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Information on EC 6.3.5.4 - asparagine synthase (glutamine-hydrolysing)
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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 beta-aspartyl-AMP intermediate and its subsequent reaction with ammonia. The ammonia released is channeled to the other active site to yield asparagine .
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Word Map
- 6.3.5.4
- leukemia
- lymphoblastic
- children
- vincristine
-
remission
- lymphoma
- l-asparagine
- methotrexate
- prednisone
- lymphocytic
- marrow
- thrombosis
-
pediatric
- cyclophosphamide
- erwinia
- doxorubicin
- cr
-
consolidation
-
relapsed
- daunorubicin
- etoposide
- dexamethasone
-
prophylaxis
- glutaminase
-
intrathecal
- chrysanthemi
-
thromboembolic
-
reinduction
-
extranodal
- cytarabine
-
l-aspartic
-
non-hodgkin
- carotovora
-
event-free
- ifosfamide
-
antileukemic
-
pegylated
- antithrombin
-
arabinoside
- 6-mercaptopurine
-
multiagent
- pseudocysts
- medicine
- analysis
- drug development
-
myelosuppression
- lymphosarcoma
- daunomycin
- nutrition
- epipodophyllotoxins
-
b-lineage
- hypofibrinogenemia
- agriculture
-
smile
- teniposide
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
AS, AS-A, AS-B, AS1, ASN3, AsnA, ASNase, AsnB, ASNS, AsnS1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AS
AS-A
AS-B
AS1
ASN3
AsnA
AsnB
ASNS
AsnS1
AsnS2
Asparagine synthetase
Asparagine synthetase (glutamine hydrolyzing)
-
-
-
-
Asparagine synthetase (glutamine)
-
-
-
-
Asparagine synthetase (glutamine-hydrolysing)
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-
-
-
Asparagine synthetase A
Asparagine synthetase B
At5g10240
bacterial type asparagine synthetase A
Glutamine-dependent asparagine synthetase
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-
-
-
L-Asparagine synthetase
-
-
-
-
LDBPK_300470
LiAS-A
Synthetase, Asn (glutamine)
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-
-
-
TS11 cell cycle control protein
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-
-
-
additional information
AS-B
-
-
-
-
AsnB
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-
-
-
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
overall ping-pong mechanism; ping-pong reaction mechanism. Glutamine is the first substrate to bind to the enzyme and Asn is the last product released
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-
-
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
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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
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ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate
NH4+ is bound to the enzyme followed by MgATP causing Asn release
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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
Arg325 is involved in stabilization of a pentacovalent intermediate leading to the formation of beta-aspartyl-AMP
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ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate
mechanism
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ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate
reaction mechanism, structure-function relationship
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ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate
reaction mechanism, structure-function relationship
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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
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
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-
carboxylic
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + cysteine sulfinic acid
AMP + diphosphate + cysteine sulfinic acid
-
-
-
?
dATP + L-Asp + L-Gln
dAMP + diphosphate + Asn + Glu
-
utilized at a similar rate as ATP
-
-
-
dATP + L-Asp + NH3
dAMP + diphosphate + Asn
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utilized at a similar rate as ATP
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-
-
L-Glutamic acid gamma-monohydroxamate + H2O
Hydroxylamine + Glu
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-
-
-
-
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
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-
-
-
-
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
-
-
-
-
-
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
-
-
-
-
-
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
-
the basic region leucine zipper protein ATF5, a transcriptional activator, stimulates asparagine promoter/reporter gene transcription via the nutrient-sensing response unit
-
-
?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
-
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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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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-
-
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-
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
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-
-
-
-
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
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-
-
-
-
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
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TaASN1 is dramatically induced by salinity, osmotic stress and exogenous abscisic acid
-
-
?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
-
TaASN2 transcripts are very low in all detected tissues and conditions and are only slightly induced by abscisic acid in roots
-
-
?
ATP + L-Asp + L-Gln
AMP + diphosphate + L-Asn + L-Glu
-
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
-
-
-
?
ATP + L-Asp + NH2OH
AMP + diphosphate + beta-aspartylhydroxamate
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-
-
-
ATP + L-Asp + NH3
AMP + diphosphate + Asn
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30% of the activity relative to Gln
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ATP + L-Asp + NH3
AMP + diphosphate + Asn
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the ratio of Gln-dependent to NH4+-dependent activity is 2.5
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ATP + L-Asp + NH3
AMP + diphosphate + Asn
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85% of the activity relative to Gln
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ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
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-
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
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-
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
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-
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
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-
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
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-
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
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-
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
ATP-dependent, mechanism including an enzyme-ATP-Asp-Gln quarternary complex, AS-B structure, two active sites
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ir
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
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glutamine is the in vivo nitrogen source
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
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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
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transfers the amide group of Gln to Asp
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?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
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-
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
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
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-
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
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-
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
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-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
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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
-
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
-
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
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
-
-
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
-
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
-
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
-
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
-
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
-
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
-
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
-
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
-
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
also reaction of EC 6.3.1.1
-
-
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
also reaction of EC 6.3.1.1
-
-
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
-
-
-
?
