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Information on EC 6.3.5.4 - asparagine synthase (glutamine-hydrolysing) and Organism(s) Arabidopsis thaliana and UniProt Accession Q9LFU1

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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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Arabidopsis thaliana
UNIPROT: Q9LFU1
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Synonyms
l-asparaginase, asnase, asparagine synthetase b, glutamine-dependent asparagine synthetase, taasn2, pvas2, taasn1, osas1, glutamine-dependent amidotransferase, ste10, 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 2
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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 + H2O
AMP + diphosphate + L-asparagine + L-glutamate
show the reaction diagram
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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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-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
rosette leaves, of 35-day-old plants
Manually annotated by BRENDA team
fourth siliques numbered from the top of 35-day-old plants
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
phylogenetic analysis has grouped ASN1 in dicot-subclass I while ASN2 and ASN3 are placed in dicot-subclass II
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
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
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ASNS3_ARATH
578
0
65227
Swiss-Prot
other Location (Reliability: 5)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 65200, about, sequence calculation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ASN3, real-time quantitative RT-PCR isozyme expression analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Maaroufi-Dguimi, H.; Debouba, M.; Gaufichon, L.; Clement, G.; Gouia, H.; Hajjaji, A.; Suzuki, A.
An Arabidopsis mutant disrupted in ASN2 encoding asparagine synthetase 2 exhibits low salt stress tolerance
Plant Physiol. Biochem.
49
623-628
2011
Arabidopsis thaliana
Manually annotated by BRENDA team
Gaufichon, L.; Marmagne, A.; Yoneyama, T.; Hase, T.; Clement, G.; Trassaert, M.; Xu, X.; Shakibaei, M.; Najihi, A.; Suzuki, A.
Impact of the disruption of ASN3-encoding asparagine synthetase on Arabidopsis development
Agronomy
6
12
2016
Arabidopsis thaliana (Q9LFU1), Arabidopsis thaliana Col-0 (Q9LFU1)
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Manually annotated by BRENDA team