize asparagine for leaf senescence
Products: -
Products: -
?
additional information
?
-
Substrates: Helianthus annuus contains three asparagine synthetase genes: HAS1, HAS1.1 and HAS2. Most of the asparagine newly synthesized for germination and cotyledon expansion is due to HAS2 activity, with little contribution of the other asparagine synthetase genes. All three genes work together to synthesize asparagine for leaf senescence
Products: -
Products: -
?
additional information
?
-
-
Substrates: upregulation of asparagine synthetase fails to avert cell cycle arrest induced by L-asparaginase in TEL/AML1-positive leukaemic cells
Products: -
Products: -
?
additional information
?
-
Substrates: under normal growth conditions HvAS1 gene seems to be important in roots where nitrogen is assimilated into asparagine for long-distance transport within the plant
Products: -
Products: -
?
additional information
?
-
Substrates: under normal growth conditions HvAS1 gene seems to be important in roots where nitrogen is assimilated into asparagine for long-distance transport within the plant
Products: -
Products: -
?
additional information
?
-
-
Substrates: under normal growth conditions HvAS1 gene seems to be important in roots where nitrogen is assimilated into asparagine for long-distance transport within the plant
Products: -
Products: -
?
additional information
?
-
Substrates: under normal growth conditions HvAS2 acts as a housekeeping gene in the leaves
Products: -
Products: -
?
additional information
?
-
Substrates: under normal growth conditions HvAS2 acts as a housekeeping gene in the leaves
Products: -
Products: -
?
additional information
?
-
-
Substrates: under normal growth conditions HvAS2 acts as a housekeeping gene in the leaves
Products: -
Products: -
?
additional information
?
-
-
Substrates: Gln-dependent enzyme is essential for Asn synthesis when the nitrogen source is growth rate limiting
Products: -
Products: -
?
additional information
?
-
-
Substrates: primary enzyme responsible for asparagine synthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: the primary site of Asn synthesis is the root and subsequently the leaves receive Asn as the principal N-source for amino acid and protein synthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: primary enzyme responsible for asparagine synthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is involved in ammonia assimilation
Products: -
Products: -
?
additional information
?
-
-
Substrates: Asn, the end product of the mass action of symbiotic NH4+ synthesis, is the principal N-transport-compound of many temperate legumes
Products: -
Products: -
?
additional information
?
-
-
Substrates: glutamine or glutamine-derived metabolites regulate AS expression in roots
Products: -
Products: -
?
additional information
?
-
-
Substrates: nitrogen metabolism, asparagine synthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: role for hexokinase in the sugar-sensing mechanism that regulates PvNAS2 expression in roots, downregulation of the asparagine synthetase enzyme and concomitantly asparagine production. Thereby a favourable environment is created for the efficient transfer of the amido group of glutamine for the synthesis of purines, and then ureide generation.
Products: -
Products: -
?
additional information
?
-
Substrates: role for hexokinase in the sugar-sensing mechanism that regulates PvNAS2 expression in roots, downregulation of the asparagine synthetase enzyme and concomitantly asparagine production. Thereby a favourable environment is created for the efficient transfer of the amido group of glutamine for the synthesis of purines, and then ureide generation.
Products: -
Products: -
?
additional information
?
-
-
Substrates: importance of asparagine synthetase in cell proliferation
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
Br-
Cl-
Co2+
I-
Mg2+
Mn2+
Ni2+
Br-
-
strong activation of Asn synthesis and Gln hydrolysis. The synthetase reactions with NH3 or NH2OH are only slightly stimulated
Cl-
-
stimulation of the Gln-dependent reaction and glutaminase reaction. Inhibition of the NH4+-dependent reaction, competitive with respect to NH4+, with negative cooperativity
Cl-
-
strong activation of Asn synthesis and Gln hydrolysis, competitive activator with respect to Gln and a noncompetitive activator with respect to MgATP2- and Asp. Cl- changes the substrate saturation kinetics of Gln from negatively cooperative to normal hyperbolic and causes a 50fold increase in the affinity for Gln. Inherent glutaminase activity is enhanced 30fold. The synthetase reactions with NH4+ or NH2OH are only slightly stimulated
Cl-
-
required for glutaminase and glutamine-dependent synthetase activity, not for the NH4+-dependent activity
Co2+
-
is the only divalent metal ion that can replace Mg2+ with 80% of the Mg2+-dependent AS-B activity activity with Gln and 52% of the Mg2+-dependent AS-B activity with NH4+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-methyl-4-(1-methylethyl)-7-oxabicyclo[2.2.1]heptane
-
trivial name 1,4-cineole, almost complete inhibition above 1 mM
8-N3ATP
-
loss of NH4+-dependent Asn synthesis, but no effect on the glutaminase activity
adenylated sulfoximine
-
0.005 mM, 65% inhibition, dead-end complex with AS-B
AMP-PNP
-
competitive vs. ATP, noncompetitive vs. aspartate, uncompetitive vs. glutamine
Cl-
-
inhibition of the ammonia-dependent reaction, competitive with respect to ammonia, with negative cooperativity. Stimulation of the Gln-dependent and glutaminase reaction
L-(alphaS,5S)-alpha-Amino-3-chloro-4,5-dihydroisoxazol-5-ylacetic acid
-
i.e. NSC-163501
L-2-amino-4-oxo-5-(5'-adenosyl)phosphonopentanoic acid
-
noncompetitive with respect to Gln and uncompetitive with respect to both ATP and Asp
L-glutamic acid gamma-methylester
-
uncompetitive vs. ATP, competitive vs. glutamine
5'-O-[p-(fluorosulfonyl)benzoyl]adenosine
-
Cys523 is the key residue involved in the formation of the 5'-O-[p-(fluorosulfonyl)benzoyl]adenosine-induced disulfide bond, inactivation can be reversed by addition of dithiothreitol
6-diazo-5-oxo-L-norleucine
-
loss of Gln-dependent reactions, but no effect on ATP binding as measured during amminoa-dependent Asn synthesis
beta-methylaspartate
-
noncompetitive vs. ATP, competitive vs. aspartate, noncompetitive vs. glutamine
Gln
-
inhibitor of the NH4+-dependent reaction catalyzed by both the C1A and C1S mutants of AS-B
additional information
L-asparagine has no significant impact on the ammonia-dependent synthetase activity at 1 mM
-
additional information
-
L-asparagine has no significant impact on the ammonia-dependent synthetase activity at 1 mM
-
additional information
-
mouse pancreas contains a proteolytic inhibitor of L-Asn synthetase
-
additional information
-
methionine sulfoximine completely inhibits the NH4+-induced accumulation of AS protein, but not the glutamine-induced accumulation
-
additional information
-
PvNAS2 is downregulated when carbon availability is reduced in nodules
-
additional information
PvNAS2 is downregulated when carbon availability is reduced in nodules
-
additional information
-
enzyme from fetal liver extracts is significantly inhibited when combined with adult liver or tumor extracts
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
1 mM aminooxyacetic acid increases AS activity in crude extract by inhibiting various aminotransferases and preventing the assimilation of aspartate into the TCA cycle
-
additional information
-
AS expression in roots is induced by NH4+ or glutamine, but not by nitrate, glutamate, aspartate and asparagine
-
additional information
-
addition of sugars to the plants, mainly glucose, induces the enzymes leading to the increased asparagine production
-
additional information
addition of sugars to the plants, mainly glucose, induces the enzymes leading to the increased asparagine production
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.38
aspartic acid
-
pH 8, reaction with glutamine, C-terminally tagged recombinant enzyme
1.3
L-aspartic acid
-
pH 8, reaction with NH3, C-terminally tagged recombinant enzyme
0.013
ATP
-
mutant E348D, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37°C
0.03
ATP
-
mutant E348D, synthetase activity, ammonia-dependent activity, 100 mM NH4Cl, pH 8.0, 37°C
0.08
ATP
-
pH 8, reaction with glutamine, C-terminally tagged recombinant enzyme
0.097
ATP
pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn3
0.1
ATP
-
wild-type, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37°C
0.1 - 1
ATP
pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn1
0.11
ATP
-
wild-type, synthetase activity, ammonia-dependent activity, 100 mM NH4Cl, pH 8.0, 37°C
0.125
ATP
pH 7.6, temperature not specified in the publication, recombinant nontagged isozyme soluble ZmAsn2
0.128
ATP
pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn2
0.128
ATP
pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn4
0.13
L-Asp
-
mutant E348D, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37°C
0.23
L-Asp
-
mutant E348D, synthetase activity, ammonia-dependent activity, 100 mM NH4Cl, pH 8.0, 37°C
0.58
L-Asp
-
wild-type, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37°C
1.2
L-Asp
-
wild-type, synthetase activity, ammonia-dependent activity, 100 mM NH4Cl, pH 8.0, 37°C
0.1 - 2
L-aspartate
pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn3
0.9 - 1
L-aspartate
pH 7.6, temperature not specified in the publication, recombinant nontagged soluble isozyme ZmAsn2
0.93
L-aspartate
pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn4
0.98
L-aspartate
pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn1
0.98
L-aspartate
pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn2
1.1
L-Gln
-
mutant E348D, glutaminase activity, pH 8.0, 37°C, 5 mM ATP present
3.5
L-Gln
-
mutant E348A, glutaminase activity, pH 8.0, 37°C, 5 mM ATP present
3.9
L-Gln
-
mutant E348Q, glutaminase activity, pH 8.0, 37°C, 5 mM ATP present
0.26
L-glutamic acid gamma-monohydroxamate
-
ATP, wild-type enzyme, Gln-dependent activity
0.09
L-glutamine
pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn2
0.1 - 1
L-glutamine
pH 7.6, temperature not specified in the publication, recombinant nontagged soluble isozyme ZmAsn2
0.233
L-glutamine
pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn4
0.423
L-glutamine
pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn3
0.543
L-glutamine
pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn1
additional information
additional information
-
biphasic kinetic, linear portion near 0.5
-
additional information
additional information
-
Km-values of a number of site-specific mutant enzymes
-
additional information
additional information
-
regulation: coregulation by light of the activities of three crucial enzymes of NH4+ assimilation and transport
-
additional information
additional information
-
Km-values of mutant enzymes R30A, R30K, N74A, N74Q, and N79A
