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ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate
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
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
overall ping-pong mechanism
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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
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
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
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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
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
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
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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ATP + cysteine sulfinic acid
AMP + diphosphate + cysteine sulfinic acid
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ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
ATP + L-Asp + L-Gln
AMP + diphosphate + L-Asn + L-Glu
ATP + L-Asp + L-Gln + H2O
AMP + diphosphate + L-Asn + L-Glu
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ATP + L-Asp + NH2OH
AMP + diphosphate + beta-aspartylhydroxamate
ATP + L-Asp + NH3
AMP + diphosphate + Asn
ATP + L-Asp + NH3
AMP + diphosphate + L-Asn
ATP + L-aspartate + L-glutamine
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
CTP + L-Asp + L-Gln
CMP + diphosphate + Asn + Glu
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weak activity
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dATP + L-Asp + L-Gln
dAMP + diphosphate + Asn + Glu
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utilized at a similar rate as ATP
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dATP + L-Asp + NH3
dAMP + diphosphate + Asn
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utilized at a similar rate as ATP
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GTP + L-Asp + L-Gln
GMP + diphosphate + Asn + Glu
L-Glutamic acid gamma-monohydroxamate + H2O
Hydroxylamine + Glu
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L-glutamine
L-glutamate + NH3
L-glutamine + H2O
L-glutamate + NH3
UTP + L-Asp + L-Gln
UMP + diphosphate + Asn + Glu
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weak activity
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additional information
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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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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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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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ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
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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
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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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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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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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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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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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ir
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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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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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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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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
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ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
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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 + 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 + L-Asn + L-Glu
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ATP + L-Asp + L-Gln
AMP + diphosphate + L-Asn + L-Glu
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ATP + L-Asp + L-Gln
AMP + diphosphate + L-Asn + L-Glu
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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
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ATP + L-Asp + NH2OH

AMP + diphosphate + beta-aspartylhydroxamate
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ATP + L-Asp + NH2OH
AMP + diphosphate + beta-aspartylhydroxamate
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ATP + L-Asp + NH2OH
AMP + diphosphate + beta-aspartylhydroxamate
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ATP + L-Asp + NH2OH
AMP + diphosphate + beta-aspartylhydroxamate
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ATP + L-Asp + NH2OH
AMP + diphosphate + beta-aspartylhydroxamate
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ATP + L-Asp + NH2OH
AMP + diphosphate + beta-aspartylhydroxamate
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ATP + L-Asp + NH3

AMP + diphosphate + Asn
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NH4+
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ATP + L-Asp + NH3
AMP + diphosphate + Asn
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ATP + L-Asp + NH3
AMP + diphosphate + Asn
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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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ATP + L-Asp + NH3
AMP + diphosphate + Asn
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NH4+
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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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ATP + L-Asp + NH3
AMP + diphosphate + Asn
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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-Asp + NH3
AMP + diphosphate + Asn
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ATP + L-Asp + NH3

AMP + diphosphate + L-Asn
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ATP + L-Asp + NH3
AMP + diphosphate + L-Asn
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ATP + L-Asp + NH3
AMP + diphosphate + L-Asn
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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
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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-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
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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
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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-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
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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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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
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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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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
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ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
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ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
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