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Information on EC 6.1.1.22 - asparagine-tRNA ligase
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6.1.1.22 asparagine-tRNA ligaseSpecify your search results
Word Map
- 6.1.1.22
- aminoacyl-trna
- asnrs
- aspartyl-trna
- malayi
- brugia
- aminoacylation
-
amidotransferase
-
asparaginylation
- asp-trnaasn
- glutaminyl-trna
- gatcabs
- filariasis
-
transamidation
-
nondiscriminating
- glu-trnagln
-
mischarged
-
misacylated
-
asn-trna
- nd-asprs
-
ammonia-dependent
-
anti-ks
- lysyl-trna
- trnaasp
-
histidyl-trna
- medicine
- drug development
The enzyme appears in viruses and cellular organisms
Synonyms
asparaginyl-trna synthetase, nars2, asparagine synthetase a, as-ar, asparagyl-transfer rna synthetase, asparaginyl trna synthetase, asparagine-trna ligase, asparaginyl-transfer rna synthetase, asparagine trna synthetase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AS-AR
AsnRS
Asparagine synthetase A
Asparagine translase
Asparagine--tRNA ligase
Asparaginyl transfer ribonucleic acid synthetase
Asparaginyl transfer RNA synthetase
Asparaginyl-transfer ribonucleate synthetase
asparaginyl-transfer RNA synthetase
Asparaginyl-tRNA synthetase
Asparagyl-transfer RNA synthetase
NARS2
Potentially protective 63 kDa antigen
PYRAB02460
Synthetase, asparaginyl-transfer ribonucleate
additional information
AsnRS
-
-
-
-
Asparagine translase
-
-
-
-
Asparagine--tRNA ligase
-
-
-
-
Asparaginyl transfer ribonucleic acid synthetase
-
-
-
-
Asparaginyl transfer RNA synthetase
-
-
-
-
Asparaginyl-transfer ribonucleate synthetase
-
-
-
-
Asparaginyl-tRNA synthetase
-
-
-
-
Asparaginyl-tRNA synthetase
-
-
Asparagyl-transfer RNA synthetase
-
-
-
-
Potentially protective 63 kDa antigen
-
-
-
-
Synthetase, asparaginyl-transfer ribonucleate
-
-
-
-
additional information
-
the enzyme belongs to the aminoacyl-tRNA synthetase family, AARS
additional information
the enzyme belongs to the class-II aminoacyl-tRNA synthetase family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-asparagine + tRNAAsn = AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
-
-
ATP + L-asparagine + tRNAAsn = AMP + diphosphate + L-asparaginyl-tRNAAsn
mechanism of substrate specificity, structure of substrate binding sites
ATP + L-asparagine + tRNAAsn = AMP + diphosphate + L-asparaginyl-tRNAAsn
substrate binding structure, active site structure, tRNAAsn and amino acid recognition, binding of Asn-AMP induces a conformational change in AsnRS
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Aminoacylation
esterification
Aminoacylation
-
-
-
-
esterification
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
L-asparagine:tRNAAsn ligase (AMP-forming)
-
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CAS REGISTRY NUMBER
COMMENTARY
37211-76-0
-
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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 + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
with the aminoacylation step E + AA + ATP = E(AA-AMP) + diphosphate, and the amidation step E(AA-AMP) + tRNA = E+AA-tRNA + AMP
-
-
r
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
AsnRS structure analysis shows binding of Mg2+-ATP in one active site and L-Asp-beta-NOH adenylate and Mg2+-diphosphate in the other active site. Active-site ordering and rearrangement during activation, overview. The AsnRSBm N-terminal extension binds tRNA, structure, overview
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
tRNAs from calf liver or Saccharomyces cerevisiae
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
with the aminoacylation step E + AA + ATP = E(AA-AMP) + diphosphate, and the amidation step E(AA-AMP) + tRNA = E+AA-tRNA + AMP
-
-
r
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
Staphylococcus aureus FPR3757
-
-
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
substrate specificity
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
calculations of substrate binding and reaction mechanism, overview
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
-
?
additional information
?
-
-
the high level of asparaginyl-tRNA synthetase expression reflects unusual metabolic demands associated with larval maturation
-
-
?
additional information
?
-
-
the parasite Brugia malayi enzyme, in analogy to the human enzyme, induces human leukocyte chemotaxis and activates G-protein-coupled receptors CXCR1 and CXCR2, but not CXCR3, filarial asparaginyl-tRNA synthetase, AsnRS, is known to be an immunodominant antigen that induces strong human immunoglobulin G3 responses and contributes to the development of chronic inflammatory disease such as lymphatic filariasis, overview
-
-
?
additional information
?
-
-
active site and ligand binding structure and mechanism, overview
-
-
?
additional information
?
-
-
human cytoplasmic aminoacyl-tRNA synthetases, which are autoantigens in idiopathic inflammatory myopathies, activate chemokine receptors on T lymphocytes, monocytes, and immature dendritic cells by recruiting immune cells that could induce innate and adaptive immune responses
-
-
?
additional information
?
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-
active site and ligand binding structure and mechanism, overview
-
-
?
additional information
?
-
the enzyme is responsible for catalyzing the specific aminoacylation of tRNAAsn with asparagine, structural basis of the water-assisted asparagine recognition by the enzyme, two water molecules play a key role in the strict recognition of asparagine and the discrimination against aspartic acid by the AsnRS, overview, binding of Asn-AMP induces a conformational change in AsnRS
-
-
?
additional information
?
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-
the enzyme is responsible for catalyzing the specific aminoacylation of tRNAAsn with asparagine, structural basis of the water-assisted asparagine recognition by the enzyme, two water molecules play a key role in the strict recognition of asparagine and the discrimination against aspartic acid by the AsnRS, overview, binding of Asn-AMP induces a conformational change in AsnRS
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-
?
additional information
?