-
additional information
additional information
-
kinetic mechanism, kinetic model
-
additional information
additional information
the AsnS isozymes are kinetically distinct with substantial differences in Km (Gln) and Vmax values, overview. None of the enzymes has cooperative enzyme kinetics
-
additional information
additional information
the AsnS isozymes are kinetically distinct with substantial differences in Km (Gln) and Vmax values, overview. None of the enzymes has cooperative enzyme kinetics
-
additional information
additional information
the AsnS isozymes are kinetically distinct with substantial differences in Km (Gln) and Vmax values, overview. None of the enzymes has cooperative enzyme kinetics
-
additional information
additional information
the AsnS isozymes are kinetically distinct with substantial differences in Km (Gln) and Vmax values, overview. None of the enzymes has cooperative enzyme kinetics
-
additional information
additional information
steady-state kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.43
ATP
-
mutant E348D, synthetase activity, ammonia-dependent activity, 100 mM NH4Cl, pH 8.0, 37°C
0.51
ATP
-
mutant E348D, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37°C
0.9
ATP
-
wild-type, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37°C
0.96
ATP
-
wild-type, synthetase activity, ammonia-dependent activity, 100 mM NH4Cl, pH 8.0, 37°C
0.3
L-Asp
-
mutant E348D, synthetase activity, ammonia-dependent activity, 100 mM NH4Cl, pH 8.0, 37°C
0.45
L-Asp
-
mutant E348D, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37°C
0.67
L-Asp
-
wild-type, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37°C
0.75
L-Asp
-
wild-type, synthetase activity, ammonia-dependent activity, 100 mM NH4Cl, pH 8.0, 37°C
1.3
L-aspartic acid
-
pH 8, reaction with glutamine, C-terminally tagged recombinant enzyme
1.7
L-aspartic acid
-
pH 8, reaction with NH3, C-terminally tagged recombinant enzyme
4.45
L-Gln
-
mutant E348Q, glutaminase activity, pH 8.0, 37°C, 5 mM ATP present
5.8
L-Gln
-
mutant E348A, glutaminase activity, pH 8.0, 37°C, 5 mM ATP present
10.02
L-Gln
-
mutant E348D, glutaminase activity, pH 8.0, 37°C, 5 mM ATP present
additional information
additional information
-
turnover-numbers of mutant enzymes R30A, R30K, N74A, N74Q, and N79A
-
additional information
additional information
-
turnover-numbers of a number of site-specific AS-B mutant enzymes
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8.7
ATP
-
wild-type, synthetase activity, ammonia-dependent activity, 100 mM NH4Cl, pH 8.0, 37°C
9
ATP
-
wild-type, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37°C
14.3
ATP
-
mutant E348D, synthetase activity, ammonia-dependent activity, 100 mM NH4Cl, pH 8.0, 37°C
39.2
ATP
-
mutant E348D, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37°C
0.63
L-Asp
-
wild-type, synthetase activity, ammonia-dependent activity, 100 mM NH4Cl, pH 8.0, 37°C
1.2
L-Asp
-
wild-type, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37°C
1.3
L-Asp
-
mutant E348D, synthetase activity, ammonia-dependent activity, 100 mM NH4Cl, pH 8.0, 37°C
3.45
L-Asp
-
mutant E348D, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37°C
1.14
L-Gln
-
mutant E348Q, glutaminase activity, pH 8.0, 37°C, 5 mM ATP present
1.66
L-Gln
-
mutant E348A, glutaminase activity, pH 8.0, 37°C, 5 mM ATP present
3.88
L-Gln
-
wild-type, glutaminase activity, pH 8.0, 37°C, 5 mM ATP present
9.1
L-Gln
-
mutant E348D, glutaminase activity, pH 8.0, 37°C, 5 mM ATP present
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.25
L-asparagine
pH 7.6, temperature not specified in the publication, recombinant nontagged soluble isozyme ZmAsn2
0.3
L-glutamate
pH 7.6, temperature not specified in the publication, recombinant nontagged soluble isozyme ZmAsn2
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.1
L-asparagine
Zea mays
pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn1
1.3
L-asparagine
Zea mays
pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAs4
1.4
L-asparagine
Zea mays
pH 7.6, temperature not specified in the publication, recombinant nontagged soluble isozyme ZmAsn2
1.5
L-asparagine
Zea mays
pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn3
1.2
L-glutamate
Zea mays
pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn4
1.3
L-glutamate
Zea mays
pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn1
1.3
L-glutamate
Zea mays
pH 7.6, temperature not specified in the publication, recombinant nontagged soluble isozyme ZmAsn2
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0696
E9BLE1
purified recombinant enzyme, pH 7.8, 37°C, substrate L-asparate
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
-
pH 7.0: about 45% of maximal activity, pH 9.0: about 90% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
three glutamine-dependent AsnB-type asparagine snythetase genes: asnB, asnH and asnO, formerly yisO
-
-
brenda
three glutamine-dependent AsnB-type asparagine snythetase genes: asnB, asnH and asnO, formerly yisO
-
-
brenda
cv. Golden Promise
UniProt
brenda
the organism contains both enzymes EC 6.3.1.1. and EC 6.3.4.5. The gene asnA codes for NH4+-dependent Asn synthetases, EC 6.3.1.1, and the gene asnB codes for Gln-dependent Asn synthetase, EC 6.3.5.4
-
-
brenda
Populus simonii x P. nigra
UniProt
brenda
wild-type and mutant enzymes C1A, C1S, H29A , H80A, D33N, D33E, and A104H
-
-
brenda
wild-type and mutant enzymes C99A, C168A, C386A, C423A, C436A, C514A, C523A
-
-
brenda
wild-type and mutant enzymes, E317A, E317Q, T318A, Y319A, Y319F, D320A, V321A, T322A, T322S, T322V, T322Y, T323A, T323I, T323L, T323S, T323V, R325A, R325K, T328S
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
the cell line expresses a Caenorhabditis elegans SID-1 (CeSID-1) transmembrane protein with the ability to uptake double-stranded RNA into the cells
brenda
-
high content of AS in grains in the middle stage of ripening, in vascular tissues
brenda
giant cell lung-cancer cell lines 95C and 95D
brenda
-
high expression in T-lineage and low expression in B-lineage
brenda
-
higher expression than in lymphoblastic leukemia cells
brenda
the enzyme is higher in lung-cancer tissues than normal lung tissue. The enzyme is insignificantly correlated with the age, gender, treatment, histopathological grade among lung-cancer patients but significantly correlated with the lymph node metastasis
brenda
-
during the ripening of the spikelets AS contents increases during the first 21 days after flowering, then declines rapidly
brenda
additional information
-
TaASN1 is dramatically induced by salinity, osmotic stress and exogenous abscisic acid
brenda
expression of HvAS1, higher mRNA levels in younger leaves than in older leaves, induced by dark treatment, induction seems to require a dramatic change in the C/N ratio since no diurnal variation is observed and up-regulation of transcription only occurs after 10 h of darkness
brenda
-
ASN3-S and ASN3-T are maintained at very low expression levels after harvest and during air curing. ASN1-S, ASN1-T, and ASN5-T are already expressed at harvest, and their levels of expression increase significantly during curing (3200-fold induction of ASN1-S, 4100-fold induction of ASN1-T, and 4400-fold induction of ASN5-T after 4 days of curing, relative to the levels at the start of curing). ASN5-S exhibits the same expression pattern, but with a lower magnitude (530-fold induction relative to the level at the start of curing). ASN1-S and ASN5-S are induced rapidly at the onset of curing in detached leaves while being expressed only after 24 h of curing in attached leaves
brenda
-
high content of AS in leaf sheath at the second position from the fully expanded top leaf, the contents gradually decreases in leaf sheaths as a function of increasing age, in vascular tissues
brenda
OsAS2 mRNA is abundant in leaf blades and sheathes of rice
brenda
PnAS1 gene expression is particularly high in leaves
brenda
PnAS2 is highly expressed in L1 leaves and in roots
brenda
-
upregulation in leaves infected by the bacterial pathogen Pseudomonas syringae, high activity in phloem cells of the main vascular bundles and in secondary veins of the leaf blade
brenda
higher in lung-cancer tissues than in normal lung tissue. Higher asparagine synthetase is correlated with lung-cancer metastasis
brenda
-
much lower expression levels than in shoots of etiolated plants, light treatment decreases expression levels
brenda
expression of isoforms SAS1, SAS2 after cultivation on nitrate. Expression of the genes is reduced to very low levels within days after submitting the plants to a N-free medium. The subsequent return to a complete medium, containing nitrate restores expression of all three genes. High and low expression of genes in the roots are associated with high and low ratios of Asn/Asp transported to the shoot through xylem
brenda
expression after cultivation on nitrate. Expression of the gene is reduced to very low levels within days after submitting the plants to a N-free medium. The subsequent return to a complete medium, containing nitrate restores expression of all three genes. High and low expression of genes in the roots are associated with high and low ratios of Asn/Asp transported to the shoot through xylem
brenda
root surface cell-specific expression of OsAS1 gene. OsAS1 is mainly expressed in the roots, with in situ hybridization showing that the corresponding mRNA is specifically accumulated in the three cell layers of the root surface (epidermis, exodermis and sclerenchyma) in an NH4+-dependent manner
brenda
OsAS2 mRNA is detectable in the roots, its content decreases when NH+4 is supplied
brenda
expression of PvNAS2 in roots is confined to vascular bundles and meristematic tissues, while in root nodules its expression is solely localized to vascular traces and outer cortical cells encompassing the central nitrogen-fixing zone, but never detected in either infected or non-infected cells located in the central region of the nodule
brenda
high expression, confined to vascular bundles and meristematic tissues
brenda
PnAS2 is highly expressed in L1 leaves and in roots
brenda
expression of PnAS3 is low in all tissues except roots
brenda
-
TaASN1 is dramatically induced by salinity, osmotic stress and exogenous abscisic acid
brenda
expression of isoforms SAS1, SAS2 in absence of nitrate
brenda
-
detection in early stages of nodule development, no detection in nodules that have become competent for nitrogen fixation
brenda
expression of PvNAS2 in roots is confined to vascular bundles and meristematic tissues, while in root nodules its expression is solely localized to vascular traces and outer cortical cells encompassing the central nitrogen-fixing zone, but never detected in either infected or non-infected cells located in the central region of the nodule
brenda
