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Information on EC 6.3.5.4 - asparagine synthase (glutamine-hydrolysing) and Organism(s) Homo sapiens and UniProt Accession P08243

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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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This record set is specific for:
Homo sapiens
UNIPROT: P08243
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The taxonomic range for the selected organisms is: Homo sapiens
Synonyms
AS, AS-A, AS-B, AS1, ASN3, AsnA, ASNase, AsnB, ASNS, AsnS1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AS-B
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ASNase
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AsnB
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Asparagine synthetase
Asparagine synthetase (glutamine hydrolyzing)
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Asparagine synthetase (glutamine)
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Asparagine synthetase (glutamine-hydrolysing)
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Asparagine synthetase B
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asparagine synthetase, glutamine-dependent
247
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Glutamine-dependent asparagine synthetase
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L-Asparagine synthetase
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Synthetase, Asn (glutamine)
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TS11 cell cycle control protein
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate
show the reaction diagram
reaction mechanism, structure-function relationship
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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].
CAS REGISTRY NUMBER
COMMENTARY hide
37318-72-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
show the reaction diagram
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?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
show the reaction diagram
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?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
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?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
show the reaction diagram
ATP + L-Asp + NH3
AMP + diphosphate + Asn
show the reaction diagram
ATP + L-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
show the reaction diagram
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
show the reaction diagram
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?
ATP + L-aspartate + NH3
AMP + diphosphate + L-asparagine
show the reaction diagram
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?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
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?
ATP + L-Asp + L-Gln
AMP + diphosphate + Asn + Glu
show the reaction diagram
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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-aspartate + L-glutamine
AMP + diphosphate + L-asparagine + L-glutamate
show the reaction diagram
ATP + L-aspartate + L-glutamine + H2O
AMP + diphosphate + L-asparagine + L-glutamate
show the reaction diagram
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additional information
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upregulation of asparagine synthetase fails to avert cell cycle arrest induced by L-asparaginase in TEL/AML1-positive leukaemic cells
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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required
Mg2+
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required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6-diazo-5-oxo-L-norleucine
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loss of Gln-dependent reactions, but no effect on ATP binding as measured during amminoa-dependent Asn synthesis
8-N3ATP
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loss of NH4+-dependent Asn synthesis, but no effect on the glutaminase activity
beta-asparaginyladenylate
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Gln
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0.4-2.0 mM, inhibits the ammonia-dependent production of Asn
mupirocin
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phosmidosine
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sulfoximine adenylate
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most potent inhibitor
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Phytohemagglutinin
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