GTP + L-Asp + L-Gln
GMP + diphosphate + Asn + Glu
-
15% of the activity relative to ATP
-
-
-
GTP + L-Asp + L-Gln
GMP + diphosphate + Asn + Glu
-
5.6% of the activity relative to ATP
-
-
-
additional information
?
-
-
physiological roles for asnB in vegetative cells and for asnO in sporulating cells, asnB may be the main gene involved in asparagine biosynthesis
-
?
additional information
?
-
-
physiological roles for asnB in vegetative cells and for asnO in sporulating cells, asnB may be the main gene involved in asparagine biosynthesis
-
?
additional information
?
-
-
comprehensive mechanism has been proposed through which either Gln or NH3 can provide nitrogen for Asn production from Asp
-
-
-
additional information
?
-
-
the N74D As-B mutant exhibits very low glutaminase activity
-
-
-
additional information
?
-
-
enzyme is extremly selective, being able to discriminate between metabolites that have similar structures to Asp
-
-
-
additional information
?
-
-
major biosynthetic pathway for asparagine, AS gene expression is down-regulated by light
-
?
additional information
?
-
-
primary enzyme responsible for asparagine synthesis
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
upregulation of asparagine synthetase fails to avert cell cycle arrest induced by L-asparaginase in TEL/AML1-positive leukaemic cells
-
-
-
additional information
?
-
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
-
?
additional information
?
-
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
-
?
additional information
?
-
under normal growth conditions HvAS2 acts as a housekeeping gene in the leaves
-
?
additional information
?
-
under normal growth conditions HvAS2 acts as a housekeeping gene in the leaves
-
?
additional information
?
-
-
Gln-dependent enzyme is essential for Asn synthesis when the nitrogen source is growth rate limiting
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
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-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
primary enzyme responsible for asparagine synthesis
-
?
additional information
?
-
-
Asn, the end product of the mass action of symbiotic NH4+ synthesis, is the principal N-transport-compound of many temperate legumes
-
-
-
additional information
?
-
-
glutamine or glutamine-derived metabolites regulate AS expression in roots
-
?
additional information
?
-
-
nitrogen metabolism, asparagine synthesis
-
?
additional information
?
-
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.
-
-
-
additional information
?
-
-
primary enzyme responsible for asparagine synthesis
-
?
additional information
?
-
-
the synthesis of Asn in mammalian tissues proceeds through the intermediate beta-aspartyladenylate
-
-
-
additional information
?
-
-
importance of asparagine synthetase in cell proliferation
-
-
-
additional information
?
-
the enzyme continues to produce glutamate even when the synthesis of asparagine has ceased due to a lack of aspartate
-
-
-
additional information
?
-
the enzyme continues to produce glutamate even when the synthesis of asparagine has ceased due to a lack of aspartate
-
-
-
additional information
?
-
-
the enzyme continues to produce glutamate even when the synthesis of asparagine has ceased due to a lack of aspartate
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-Asp + L-Gln
AMP + diphosphate + L-Asn + L-Glu
-
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
-
-
?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
-
the basic region leucine zipper protein ATF5, a transcriptional activator, stimulates asparagine promoter/reporter gene transcription via the nutrient-sensing response unit
-
-
?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
-
TaASN1 is dramatically induced by salinity, osmotic stress and exogenous abscisic acid
-
-
?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
-
TaASN2 transcripts are very low in all detected tissues and conditions and are only slightly induced by abscisic acid in roots
-
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
P22106
-
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
glutamine is the in vivo nitrogen source
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
?
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
-
the enzyme might play a functional role in nitrogen translocation from root to aerial organs in Phaseolus vulgaris
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Q9LFU1
-
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Q9LFU1
-
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
Q2L9S5
-
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
-
-
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
E9BLE1
-
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
E9BLE1
-
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
A4I213
-
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
A4I213
-
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
A9XS73
-
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
D9IXC8, E7EAQ2
-
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
A0A1D5VHV8, A0A1D5YL35
-
-
-
?
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
B4FFJ0, B5U8J7, B5U8J8, B5U8J9
-
-
-
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
P22106
-
-
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
-
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
-
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
-
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
-
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
-
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
-
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
-
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
-
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
E9BLE1
also reaction of EC 6.3.1.1
-
-
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
E9BLE1
also reaction of EC 6.3.1.1
-
-
?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
A4I213
-
-
-
?
additional information
?