mainly induced during the early days of nitrogen fixation, confined to vascular traces and outer cortical cells. Down-regulation when carbon availability is reduced, while the addition of sugars to the plants induces expression
brenda
-
TaASN1 is dramatically induced by salinity, osmotic stress and exogenous abscisic acid
brenda
-
the gene for AS is predominantly expressed in shoots as compared to roots of etiolated plants, light treatment decreases expression levels
brenda
-
TaASN1 is dramatically induced by salinity, osmotic stress and exogenous abscisic acid
brenda
fourth siliques numbered from the top of 35-day-old plants
brenda
-
fourth siliques numbered from the top of 35-day-old plants
-
brenda
-
young, TaASN1 is dramatically induced by salinity, osmotic stress and exogenous abscisic acid
brenda
additional information
-
the three asparagine synthetase genes asnB, asnH and asnO are differentially expressed during cell growth, expression pattern
brenda
additional information
-
the three asparagine synthetase genes asnB, asnH and asnO are differentially expressed during cell growth, expression pattern
-
brenda
additional information
analysis of mRNA expression in 19 ovarian cancer cell lines
brenda
additional information
-
analysis of mRNA expression in 19 ovarian cancer cell lines
brenda
additional information
-
the enzyme is ubiquitous in its organ distribution in mammals, but basal expression is relatively low in tissues other than the exocrine pancreas
brenda
additional information
-
ASNS expression is not detected in normal brain tissue, and the expression is marginal in low-grade pilocytic astrocytoma and diffuse astrocytoma
brenda
additional information
expression pattern, dark treatment of plants increases expression of HvAS1
brenda
additional information
expression pattern, dark treatment of plants increases expression of HvAS1
brenda
additional information
-
expression pattern, dark treatment of plants increases expression of HvAS1
brenda
additional information
expression pattern, no expression of HvAS2 in roots
brenda
additional information
expression pattern, no expression of HvAS2 in roots
brenda
additional information
-
expression pattern, no expression of HvAS2 in roots
brenda
additional information
expression of barley HvASN genes during leaf senescence and in response to starvation-induced senescence, monitoring of HvASN expression during developmental and stress-induced senescence, overview. Changes in HvASN transcript levels in plants grown under nitrate-limiting conditions, all the HvASN transcript levels (except HvASN4) decrease with ageing under low-nitrate conditions and increased under high-nitrate conditions
brenda
additional information
expression of barley HvASN genes during leaf senescence and in response to starvation-induced senescence, monitoring of HvASN expression during developmental and stress-induced senescence, overview. Changes in HvASN transcript levels in plants grown under nitrate-limiting conditions, all the HvASN transcript levels (except HvASN4) decrease with ageing under low-nitrate conditions and increased under high-nitrate conditions
brenda
additional information
expression of barley HvASN genes during leaf senescence and in response to starvation-induced senescence, monitoring of HvASN expression during developmental and stress-induced senescence, overview. Changes in HvASN transcript levels in plants grown under nitrate-limiting conditions, all the HvASN transcript levels (except HvASN4) decrease with ageing under low-nitrate conditions and increased under high-nitrate conditions
brenda
additional information
expression of barley HvASN genes during leaf senescence and in response to starvation-induced senescence, monitoring of HvASN expression during developmental and stress-induced senescence, overview. Changes in HvASN transcript levels in plants grown under nitrate-limiting conditions, all the HvASN transcript levels (except HvASN4) decrease with ageing under low-nitrate conditions and increased under high-nitrate conditions
brenda
additional information
expression of barley HvASN genes during leaf senescence and in response to starvation-induced senescence, monitoring of HvASN expression during developmental and stress-induced senescence, overview. Changes in HvASN transcript levels in plants grown under nitrate-limiting conditions, all the HvASN transcript levels (except HvASN4) decrease with ageing under low-nitrate conditions and increased under high-nitrate conditions
brenda
additional information
OsAS1 mRNA is the major species in rice roots when the seedlings are hydroponically grown for 18 d after germination with water
brenda
additional information
OsAS1 mRNA is the major species in rice roots when the seedlings are hydroponically grown for 18 d after germination with water
brenda
additional information
isozyme OsAS1 mRNA is the major species in rice roots when the seedlings are hydroponically grown for 18 d after germination with water
brenda
additional information
isozyme OsAS1 mRNA is the major species in rice roots when the seedlings are hydroponically grown for 18 d after germination with water
brenda
additional information
expression pattern of PVAS1, not expressed in nodules, not repressed by light
brenda
additional information
-
expression pattern of PVAS1, not expressed in nodules, not repressed by light
brenda
additional information
isoform PvAs3 is ubiquitously expressed and not repressed by light
brenda
additional information
comparative expressionanalysis of isozymes during pine development, quantitative real time-PCR expression analysis, overview
brenda
additional information
comparative expressionanalysis of isozymes during pine development, quantitative real time-PCR expression analysis, overview
brenda
additional information
-
comparative expressionanalysis of isozymes during pine development, quantitative real time-PCR expression analysis, overview
brenda
additional information
comparative expression analysis of isozymes during pine development, quantitative real time-PCR expression analysis, overview. PpAS2 expression is essentially constitutive
brenda
additional information
comparative expression analysis of isozymes during pine development, quantitative real time-PCR expression analysis, overview. PpAS2 expression is essentially constitutive
brenda
additional information
-
comparative expression analysis of isozymes during pine development, quantitative real time-PCR expression analysis, overview. PpAS2 expression is essentially constitutive
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the enzyme is recruited to centrosomes and associates with mitotic spindles in actively dividing cells
brenda
the enzyme is recruited to centrosomes and associates with mitotic spindles in actively dividing cells
brenda
-
tomato mosaic virus coat protein-interacting protein L (IP-L) and asparagine synthetase B (NbAS-B) interact in the nucleus and cytosol and IP-L apparently stabilizes NbAS-B, thus enhancing its accumulation
brenda
additional information
-
tomato mosaic virus coat protein-interacting protein L (IP-L) and asparagine synthetase B (NbAS-B) interact in the nucleus and cytosol and IP-L apparently stabilizes NbAS-B, thus enhancing its accumulation
brenda
additional information
E9BLE1
subcellular localization study using GFP-tagged enzyme
-
brenda
additional information
-
subcellular localization study using GFP-tagged enzyme
-
brenda
additional information
-
subcellular localization study using GFP-tagged enzyme
-
-
brenda
additional information
enzyme subcellular localisation determination, no localization of the Leishmania infantum enzyme in mitochondria
-
brenda
additional information
-
enzyme subcellular localisation determination, no localization of the Leishmania infantum enzyme in mitochondria
-
brenda
additional information
-
enzyme subcellular localisation determination, no localization of the Leishmania infantum enzyme in mitochondria
-
-
brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
targeting of knockdown of asparagine synthetase may improve the antitumor potency in pancreatic ductal adenocarcinomas
evolution
malfunction
metabolism
physiological function
additional information
evolution
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CaAS1 and its related plant proteins all contain an AsnB domain and an ASN synthetase domain
evolution
genes PpAS1 and PpAS2 encode both class II asparagine synthetases suggesting an ancient origin of the genes in plants. Amino acid residues essential for aspartate, AMP, and glutamine binding are conserved
evolution
genes PpAS1 and PpAS2 encode both class II asparagine synthetases suggesting an ancient origin of the genes in plants. Amino acid residues essential for aspartate, AMP, and glutamine binding are conserved, except valine268, included in the AMP binding site, which has been replaced by an isoleucine in the AS2 sequence
evolution
phylogenetic analysis has grouped ASN1 in dicot-subclass I while ASN2 and ASN3 are placed in dicot-subclass II
evolution
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the ability of asparagine synthetase to form filaments is evolutionarily conserved. Asparagine synthetase forms filaments in yeast in response to nutrient limitation
evolution
the ability of asparagine synthetase to form filaments is evolutionarily conserved. These structures may have acquired a novel mitotic function in higher eukaryotes
evolution
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phylogenetic analysis has grouped ASN1 in dicot-subclass I while ASN2 and ASN3 are placed in dicot-subclass II
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evolution
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the ability of asparagine synthetase to form filaments is evolutionarily conserved. Asparagine synthetase forms filaments in yeast in response to nutrient limitation
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malfunction
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salt tolerance of Arabidopsis knockout mutant with T-DNA insertion in ASN2 gene encoding asparagines synthetase is investigated. Results indicate that the knockout mutant is impaired in nitrogen assimilation and translocation under salt treatment
malfunction
silencing of the BmASNS gene enhances the sensitivity of silkworm cells to amino acid starvation. Ectopic overexpression of BmASNS gene effectively inhibits cell growth in silkworm cells, whereas its overexpression can rescue cell growth upon amino acid deprivation treatment. Silkworm cells lacking BmASNS under the condition of amino acid deprivation show severely impaired proliferation
malfunction
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silencing of CaAS1 gene results in enhanced susceptibility to Xanthomonas campestris pv. vesicatoria infection, phenotypes, overview
malfunction
