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Information on EC 6.3.5.4 - asparagine synthase (glutamine-hydrolysing) and Organism(s) Oryza sativa and UniProt Accession Q43011

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EC Tree
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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Oryza sativa
UNIPROT: Q43011
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The taxonomic range for the selected organisms is: Oryza sativa
The enzyme appears in selected viruses and cellular organisms
Synonyms
l-asparaginase, asnase, asparagine synthetase b, glutamine-dependent asparagine synthetase, taasn2, pvas2, osas1, taasn1, ste10, glutamine-dependent amidotransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AS-B
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AsnB
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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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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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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
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
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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methionine sulfoximine completely inhibits the NH4+-induced accumulation of AS protein, but not the glutamine-induced accumulation
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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AS expression in roots is induced by NH4+ or glutamine, but not by nitrate, glutamate, aspartate and asparagine
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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high content of AS in grains in the middle stage of ripening, in vascular tissues
Manually annotated by BRENDA team
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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
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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during the ripening of the spikelets AS contents increases during the first 21 days after flowering, then declines rapidly
Manually annotated by BRENDA team
additional information
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organ and cellular localization
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66000
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x * 66000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 66000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant fusion protein consisting of the 42 kDa N-terminal region of AS and a 17 kDa tagged-region from pET32a(+) expression plasmid
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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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kawachi, T.; Sueyoshi, K.; Nakajima, A.; Yamagata, H.; Sugimoto, T.; Oji, Y.
Expression of asparagine synthetase in rice (Oryza sativa) roots in response to nitrogen
Physiol. Plant.
114
41-46
2002
Oryza sativa
Manually annotated by BRENDA team
Nakano, K.; Suzuki, T.; Hayakawa, T.; Yamaya, T.
Organ and cellular localization of asparagine synthetase in rice plants
Plant Cell Physiol.
41
874-880
2000
Oryza sativa
Manually annotated by BRENDA team