-
-
physiological roles for asnB in vegetative cells and for asnO in sporulating cells, asnB may be the main gene involved in asparagine biosynthesis
-
?
additional information
?
-
-
physiological roles for asnB in vegetative cells and for asnO in sporulating cells, asnB may be the main gene involved in asparagine biosynthesis
-
?
additional information
?
-
-
comprehensive mechanism has been proposed through which either Gln or NH3 can provide nitrogen for Asn production from Asp
-
-
-
additional information
?
-
-
major biosynthetic pathway for asparagine, AS gene expression is down-regulated by light
-
?
additional information
?
-
-
primary enzyme responsible for asparagine synthesis
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
Q9LKQ9
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
-
-
-
additional information
?
-
Q9SP19
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
-
-
-
additional information
?
-
Q9SP20
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
-
-
-
additional information
?
-
-
upregulation of asparagine synthetase fails to avert cell cycle arrest induced by L-asparaginase in TEL/AML1-positive leukaemic cells
-
-
-
additional information
?
-
Q84LA5
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
-
?
additional information
?
-
Q93XP9
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
-
?
additional information
?
-
Q84LA5
under normal growth conditions HvAS2 acts as a housekeeping gene in the leaves
-
?
additional information
?
-
Q93XP9
under normal growth conditions HvAS2 acts as a housekeeping gene in the leaves
-
?
additional information
?
-
-
Gln-dependent enzyme is essential for Asn synthesis when the nitrogen source is growth rate limiting
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
primary enzyme responsible for asparagine synthesis
-
?
additional information
?
-
-
Asn, the end product of the mass action of symbiotic NH4+ synthesis, is the principal N-transport-compound of many temperate legumes
-
-
-
additional information
?
-
-
glutamine or glutamine-derived metabolites regulate AS expression in roots
-
?
additional information
?
-
-
nitrogen metabolism, asparagine synthesis
-
?
additional information
?
-
A9XS73
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.
-
-
-
additional information
?
-
-
primary enzyme responsible for asparagine synthesis
-
?
additional information
?
-
-
importance of asparagine synthetase in cell proliferation
-
-
-
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+
Mg2+
-
divalent metal ion required, Mg2+ more effective than Mn2+; Km: 23.7
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
-
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
-
enzyme from fetal liver extracts is significantly inhibited when combined with adult liver or tumor extracts
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
1 mM aminooxyacetic acid increases AS activity in crude extract by inhibiting various aminotransferases and preventing the assimilation of aspartate into the TCA cycle
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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, glutamine-dependent activity, pH 8.0, 37°C; mutant E348D, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37°C
0.03
ATP
-
mutant E348D, ammonia-dependent activity, pH 8.0, 37°C; 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, 22°C; pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn3
0.1 - 1
ATP
pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn1
0.1
ATP
-
wild-type, glutamine-dependent activity, pH 8.0, 37°C; wild-type, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37°C
0.11
ATP
-
wild-type, ammonia-dependent activity, pH 8.0, 37°C; wild-type, synthetase activity, ammonia-dependent activity, 100 mM NH4Cl, pH 8.0, 37°C
0.125
ATP
pH 7.6, 22°C; pH 7.6, temperature not specified in the publication, recombinant nontagged isozyme soluble ZmAsn2
0.128
ATP
pH 7.6, 22°C; pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn2; pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn4
0.13
L-Asp
-
mutant E348D, glutamine-dependent activity, pH 8.0, 37°C; mutant E348D, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37°C
0.23
L-Asp
-
mutant E348D, ammonia-dependent activity, pH 8.0, 37°C; mutant E348D, synthetase activity, ammonia-dependent activity, 100 mM NH4Cl, pH 8.0, 37°C
0.58
L-Asp
-
wild-type, glutamine-dependent activity, pH 8.0, 37°C; wild-type, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37°C
1.2
L-Asp
-
wild-type, ammonia-dependent activity, pH 8.0, 37°C; 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; 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
-
Km-values of mutant enzymes R30A, R30K, N74A, N74Q, and N79A
-
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
-