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knockdown of asparagine synthetase (ASNS) leads to cell death even in the presence of glutamine, which can be reversed by addition of exogenous asparagine. Asparagine plays a critical role in regulating cellular adaptation to glutamine depletion. ASNS knockdown leads to profound apoptosis even in the presence of glutamine. Addition of extracellular asparagine completely restored cell survival and proliferation. Clinically, the expression of ASNS correlates with the progression of disease and poor prognosis of glioma and neuroblastoma patients. In neuroblastoma with unfavourable prognosis, ASNS expression is significantly higher. Asparagine-induced suppression of apoptosis: asparagine addition to glutamine-deprived cells alters the transcriptional response, suppressing the induction of the reported UPR effectors CHOP and XBP1 while maintaining the transcriptional induction of adaptive components of the UPR-response such as ASNS and HERPUD1. At the protein level, exogenous addition of asparagine suppresses CHOP induction without altering ATF4 accumulation or upstream eIF2alpha phosphorylation
malfunction
retrotransposon-mediated knockout mutants lacking AS1 show slight stimulation of shoot length and slight reduction in root length at the seedling stage. On the other hand, the mutation causes an approximately 80-90% reduction in free asparagine content in both roots and xylem sap
malfunction
enzyme AS-A ablation drives parasites auxotrophic to asparagine, but LiAS-A is not detrimental for parasite survival, growth or infectivity. The parasite burden in the spleen and liver of female BALB/c mice is not statistically different in LiASA mutants when compared to the wild-type
malfunction
no visible phenotype is detected for the asn3-1 and asn3-2 mutant. Both asn3-1 and asn3-2 rosette leaves contain wild-type levels of chlorophyll and ammonium content, indicating that ASN3 disruption does not cause a defective nitrogen status during vegetative growth. During seed development, leaves and stems serve as source tissues to supply nitrogen resources to developing siliques which in turn deliver nitrogen to seeds. When compared to wild-type seeds, asn3-1 seeds display reduced glutamine (by 30%), asparagine (20%) and aspartate (20%) contents while exhibiting increased glutamate (10%) amounts
malfunction
asparagine synthetase deficiency, ASD, is a neurological disorder having severe impacts on psychomotor development and mortality at an early age. Children with mutations in the ASNS gene exhibit developmental delays, intellectual disability, microcephaly, intractable seizures, and progressive brain atrophy. Mutations in the ASNS gene have been clinically associated with asparagine synthetase deficiency (ASD), phenotype. Neurologic disorder associated with asparagine synthetase deficiency (ASD). The transcription factor ATF4 binds to an enhancer element within the proximal promoter of the ASNS gene and activates transcription. Role of ATF4 in tumor cell survival and proliferation, ATF4 knockdown causes reduced survival in HT-1080 fibrosarcoma and DLD-1 colorectal adenocarcinoma cells in the absence of nonessential amino acids. Reduced proliferative capacity and increased apoptosis correlate with lower ASNS expression in the ATF4-deficient cells. Supplementation of the tumor cells with asparagine, but not other amino acids, leads to increased cell survival. Role of ASNS activity in modulating tumor growth
malfunction
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no visible phenotype is detected for the asn3-1 and asn3-2 mutant. Both asn3-1 and asn3-2 rosette leaves contain wild-type levels of chlorophyll and ammonium content, indicating that ASN3 disruption does not cause a defective nitrogen status during vegetative growth. During seed development, leaves and stems serve as source tissues to supply nitrogen resources to developing siliques which in turn deliver nitrogen to seeds. When compared to wild-type seeds, asn3-1 seeds display reduced glutamine (by 30%), asparagine (20%) and aspartate (20%) contents while exhibiting increased glutamate (10%) amounts
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malfunction
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enzyme AS-A ablation drives parasites auxotrophic to asparagine, but LiAS-A is not detrimental for parasite survival, growth or infectivity. The parasite burden in the spleen and liver of female BALB/c mice is not statistically different in LiASA mutants when compared to the wild-type
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metabolism
Asn is a major amino acid in maize and since AsnS is the primary means of Asn synthesis in plants it plays a very important role in nitrogen metabolism
metabolism
asparagine synthetase (AS) is responsible for the conversion of aspartate into Asn in an ATP-dependent manner, using ammonia or glutamine as a nitrogen source. There are two structurally distinct AS: the strictly ammonia-dependent type A, and the type B, which preferably uses glutamine
metabolism
E9BLE1
asparagine is formed by two structurally distinct asparagine synthetases in prokaryotes. One is the ammonia-utilizing asparagine synthetase A (AsnA, EC 6.3.1.1), and the other is asparagine synthetase B (AsnB, EC 6.3.5.4) that uses glutamine or ammonia as a nitrogen source. Sequence-based analysis suggests that Leishmania spp. possess the asparagine tRNA synthetase paralogue asparagine synthetase A (LdASNA) that is ammonia-dependent, but enzyme LdASNA from Leishmania donovani is both ammonia- and glutamine-dependent, EC 6.3.5.4
metabolism
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asparagine synthetase is a key enzyme that catalyses the conversion of amide groups from glutamine or ammonium to aspartate, which leads to the generation of asparagine
metabolism
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asparagine is formed by two structurally distinct asparagine synthetases in prokaryotes. One is the ammonia-utilizing asparagine synthetase A (AsnA, EC 6.3.1.1), and the other is asparagine synthetase B (AsnB, EC 6.3.5.4) that uses glutamine or ammonia as a nitrogen source. Sequence-based analysis suggests that Leishmania spp. possess the asparagine tRNA synthetase paralogue asparagine synthetase A (LdASNA) that is ammonia-dependent, but enzyme LdASNA from Leishmania donovani is both ammonia- and glutamine-dependent, EC 6.3.5.4
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metabolism
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asparagine synthetase (AS) is responsible for the conversion of aspartate into Asn in an ATP-dependent manner, using ammonia or glutamine as a nitrogen source. There are two structurally distinct AS: the strictly ammonia-dependent type A, and the type B, which preferably uses glutamine
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physiological function
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Arabidopsis knockout mutant with T-DNA insertion in ASN2 gene, subject to 100 mM NaCl stress for 6 to 24 h. The salt treatment decreases chlorophyll and soluble protein contents, and increases ammonium level in the asn2-1 leaves. The salinity induces ASN1 mRNA level in the wild-type and asn2-1 leaves. The salt treatment inhibits the transcript and protein levels of chloroplastic glutamine synthetase 2, EC 6.3.1.2 in the wild-type and asn2-1 leaves
physiological function
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silencing of the gene encoding AS1 results in enhanced susceptibility to Xanthomonas campestris pv. vesicatoria infection. Transgenic Arabidopsis thaliana plants that overexpress CaAS1 exhibit enhanced resistance to Pseudomonas syringae pv. tomato DC3000 and Hyaloperonospora arabidopsidis. Increased CaAS1 expression influences early defense responses in diseased leaves, including increased electrolyte leakage, reactive oxygen species and nitric oxide burst. In CaAS1-silenced pepper and/or CaAS1-overexpressing Arabidopsis, CaAS1-dependent changes in asparagine levels correlate with increased susceptibility or defense responses to microbial pathogens, respectively
physiological function
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elevated expression of ASNS protein is associated with resistance to asparaginase therapy in childhood acute lymphoblastic leukemia and may be a predictive factor in drug sensitivity for certain solid tumors as well. Activation of the GCN2-eIF2-ATF4 signaling pathway, leading to increased ASNS expression, appears to be a component of solid tumor adaptation to nutrient deprivation and/or hypoxia, roles of the enzyme in fetal development, tissue differentiation, and tumor growth, overview. Possible correlation between ASNase sensitivity and the DNA methylation status of the ASNS gene
physiological function
BmAsns protein negatively regulates silkworm cell proliferation. The recovery of cell growth by overexpressed BmAsns protein is due to the rapid turnover of autophagic vacuoles in the cells
physiological function
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asparagine synthetase 1 is essential for plant defense to microbial pathogens. Increased CaAS1 expression influences early defense responses in diseased leaves, including increased electrolyte leakage, reactive oxygen species and nitric oxide bursts. In plants, increased conversion of aspartate to asparagine appears to be associated with enhanced resistance to bacterial and oomycete pathogens, phenotypes, overview
physiological function
the expression of PpAS1 is regulated by developmental and environmental factors
physiological function
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asparagine synthetase (ASNS) plays an important role during tumor cell accumulation and progression by maintaining cell viability. The enzyme synthesizes asparagine de novo from aspartate and glutamine. Asparagine plays a critical role in regulating cellular adaptation to glutamine depletion. The anti-apoptotic function of glutamine depends on the ability of asparagine synthetase to maintain glutamine-dependent biosynthesis of asparagine. Transcription factor ATF4 induces asparagine synthetase which results in glutamine-dependent asparagine synthesis from aspartate, in turn asparagine accumulation then suppresses GCN2 and reduces ATF4
physiological function
asparagine synthetase1, but not asparagine synthetase2, is responsible for the biosynthesis of asparagine following the supply of ammonium to rice roots. AS1 is apparently coupled to the primary assimilation of NH+4 in rice roots
physiological function
asparagine synthetase1, but not asparagine synthetase2, is responsible for the biosynthesis of asparagine following the supply of ammonium to rice roots
physiological function
Leishmania infantum encodes for a functional AS-A enzyme, which uses either ammonia or glutamine as nitrogen donor for asparagine synthesis. LiAS-A is required for promastigotes growth only in asparagine limiting conditions
physiological function
E9BLE1
enzyme LdASNA is essential for survival of the Leishmania parasite
physiological function
asparagine synthetase transfers the amide group of glutamine to aspartate, forming asparagine and glutamate. Asparagine, glutamine, aspartate and glutamate are important nitrogen carriers transported in the phloem, asparagine is a major nitrogen transporter since it contains more nitrogen per carbon (2N:4C) compared to glutamine (2N:5C), aspartate (1N:4C) and glutamate (1N:5C). Role of isozyme ASN3-encoded asparagine synthetase during vegetative growth, seed development and germination of Arabidopsis thaliana, overview
physiological function
asparagine synthesis is catalyzed by the enzyme asparagine synthetase, and occurs by the ATP-dependent transfer of the amino group of glutamine to a molecule of aspartate to generate glutamate and asparagine, isozyme TaASN1 is an active asparagine synthetase, producing asparagine and glutamate from glutamine and aspartate, reaction modeling. There are large differences in the free asparagine concentration of grain from different wheat varieties
physiological function
asparagine synthesis is catalyzed by the enzyme asparagine synthetase, and occurs by the ATP-dependent transfer of the amino group of glutamine to a molecule of aspartate to generate glutamate and asparagine, isozyme TaASN2 is an active asparagine synthetase, producing asparagine and glutamate from glutamine and aspartate, reaction modeling, There are also large differences in the free asparagine concentration of grain from different wheat varieties
physiological function
asparagine synthesis is catalyzed by the enzyme asparagine synthetase, and occurs by the ATP-dependent transfer of the amino group of glutamine to a molecule of aspartate to generate glutamate and asparagine
physiological function
asparagine synthetase (ASNS) catalyzes the synthesis of asparagine and glutamate from aspartate and glutamine in an ATP-dependent amidotransferase reaction. Elevated ASNS protein expression is associated with resistance to asparaginase therapy in childhood acute lymphoblastic leukemia. Regulation of ASNS expression, overview. transcription factor ATF4 binds to an enhancer element within the proximal promoter of the ASNS gene and activates transcription. Asparagine depletion activates the amino acid response, AAR, whereas endoplasmic reticulum stress activates the unfolded protein response, UPR
physiological function
asparagine synthetase (ASNS) catalyzes the synthesis of asparagine and glutamate from aspartate and glutamine in an ATP-dependent amidotransferase reaction
physiological function
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key enzymes of nitrogen metabolism in plants. The product of asparagine synthase is asparagine, which is one of the key compounds involved in N transport and storage in plants. Possible role of the asparagine synthase genes in improving cotton growth, fiber development, and especially N metabolism in cotton
physiological function
essential enzyme for endogenous asparagine products. Asparagine synthetase promotes metastasis depending on Wnt pathway and mitochondrial functions even without endogenous asparagine products. Asparagine synthetase regulates lung-cancer metastasis by stabilizing the beta-catenin complex and modulating mitochondrial response
physiological function
key enzyme in plant nitrogen metabolism, plays an important role in plant nitrogen assimilation and distribution. Asparagine (Asn), the product of asparagine synthetase, is one of the main compounds responsible for organic nitrogen transport and storage in plants
physiological function
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co-localization data from both functional and activity-disrupted Asn1/2p suggest that asparagine synthetase associates with the mitotic spindle in an activity-independent manner, implying that the enzyme, in higher eukaryotes with open mitosis, might have a moonlighting function in cell division, in addition to its catalytic function
physiological function
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asparagine synthetase associates with tomato mosaic virus coat protein-interacting protein L (IP-L) and confers resistance against tobacco mosaic virus via the asparagine-induced salicylic acid signalling pathway
physiological function
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asparagine synthetases are activated and can contribute to Asn production during air curing (a senescence-induced process that allows tobacco leaves to dry out). ASN1 and ASN5 are critical for regulating Asn synthesis in cured tobacco leaves
physiological function
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key enzymes of nitrogen metabolism in plants. The product of asparagine synthase is asparagine, which is one of the key compounds involved in N transport and storage in plants. Possible role of the asparagine synthase genes in improving cotton growth, fiber development, and especially N metabolism in cotton
physiological function
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key enzymes of nitrogen metabolism in plants. The product of asparagine synthase is asparagine, which is one of the key compounds involved in N transport and storage in plants. Possible role of the asparagine synthase genes in improving cotton growth, fiber development, and especially N metabolism in cotton
physiological function
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overexpression of asparagine synthetase B (NbAS-B) in tobacco reduces tobacco mosaic virus/green fluorescent protein infection by significantly improving the synthesis of asparagine
physiological function
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ASN1 and ASN5 are key regulators of asparagine metabolism during leaf curing, a senescence-induced process that allows tobacco leaves to dry out
physiological function
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ASN1 and ASN5 are key regulators of asparagine metabolism during leaf curing, a senescence-induced process that allows tobacco leaves to dry out
physiological function
asparagine synthetase regulates lung-cancer metastasis by stabilizing the beta-catenin complex and modulating mitochondrial response
physiological function
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asparagine synthetase transfers the amide group of glutamine to aspartate, forming asparagine and glutamate. Asparagine, glutamine, aspartate and glutamate are important nitrogen carriers transported in the phloem, asparagine is a major nitrogen transporter since it contains more nitrogen per carbon (2N:4C) compared to glutamine (2N:5C), aspartate (1N:4C) and glutamate (1N:5C). Role of isozyme ASN3-encoded asparagine synthetase during vegetative growth, seed development and germination of Arabidopsis thaliana, overview
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physiological function
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enzyme LdASNA is essential for survival of the Leishmania parasite
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physiological function
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Leishmania infantum encodes for a functional AS-A enzyme, which uses either ammonia or glutamine as nitrogen donor for asparagine synthesis. LiAS-A is required for promastigotes growth only in asparagine limiting conditions
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additional information
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human enzyme activity is highly regulated in response to cell stress, primarily by increased transcription from a single gene located on chromosome 7, ASNS transcription control by C/EBP-ATF response element within the promoter. Protein limitation or an imbalanced dietary amino acid composition activate the ASNS gene through the amino acid response, a process that is replicated in cell culture through limitation for any single essential amino acid
additional information
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transgenic Arabidopsis thaliana plants that overexpress CaAS1 exhibit enhanced resistance to Pseudomonas syringae pv. tomato DC3000 and Hyaloperonospora arabidopsidis
additional information
enzyme structure homology modeling, structure and sequence comparisons of the enzymes from Leishmania infantum and Leishmania major, overview
additional information
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enzyme structure homology modeling, structure and sequence comparisons of the enzymes from Leishmania infantum and Leishmania major, overview
additional information
glutamine is predicted to bind in a manner so that the carboxamide group is oriented toward the interface of the two domains to allow the transfer of an ammonia group from glutamine to aspartate
additional information
glutamine binds in a manner so that the carboxamide group is oriented toward the interface of the two domains to allow the transfer of an ammonia group from glutamine to aspartate
additional information
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Asn1p and Asn2p both co-assemble into filaments in response to nutrient limitation. However, the ability of Asn2p to form filaments is strictly dependent on the presence of Asn1p
additional information
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enzyme structure homology modeling, structure and sequence comparisons of the enzymes from Leishmania infantum and Leishmania major, overview
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Show AA Sequence and Transmembrane Helices (30036 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52500
65000
x * 65500, amino acid sequence calculation, x * 65000, Western blot analysis, HvAS1
65500
66000
70000
52500
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1 * 52500, possibly the enzyme population is heterogeneous with slight differences in subunit composition, SDS-PAGE after treatment with dimethyl suberimidate
52500
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2 * 52500, possibly the enzyme population is heterogeneous with slight differences in subunit composition, SDS-PAGE after treatment with dimethyl suberimidate
65500
x * 65500, amino acid sequence calculation, x * 65000, Western blot analysis, HvAS1
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
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1 * 52500, possibly the enzyme population is heterogeneous with slight differences in subunit composition, SDS-PAGE after treatment with dimethyl suberimidate
additional information
?
x * 65500, amino acid sequence calculation, x * 65000, Western blot analysis, HvAS1
?
E9BLE1
x * 40000, about, sequence calculation, x * 44000, recombinant Hi6-tagged enzyme, SDS-PAGE
?