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; the AsnS isozymes are kinetically distinct with substantial differences in Km (Gln) and Vmax values, overview. None of the enzymes has cooperative enzyme kinetics; the AsnS isozymes are kinetically distinct with substantial differences in Km (Gln) and Vmax values, overview. None of the enzymes has cooperative enzyme kinetics; 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; the AsnS isozymes are kinetically distinct with substantial differences in Km (Gln) and Vmax values, overview. None of the enzymes has cooperative enzyme kinetics; the AsnS isozymes are kinetically distinct with substantial differences in Km (Gln) and Vmax values, overview. None of the enzymes has cooperative enzyme kinetics; 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; the AsnS isozymes are kinetically distinct with substantial differences in Km (Gln) and Vmax values, overview. None of the enzymes has cooperative enzyme kinetics; the AsnS isozymes are kinetically distinct with substantial differences in Km (Gln) and Vmax values, overview. None of the enzymes has cooperative enzyme kinetics; 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; the AsnS isozymes are kinetically distinct with substantial differences in Km (Gln) and Vmax values, overview. None of the enzymes has cooperative enzyme kinetics; the AsnS isozymes are kinetically distinct with substantial differences in Km (Gln) and Vmax values, overview. None of the enzymes has cooperative enzyme kinetics; 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
-
additional information
additional information
-
biphasic kinetic, linear portion near 0.5
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.43
ATP
-
mutant E348D, ammonia-dependent activity, pH 8.0, 37°C; mutant E348D, synthetase activity, ammonia-dependent activity, 100 mM NH4Cl, pH 8.0, 37°C
0.51
ATP
-
mutant E348D, glutamine-dependent activity, pH 8.0, 37°C; mutant E348D, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37°C
0.9
ATP
-
wild-type, glutamine-dependent activity, pH 8.0, 37°C; wild-type, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37°C
0.96
ATP
-
wild-type, ammonia-dependent activity, pH 8.0, 37°C; wild-type, synthetase activity, ammonia-dependent activity, 100 mM NH4Cl, pH 8.0, 37°C
0.3
L-Asp
-
mutant E348D, ammonia-dependent activity, pH 8.0, 37°C; mutant E348D, synthetase activity, ammonia-dependent activity, 100 mM NH4Cl, pH 8.0, 37°C
0.45
L-Asp
-
mutant E348D, glutamine-dependent activity, pH 8.0, 37°C; mutant E348D, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37°C
0.67
L-Asp
-
wild-type, glutamine-dependent activity, pH 8.0, 37°C; wild-type, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37°C
0.75
L-Asp
-
wild-type, ammonia-dependent activity, pH 8.0, 37°C; 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
3 - 6
L-glutamine
-
glutaminase activity; glutamine-dependent synthetase activity
6.08
L-glutamine
-
glutaminase activity in the presence of ATP; glutamine dependent asparagine synthetase activity
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8.7
ATP
-
wild-type, ammonia-dependent activity, pH 8.0, 37°C; wild-type, synthetase activity, ammonia-dependent activity, 100 mM NH4Cl, pH 8.0, 37°C
9
ATP
-
wild-type, glutamine-dependent activity, pH 8.0, 37°C; wild-type, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37°C
14.3
ATP
-
mutant E348D, ammonia-dependent activity, pH 8.0, 37°C; mutant E348D, synthetase activity, ammonia-dependent activity, 100 mM NH4Cl, pH 8.0, 37°C
39.2
ATP
-
mutant E348D, glutamine-dependent activity, pH 8.0, 37°C; mutant E348D, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37°C
0.63
L-Asp
-
wild-type, ammonia-dependent activity, pH 8.0, 37°C; wild-type, synthetase activity, ammonia-dependent activity, 100 mM NH4Cl, pH 8.0, 37°C
1.2
L-Asp
-
wild-type, glutamine-dependent activity, pH 8.0, 37°C; wild-type, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37°C
1.3
L-Asp
-
mutant E348D, ammonia-dependent activity, pH 8.0, 37°C; 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
1.3
glutamate
Zea mays
B4FFJ0, B5U8J7, B5U8J8, B5U8J9
pH 7.6, 22°C; pH 7.6, 22°C; pH 7.6, 22°C
1.1
L-asparagine
Zea mays
B4FFJ0, B5U8J7, B5U8J8, B5U8J9
pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn1
1.3
L-asparagine
Zea mays
B4FFJ0, B5U8J7, B5U8J8, B5U8J9
pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAs4
1.4
L-asparagine
Zea mays
B4FFJ0, B5U8J7, B5U8J8, B5U8J9
pH 7.6, temperature not specified in the publication, recombinant nontagged soluble isozyme ZmAsn2
1.5
L-asparagine
Zea mays
B4FFJ0, B5U8J7, B5U8J8, B5U8J9
pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn3
1.2
L-glutamate
Zea mays
B4FFJ0, B5U8J7, B5U8J8, B5U8J9
pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn4
1.3
L-glutamate
Zea mays
B4FFJ0, B5U8J7, B5U8J8, B5U8J9
pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn1; pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn3; 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
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
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
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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
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