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x * 40000, about, sequence calculation, x * 44000, recombinant Hi6-tagged enzyme, SDS-PAGE
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dimer
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2 * 52500, possibly the enzyme population is heterogeneous with slight differences in subunit composition, SDS-PAGE after treatment with dimethyl suberimidate
homodimer
2 * 42000, recombinant enzyme, SDS-PAGE, 2 * 39800, native enzyme, SDS-PAGE
homodimer
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2 * 42000, recombinant enzyme, SDS-PAGE, 2 * 39800, native enzyme, SDS-PAGE
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additional information
the enzyme contains two functional domains, the N-terminal domain (residues 1-208) consists of a two-layer, antiparallel beta-sheet core surrounded by four alpha-helices, this domain harbors the glutamine-binding pocket, consisting of residues Arg49, Asn75, Glu77, and Asp97. The C-terminal domain (residues 209-561) is composed primarily of alpha-helices, but also encompasses a five-stranded, parallel beta-sheet that contains the ATP-binding site: residues Leu256, Val288, Asp295, Ser363, Gly364, Glu365, and Asp401
additional information
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dimerization of the 160000 MW enzyme is induced by MgCl2 and ATP
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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not stained for carbohydrate by the periodic acid-Schiff procedure
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
AS-B is dialyzed against 20 mM Bis-Tris, pH 6.5, 150 mM NaCl, 0.5 mM EDTA, and 2 mM dithiothreitol, crystals are grown by hanging drop vapor diffusion at 4°C, AS-B solution is adjusted to 6.5 mg/ml and contains 10 mM MgCl2, 5 mM glutamine, and 10 mM AMP, 0.01 ml of protein solution are mixed with 0.01 ml precipitant solution containing 14% polyethylene glycol 8000 and 50 mM HEPES, pH 7.0, these droplets are suspended against wells containing 15% polyethylene glycol 8000 and 50 mM HEPES, pH 7.0, crystals diffract to 2.0 A
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C1A
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replacement of Cys1 by either Ala or Ser results in a loss of glutaminase activity and Gln-dependent activity, without any significant effect upon NH4+-dependent Asn synthesis. Kinetic parameters of the NH4+-dependent activity of H29A and H80A are unchanged with respect to wild-type AS-B, the apparent Km for Gln is increased by a factor of 4.5 in Gln-dependent Asn synthesis
C1S
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replacement of Cys1 by either Ala or Ser results in a loss of glutaminase activity and Gln-dependent activity, without any significant effect upon NH4+-dependent Asn synthesis. Kinetic parameters of the NH4+-dependent activity of H29A and H80A are unchanged with respect to wild-type AS-B, the apparent Km for Gln is increased by a factor of 4.5 in Gln-dependent Asn synthesis
E348A
E348D
E348Q
N74A
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mutant N74A, in which Asn is replaced by Ala can also use NH2OH as an alternative substrate to NH4+ and catalyze the hydrolysis of L-glutamic acid gamma-monohydroxamate
N74D
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replacement of the catalytically important residue Asn-74 by Asp, N74D, in the N-terminal domain of Escherichia coli Asn synthetase B confers nitrile hydratase activity upon the mutant enzyme. While wild-type As-B can efficiently catalyze the hydrolysis of Gln to Glu, the N74D As-B mutant exhibits very low glutaminase activity
N74X
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overexpression of a series of mutant enzymes. Site-directed mutagenesis of Asn74 shows that this residue plays a role in catalysis of nitrogen transfer from Gln. Replacement of Arg-30 by an Ala residue yields a mutant enzyme for which the apparent Km for Gln is increased in the Gln-dependent synthesis of Asn. In addition ATP-dependent stimulation of the glutaminase activity is modified or completely eliminated when Arg-30 is replaced by other amino acids
R30A
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overexpression of a series of mutant enzymes. Site-directed mutagenesis of Asn74 shows that this residue plays a role in catalysis of nitrogen transfer from Gln. Replacement of Arg-30 by an Ala residue yields a mutant enzyme for which the apparent Km for Gln is increased in the Gln-dependent synthesis of Asn. In addition ATP-dependent stimulation of the glutaminase activity is modified or completely eliminated when Arg-30 is replaced by other amino acids
R325A
R325L
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a number of site-specific AS-B mutants. When Arg325 is replaced by Ala or Lys, the resulting mutant enzymes possess no detectable Asn synthetase activity. Mutation of Thr322 and Thr323 also produce enzymes with altered kinetic properties, suggesting that these Thr are involved in Asp binding and/or stabilization of intermediates en route to beta-aspartyl-AMP
T322X
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a number of site-specific AS-B mutants. When Arg325 is replaced by Ala or Lys, the resulting mutant enzymes possess no detectable Asn synthetase activity. Mutation of Thr322 and Thr323 also produce enzymes with altered kinetic properties, suggesting that these Thr are involved in Asp binding and/or stabilization of intermediates en route to beta-aspartyl-AMP
T323X
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a number of site-specific AS-B mutants. When Arg325 is replaced by Ala or Lys, the resulting mutant enzymes possess no detectable Asn synthetase activity. Mutation of Thr322 and Thr323 also produce enzymes with altered kinetic properties, suggesting that these Thr are involved in Asp binding and/or stabilization of intermediates en route to beta-aspartyl-AMP
A380S
naturally occuring mutation, homozygous mutation, mutation of a polar residue in the hydrophobic region
A6E
naturally occuring mutation, compound heterozygous, mutation of a charged amino acid in hydrophobic region, causing steric clash with Phe8
C1A
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altering Cys-1 to either Ala or Ser eliminated the Gln-dependent activity, while only minimally affecting the kinetic properties of the NH4+-dependent reaction
C1S
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altering Cys-1 to either Ala or Ser eliminated the Gln-dependent activity, while only minimally affecting the kinetic properties of the NH4+-dependent reaction
F362V
naturally occuring mutation, homozygous mutation, causes a decrease in van der Waals interactions
G289A
naturally occuring mutation, compound heterozygous, mutation proximal to the ATP-binding site, causing steric hindrance with Ser293
L145S
L247W
R340H
naturally occuring mutation, homozygous mutation, causes a loss of hydrogen bonds, and a steric clash with Phe482
R49Q
naturally occuring mutation, homozygous mutation of the glutamine-binding site, causes loss of hydrogen bonding
R550C
S480F
naturally occuring mutation, compound heterozygous, mutation of a nonpolar residue on protein surface that may decrease solubility
T337I
naturally occuring mutation, Proximal to ATP-binding site, causes a hydrophobic patch on protein that may decrease solubility
V489D
Y398C
naturally occuring mutation, homozygous mutation, causes a decrease in van der Waals interactions, solvent-accessible thiol group
Y541Cfs
the mutant enzyme shows significantly lower enzymatic activity when compared with that of the wild-type protein. For the Trp541Cysfs*5 variant expression construct, the 6*His-tag is added just before the new termination codon generated by the frameshift mutation
up
gene PpAS2 expression is upregulated during drought, but the level of PpAS2 transcripts is not altered by darkness
A6E
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mutation in ASN1 causes a lowering in the protein expression levels of asparagine synthetase and also affects the growth of yeast. ASN2 is deleted from the yeast genome, allowing only ASN1 to be mutated and characterized
A6E
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mutation in ASN1 causes a lowering in the protein expression levels of asparagine synthetase and also affects the growth of yeast. ASN2 is deleted from the yeast genome, allowing only ASN1 to be mutated and characterized
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additional information
E348A
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mutant exhibits similar glutaminase activity to the wild-type enzyme in the absence of ATP, but is not capable of catalyzing asparagine formation when glutamine is employed as a nitrogen source
E348A
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mutant shows similar glutaminase activity to the wild-type enzyme in the absence of ATP, mutant is not capable of catalyzing asparagine formation when glutamine is employed as a nitrogen source, mutant shows no synthetase activity, ATP-dependent stimulation of glutaminase activity is less than that of wild-type enzyme
E348D
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mutant exhibits similar glutaminase activity to the wild-type enzyme in the absence of ATP and is capable of catalyzing asparagine formation when glutamine is employed as a nitrogen source. Formation of the beta-aspartyl-AMP intermediate, and therefore the eventual production of asparagine, is dependent on the presence of a carboxylate side chain at this position in the synthetase active site. In addition, E348 may also play a role in mediating the conformational changes needed to coordinate, albeit weakly, the glutaminase and synthetase activities of the enzyme and to establish the structural integrity of the intramolecular tunnel along which ammonia is translocated
E348D
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mutant shows similar glutaminase activity to the wild-type enzyme in the absence of ATP, mutant is capable of catalyzing asparagine formation when glutamine is employed as a nitrogen source, glutaminase activity of the E348D mutant is stimulated more than 6fold relative to wild-type by the presence of 5 mM ATP, a 5fold decrease in the Km value for aspartate is observed for both the glutamine- and ammonia-dependent synthetase reactions, together with a kcat that is half of that observed for the wildtype enzyme
E348Q
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mutant exhibits similar glutaminase activity to the wild-type enzyme in the absence of ATP, but is not capable of catalyzing asparagine formation when glutamine is employed as a nitrogen source
E348Q
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mutant shows similar glutaminase activity to the wild-type enzyme in the absence of ATP, mutant is not capable of catalyzing asparagine formation when glutamine is employed as a nitrogen source, mutant shows no synthetase activity, ATP-dependent stimulation of glutaminase activity is less than that of wild-type enzyme
R325A
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a number of site-specific AS-B mutants. When Arg325 is replaced by Ala or Lys, the resulting mutant enzymes possess no detectable Asn synthetase activity. Mutation of Thr322 and Thr323 also produce enzymes with altered kinetic properties, suggesting that these Thr are involved in Asp binding and/or stabilization of intermediates en route to beta-aspartyl-AMP
L145S
naturally occuring mutation, compound heterozygous, mutation of a polar side chain in hydrophobic region
L145S
mutant enzyme is less stable than wild-type enzyme. The mutant enzyme shows significantly lower enzymatic activity when compared with that of the wild-type protein
L247W
naturally occuring mutation, causes a decrease in van der Waals interactions
R550C
naturally occuring mutation, causes a decrease in side chain length likely to result in loss of interactions
R550C
naturally occuring mutation, homozygous mutation, causes a decrease in side chain length likely to result in loss of interactions
V489D
naturally occuring mutation, compound heterozygous, inserts a charged amino acid in hydrophobic region
V489D
mutant enzyme is less stable than wild-type enzyme. The mutant enzyme shows significantly lower enzymatic activity when compared with that of the wild-type protein
additional information
phenotypes of isozyme ASN3 knockout mutant lines asn3-1 (SALK_053490) and asn3-2 (SALK_074279), The level of ASN3 mRNA is reduced to 2.5% and 15% of the wild-type value in the seeds of asn3-1 and asn3-2, respectively, overview. Impact of ASN3 disruption on asparagine, glutamine, aspartate and glutamate levels in asn3-1 siliques and compared to wild-type: The young siliques of the asn3-1 knockout line show an increase in glutamine (Glnasn3-1 to GlnCol-0 ratio of 1.014), glutamate (Gluasn3-1 to GluCol-0 ratio of 1.189) and aspartate (Aspasn3-1 to AspCol-0 ratio of 1.149) and a decrease in asparagine (Asnasn3-1 to AsnCol-0 ratio of 0.902)
additional information
-
phenotypes of isozyme ASN3 knockout mutant lines asn3-1 (SALK_053490) and asn3-2 (SALK_074279), The level of ASN3 mRNA is reduced to 2.5% and 15% of the wild-type value in the seeds of asn3-1 and asn3-2, respectively, overview. Impact of ASN3 disruption on asparagine, glutamine, aspartate and glutamate levels in asn3-1 siliques and compared to wild-type: The young siliques of the asn3-1 knockout line show an increase in glutamine (Glnasn3-1 to GlnCol-0 ratio of 1.014), glutamate (Gluasn3-1 to GluCol-0 ratio of 1.189) and aspartate (Aspasn3-1 to AspCol-0 ratio of 1.149) and a decrease in asparagine (Asnasn3-1 to AsnCol-0 ratio of 0.902)
-
additional information
-
various mutant strains, deletion of asnO or asnH, singly or in combination, has no effect on growth rates in media with or without asparagine, deletion of asnB leads to a slow-growth phenotype, even in the presence of asparagine, strains lacking asnO cannot sporulate
additional information
-
various mutant strains, deletion of asnO or asnH, singly or in combination, has no effect on growth rates in media with or without asparagine, deletion of asnB leads to a slow-growth phenotype, even in the presence of asparagine, strains lacking asnO cannot sporulate
-
additional information
RNA interference is used to silence BmASNS expression in silkworm cells
additional information
-
the replacement of the N-terminal Cys by Ala results in the loss of the Gln-dependent Asn synthetase activity, while the NH4+-dependent activity remains unaffected
additional information
identification of two naturally occuring nonsense mutations, R407* and W541Cfs*5 (frameshift mutation), leading to truncated enzyme mutants
additional information
E9BLE1
gene deletion mutations of gene asnA are attempted via targeted gene replacement. Gene deletion of LdASNA leads to growth delay in mutants. Chromosomal null mutants of LdASNA cannot be obtained as the double transfectant mutants show aneuploidy
additional information
-
gene deletion mutations of gene asnA are attempted via targeted gene replacement. Gene deletion of LdASNA leads to growth delay in mutants. Chromosomal null mutants of LdASNA cannot be obtained as the double transfectant mutants show aneuploidy
additional information
-
gene deletion mutations of gene asnA are attempted via targeted gene replacement. Gene deletion of LdASNA leads to growth delay in mutants. Chromosomal null mutants of LdASNA cannot be obtained as the double transfectant mutants show aneuploidy
-
additional information
generation of a AS-A gene knockout mutant by targeted gene replacement
additional information
-
generation of a AS-A gene knockout mutant by targeted gene replacement
additional information
-
generation of a AS-A gene knockout mutant by targeted gene replacement
-
additional information
construction of an OsAS1 knockout mutant by insertion of retrotransposon Tos17
additional information
construction of an OsAS1 knockout mutant by insertion of retrotransposon Tos17
additional information
PvAs3 is able to complement Escherichia coli asparagine auxotroph strain ER
additional information
PpAS2 transcript abundance is not affected by any nitrogen treatments or by water stress, PpAS2 expression is essentially constitutive
additional information
PpAS2 transcript abundance is not affected by any nitrogen treatments or by water stress, PpAS2 expression is essentially constitutive
additional information
-
PpAS2 transcript abundance is not affected by any nitrogen treatments or by water stress, PpAS2 expression is essentially constitutive
additional information
-
design of a silencing construct that simultaneously targets the expression of both isoforms StAs1and StAs2. Tubers of the transformed intragenic plants contain up to 20fold reduced levels of free asparagine. This coincides with a small increase in the formation of glutamine and does not affect tuber shape or yield. Heat-processed products derived from the low-asparagine tubers are indistinguishable from their untransformed counterparts in terms of sensory characteristics. However, both French fries and potato chips accumulate as little as 5% of the acrylamide present in wild-type controls
additional information
after ste10 gene knock-out, the monosaccharide composition of the exopolysaccharide produced by the mutant is changed in comparison with that of native exopolysaccharide Ebosin while its antagonist activity for IL-1R decreases significantly
additional information
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variety Chinese Spring lacks a TaASN2 gene in the B genome
additional information
variety Chinese Spring lacks a TaASN2 gene in the B genome
additional information
variety Chinese Spring lacks a TaASN2 gene in the B genome
additional information
variety Chinese Spring lacks a TaASN2 gene in the B genome
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
-
4°C, 24 h, 29.8% of the residual enzyme activity is retained
8
-
half-life in the buffer solution at pH 8 and 30°C is 857.85 min
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
half-life in the buffer solution at pH 8 and 30°C is 857.85 min
40
additional information
-
a combination of L-Asp, ATP, and Mg2+ protects against heat inactivation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity is markedly decreased by freezing for 7 days at -87°C in the presence of 1 mM dithiothreitol. Protection by 10 mM dithiothreitol
-
enzyme requires protection by high levels of thiols, glycerol and substrates also stabilize
-
glycerol and 2-mercaptoethanol are essential for enzyme stability during purification at 4°C
-
unstable enzyme, 20-25% v/v glycerol and 65-70 mM 2-mercaptoethanol stabilize during storage at low temperatures
unstable enzyme, 20-25% v/v glycerol and 65-70 mM 2-mercaptoethanol stabilize during storage at low temperatures
-
unstable enzyme, 20-25% v/v glycerol and 65-70 mM 2-mercaptoethanol stabilize during storage at low temperatures
-
unstable enzyme, 20-25% v/v glycerol and 65-70 mM 2-mercaptoethanol stabilize during storage at low temperatures
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SDS
proteins are always extracted in buffer with 2% SDS, otherwise a high degree of degradation is detected
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, inactivated after 3 months, reactivation by addition of dithiothreitol
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
development of a method to refold recombinant AsnS from inclusion bodies
partial
recombinant fusion protein consisting of the 42 kDa N-terminal region of AS and a 17 kDa tagged-region from pET32a(+) expression plasmid
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography to over 95% purity
E9BLE1
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, and ion exchange chromatography
refolded, solubilized recombinant His-tagged isozyme AsnS1 by nickel affinity chromatography
refolded, solubilized recombinant His-tagged isozyme AsnS2 by nickel affinity chromatography, recombinant nontagged isozyme ZmAsnS2 from Escherichia coli by anion exchange chromatography
refolded, solubilized recombinant His-tagged isozyme AsnS4 by nickel affinity chromatography
refolded, solubilized recombinant His-tagged isozyme by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a fusion protein consisting of the 42 kDa N-terminal region of AS and a 17 kDa tagged-region from pET32a(+) expression plasmid, expression in Escherichia coli
-
C-terminally tagged enzyme, baculovirus-based expression system, the recombinant enzyme is correctly processed, exhibits high activity and is stable on prolonged storage at -80°C
-
cloned into a 2 mü plasmid, pBS24.1GAS, suitable for replication in a Saccharomyces cerevisiae ciro strain AB116
-
cloning and specificity of the amino acid-dependent contol of its mRNA content
-
DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3), enzyme expression analysis
expressed in silkworm using a baculoviral expression system. ASNS deficient HEK293 cells are established using the CRISPR/Cas9 method and evaluated the growth of cells without asparagine after transduction of ASNS variants with a lentiviral expression system. The four ASNS variants display significantly low enzymatic activity. A method for evaluating the enzymatic activity of the recombinant human ASNS variants is established. The results of the cell-based assay corroborate the results of the enzymatic activity. These methods should enable the evaluation of the pathogenicity of ASNS variants
expression in Escherichia coli
expression in Escherichia coli. Complementation experiments using an Asn-deficient Escherichia coli strain to demonstrate that three putative asparagine synthetase family members in poplar (Populus simonii x P. nigra) function in Asn synthesis
expression in Escherichia coli. Complementation experiments using an Asn-deficient Escherichia coli strain to demonstrate that three putative asparagine synthetase family members in poplar (Populus simonii x Populus nigra) function in Asn synthesis
from BmN4 cells, recombinant expression of the GFP-tagged or Venus fluorescent protein-tagged enzyme in BmN4 cells
gene ASN1, a single copy gene located on chromosome 5 of each genome, genetic organization, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression in Escherichia coli strain Rosetta DE3
gene ASN2, a single copy gene located on chromosome 3 of each genome, variety Chinese Spring lacks a TaASN2 gene in the B genome, DNA and amino acid sequence determination and analysis, sequence comparisons, genetic organization, recombinant expression in Escherichia coli strain Rosetta DE3
gene ASN3, real-time quantitative RT-PCR isozyme expression analysis
gene ASN3, two copies of TaASN3 are found on chromosome 1 of each genome, termed TaASN3.1 and TaASN3.2, DNA and amino acid sequence determination and analysis, sequence comparisons, genetic organization, recombinant expression in Escherichia coli strain Rosetta DE3
gene ASN4, a single copy gene located on chromosome 4 of each genome, DNA and amino acid sequence determination and analysis, sequence comparisons
gene asnS, expression of C-terminally His-tagged isozyme AsnS1 in Escherichia coli strains BL21(DE3) and Rosetta(DE3) mainly in the inclusion bodies
gene asnS2, expression of nontagged isozyme ZmAsnS2 in Escherichia coli, expression of C-terminally His-tagged isozyme AsnS2 in Escherichia coli strains BL21(DE3) and Rosetta(DE3) mainly in the inclusion bodies although small amounts of ZmAsnS2 are recovered in the soluble fraction
gene asnS3, expression of C-terminally His-tagged isozyme AsnS3 in Escherichia coli strains BL21(DE3) and Rosetta(DE3) mainly in the inclusion bodies
gene asnS4, expression of C-terminally His-tagged isozyme AsnS4 in Escherichia coli strains BL21(DE3) and Rosetta(DE3) mainly in the inclusion bodies
gene CaAS1, enzyme overexpression in transgenic Arabidopsis thaliana plants leads to enhanced resistance of the plants to Pseudomonas syringae pv. tomato DC3000 and Hyaloperonospora arabidopsidis, phenotypes, overview
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gene HvASN1, DNA and amino acid sequence determination and analysis, phylogenetic tree, expression analysis
gene HvASN2, DNA and amino acid sequence determination and analysis, phylogenetic tree, expression analysis
gene HvASN3, DNA and amino acid sequence determination and analysis, phylogenetic tree, expression analysis
gene HvASN4, DNA and amino acid sequence determination and analysis, phylogenetic tree, expression analysis
gene HvASN5, DNA and amino acid sequence determination and analysis, phylogenetic tree, expression analysis
gene LDBPK_300470, DNA and amino acid sequence determination and analysis, sequence comaparisons and phylogenetic analysis, cloning of the pSP-alpha-blast-alpha-ASNA and pSP72-alpha-neo-alpha-GFP-ASNA episome, overexpression of GFP-tagged ASNA in Leishmania donovani Bob strain MHOM/SD/62/1SCL2D, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21
E9BLE1
gene NAS2, DNA and mino acid sequence determination and analysis, promoter determination, tissue expression analysis, overview
gene Os03g0291500, quantitative real-time PCR enzyme expression analysis
gene Os06g0265000, quantitative real-time PCR enzyme expression analysis
gene PpAS1, DNA and amino acid sequence analysis, sequence comparisons, phylogenetic analysis, genetic regulation of AS1 transcription, overview
gene PpAS2, DNA and amino acid sequence analysis, sequence comparisons, phylogenetic analysis
HvAS1, from leaves, located to the long arm of chromosome 5, sequencing
HvAS2, from leaves, located to the short arm of chromosome 3, sequencing
mutant enzyme in which the N-terminal Cys is replaced by Ala is expressed in Saccharomyces
-
PVAS2 is cloned into the expression vector pGEXKG and overexpressed as a glutathione S-transferase fusion protein. PVAS2 is cloned into pUC18, expression in Escherichia coli asparagine-auxotroph ER4813
-
three asparagine snythetase genes asnB, asnH and asnO, expression in Bacillus subtilis and in Escherichia coli ME6279, sequencing, genetic organization
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ASN1-S and ASN5-S are induced rapidly at the onset of curing in detached leaves while being expressed only after 24 h of curing in attached leaves. Induction of ASN1-S is stronger in cured detached leaves than in cured attached leaves
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ASNS activity is highly responsive to cellular stress, primarily by increased transcription from the single gene located on chromosome 7. The transcription factor ATF4 binds to an enhancer element within the proximal promoter of the ASNS gene and activates transcription
gene PpAS1 expression is upregulated during drought, and in the dark in all organs. PpAS1 transcripts accumulate with seedlings that are grown under high concentrations of nitrate or ammonium. Ability of PtMYB1 to activate the transcription of PpAS1 in vivo, PtMYB1 negatively regulates PpAS1 promoter in pine protoplasts
human enzyme activity is highly regulated in response to cell stress, primarily by increased transcription from a single gene located on chromosome 7. Protein limitation or an imbalanced dietary amino acid composition activate the ASNS gene through the amino acid response, a process that is replicated in cell culture through limitation for any single essential amino acid. Endoplasmic reticulum stress also increases ASNS transcription through the PERK-eIF2-ATF4 arm of the unfolded protein response. Both the amino acid response and unfolded protein response lead to increased synthesis of ATF4, which binds to the C/EBP-ATF response element and induces ASNS transcription
-
infection with Xanthomonas campestris pv. vesicatoria induces early and strong CaAS1 expression in leaves. Significant induction of CaAS1 expression occurs in pepper leaves following treatment with salicylic acid, methyl jasmonate or wounding
-
infection with Xanthomonas campestris pv. vesicatoria induces early and strong CaAS1 expression in pepper leaves
-
long-term dark treatment results in a significant increase in PnAS1 expression level
long-term dark treatment results in a significant increase in PnAS3 expression level
OsAS2 mRNA content decreases in roots when NH4+ is supplied
PnAS1 gene expression level is slightly increased by NH4+
PnAS3 is up-regulated by Gln but not by NH4+
the beta-adrenergic agonist, ractopamine, increases skeletal muscle expression of asparagine synthetase as part of an integrated stress response gene program
-
the expression of ASN1 and ASN5 genes is upregulated during curing - a senescence-induced process that allows tobacco leaves to dry out
the expressions of tomato mosaic virus coat protein-interacting protein L (IP-L) and asparagine synthetase B (NbAS-B) are continuously induced on TMV-green fluorescent protein (GFP) infection
-
the majority of Gossypium hirsutum asparagine synthases are upregulated in vegetative and reproductive organs, fiber development, and N metabolism
-
transcription factor ATF4 induces asparagine synthetase which results in glutamine-dependent asparagine synthesis from aspartate, in turn asparagine accumulation then suppresses GCN2 and reduces ATF4
-
under long-term light conditions PnAS2 expression decreases significantly in the intermediate region of leaves
the expression of ASN1 and ASN5 genes is upregulated during curing - a senescence-induced process that allows tobacco leaves to dry out
-
the expression of ASN1 and ASN5 genes is upregulated during curing - a senescence-induced process that allows tobacco leaves to dry out
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
refolding of recombinant C-terminally His-tagged enzyme from Escherichia coli strains BL21(DE3) and Rosetta(DE3) inclusion bodies to active proteins, method development using 6-8 M guanidine-HCl, overview. Vmax of the enzyme is lowered about 30% by refolding, but Km values for all three substrates show no substantial change
refolding of recombinant C-terminally His-tagged enzymes from Escherichia coli strains BL21(DE3) and Rosetta(DE3) inclusion bodies to active proteins, method development using 6-8 M guanidine-HCl, overview. Vmax of the enzyme is lowered about 30% by refolding, but Km values for all three substrates show no substantial change
refolding of recombinant C-terminally His-tagged isozyme AsnS1 from Escherichia coli strains BL21(DE3) and Rosetta(DE3) inclusion bodies to active protein, method development using 6-8 M guanidine-HCl, overview. Vmax of the enzyme is lowered about 30% by refolding, but Km values for all three substrates show no substantial change
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
analysis
drug development
medicine
nutrition
-
design of a silencing construct that simultaneously targets the expression of both isoforms StAs1and StAs2. Tubers of the transformed intragenic plants contain up to 20fold reduced levels of free asparagine. This coincides with a small increase in the formation of glutamine and does not affect tuber shape or yield. Heat-processed products derived from the low-asparagine tubers are indistinguishable from their untransformed counterparts in terms of sensory characteristics. However, both French fries and potato chips accumulate as little as 5% of the acrylamide present in wild-type controls
synthesis
-
synthesis of L-asparagine catalyzed by a asparagine synthase coupled with an ATP regeneration system. In order to solve the problem of ATP supply in the reaction process, PPK2-III from Deinococcus ficus is expressed in Escherichia coli Rosetta (DE3), which can use polyphosphate to synthesize ATP. A coupling catalytic reaction system including LsaAS-A, DfiPPK2-III and substrate is then constructed to prepare L-Asn from L-Asp. Biotransformation experiments show that the whole-cell reaction system can obtain higher product yield than free enzyme catalysis, so preparation of L-Asn from L-Asp by whole cell catalysis is optimized under batch modes. In order to reduce substrate inhibition, fed-batch strategy is used to control substrate concentration and 218.26 mmol/l L-Asn is obtained with a yield of 64.19%
agriculture
-
transgenic Arabidopsis thaliana plants that overexpress CaAS1 exhibit enhanced resistance to Pseudomonas syringae pv. tomato DC3000 and Hyaloperonospora arabidopsidis. Increased CaAS1 expression influences early defense responses in diseased leaves, including increased electrolyte leakage, reactive oxygen species and nitric oxide burst. In CaAS1-silenced pepper and/or CaAS1-overexpressing Arabidopsis, CaAS1-dependent changes in asparagine levels correlate with increased susceptibility or defense responses to microbial pathogens, respectively
agriculture
nontransgenic, induced genetic variants in ASN-A2 genes confer significant reductions in free asparagine concentration in wheat grains with no detrimental effects on agronomic or quality traits in field conditions. They have the potential to reduce the acrylamide-forming potential of common wheat
analysis
-
high-performance liquid chromatography assay for Asn synthetase is an extremly sensitive and reliable method for assaying Asn synthetase
analysis
-
a rapid, inexpensive micro assay that can be adapted for large numbers of samples
analysis
mass spectrometry-based procedure for the direct quantification of asparagine synthetase protein concentration in complex sample mixtures. Assay is able to distinguish samples from transformed cell lines that express the enzyme over a wide dynamic range of concentration. The method directly detects asparagine synthetase protein, use in blast samples from patients with acute lymphoblastic leukemia
analysis
development of a sensitive, non-radioactive assay for AsnS, based on incubation of desalted enzyme and substrates and then direct detection of either product asparagine or glutamate by HPLC
drug development
enzyme AS-A is unlikely to be a suitable drug target against Leishmania parasites
drug development
E9BLE1
the absence of an LdASNA homologue from humans and its essentiality for the parasites make LdASNA a drug target
drug development
-
the absence of an LdASNA homologue from humans and its essentiality for the parasites make LdASNA a drug target
-
drug development
-
enzyme AS-A is unlikely to be a suitable drug target against Leishmania parasites
-
medicine
mass spectrometry-based procedure for the direct quantification of asparagine synthetase protein concentration in complex sample mixtures. Assay is able to distinguish samples from transformed cell lines that express the enzyme over a wide dynamic range of concentration. The method directly detects asparagine synthetase protein, use in blast samples from patients with acute lymphoblastic leukemia
medicine
analysis of asparagine synthetase mRNA expression in 19 ovarian cancer cell lines. L-Asparaginase activity is only weakly correlated with asparagine synthetase mRNA expression, while asparagine synthetase protein expression measured by liquid-phase immunoassay exhibits a much stronger correlation
EXTERNAL LINKS (specific for EC-Number 6.3.5.4)
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