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analysis of the molecular mechanism by molecular dynamics simulations and computational calculations using wild-type andmutant enzymes, overview
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-
?
additional information
?
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acylate Phaseolus aureus tRNA with an efficiency of 68% compared to the Phaseolus aureus enzyme. The tRNA of Vicia faba and Vicia sativa appears to be completely interchangeable
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-
?
additional information
?
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acylate Phaseolus aureus tRNA with an efficiency of 68% compared to the Phaseolus aureus enzyme. The tRNA of Vicia faba and Vicia sativa appears to be completely interchangeable
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-
?
additional information
?
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acylates tRNA of Vicia faba or Vicia sativa with an efficiency of 83% compared to Phaseolus aureus tRNA
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-
?
additional information
?
-
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isoasparagine (with 96% of the efficiency compared to L-Asn), aspartate-3-hydroxamate (with 81% of the efficiency compared to L-Asn) and 3-cyanoalanine (with 36% of the efficiency compared to L-Asn)
-
-
?
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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-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
-
-
?
additional information
?
-
-
the high level of asparaginyl-tRNA synthetase expression reflects unusual metabolic demands associated with larval maturation
-
-
?
additional information
?
-
-
the parasite Brugia malayi enzyme, in analogy to the human enzyme, induces human leukocyte chemotaxis and activates G-protein-coupled receptors CXCR1 and CXCR2, but not CXCR3, filarial asparaginyl-tRNA synthetase, AsnRS, is known to be an immunodominant antigen that induces strong human immunoglobulin G3 responses and contributes to the development of chronic inflammatory disease such as lymphatic filariasis, overview
-
-
?
additional information
?
-
-
human cytoplasmic aminoacyl-tRNA synthetases, which are autoantigens in idiopathic inflammatory myopathies, activate chemokine receptors on T lymphocytes, monocytes, and immature dendritic cells by recruiting immune cells that could induce innate and adaptive immune responses
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
stimulates tRNA esterification with 5% of the efficiency compared to Mg2+
Co2+
-
stimulates ATP-diphosphate exchange with 17% the efficiency compared to Mg2+ and tRNA esterification with 45%
Mg2+
Mn2+
-
stimulates ATP-diphosphate exchange with 30% the efficiency compared to Mg2+ and tRNA esterification with 72% efficiency
Ni2+
-
stimulates tRNA esterification with 15% of the efficiency compared to Mg2+
Mg2+
-
required, optimal concentration is 20 mM in ATP-diphosphate exchange and 12 mM in tRNA esterification, Km: 5.8 mM in ATP-diphosphate exchange, 2.8 in tRNA esterification
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5'-O-[N-(L-asparaginyl)sulfamoyl]adenosine
a non-hydrolysable analogue of asparaginyl adenylate, i.e. Asn-SA
Aspartate 3-hydroxamate
-
Asn-dependent ATP-diphosphate exchange, competitive
NSC35467
-
i.e. 2-(3-methyl-1 lambda5-pyridin-1-yl)-1-(2-phenanthryl)ethanone, 53% inhibition at 0.2 mM
asparaginyl sulfamoyl adenylate
-
i.e. ASNAMS, a non-hydrolyzable analogue of asparaginyl adenylate
asparaginyl sulfamoyl adenylate
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i.e. ASNAMS, a non-hydrolyzable analogue of asparaginyl adenylate
NSC12156
-
i.e. N1,N3-bis(4-amino-2-methyl-6-quinolinyl)-2,2-dimethylmalonamide, 47% inhibition at 0.2 mM, docking mode and binding structure, overview
NSC12156
-
i.e. N1,N3-bis(4-amino-2-methyl-6-quinolinyl)-2,2-dimethylmalonamide, 54% inhibition at 0.2 mM, docking mode and binding structure, overview
NSC363624
-
i.e. 4-(3-(4-amino-6-isopropenyl-1,3,5-triazin-2-yl)phenyl)-6-isopropenyl-1,3,5-triazin-2-ylamine, 50% inhibition at 0.025 mM
NSC363624
-
i.e. 4-(3-(4-amino-6-isopropenyl-1,3,5-triazin-2-yl)phenyl)-6-isopropenyl-1,3,5-triazin-2-ylamine, 80% inhibition at 0.025 mM
rishirilide B
-
CSD code CUQZUJ, isolated from Streptomyces rishiriensis, has antithrombotic activity through selective alpha2-macroglobulin inhibition, leading to the activation of plasmin
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the larger component of MW 80000-90000 requires the addition of an activator for enzyme transfer activity
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Alzheimer Disease
Alzheimer's Disease Risk Variant rs2373115 Regulates GAB2 and NARS2 Expression in Human Brain Tissues.
Ataxia
De Novo and Bi-allelic Pathogenic Variants in NARS1 Cause Neurodevelopmental Delay Due to Toxic Gain-of-Function and Partial Loss-of-Function Effects.
Autoimmune Diseases
Unique N-terminal extension domain of human asparaginyl-tRNA synthetase elicits CCR3-mediated chemokine activity.
Carcinogenesis
Asparaginyl-tRNA Synthetase, a Novel Component of Hippo Signaling, Binds to Salvador and Enhances Yorkie-Mediated Tumorigenesis.
Cataract
Exome Sequencing and Epigenetic Analysis of Twins Who Are Discordant for Congenital Cataract.
Central Nervous System Diseases
The phenotypic variability and natural history of NARS2 associated disease.
Colitis
Nematode asparaginyl-tRNA synthetase resolves intestinal inflammation in mice with T-cell transfer colitis.
Deafness
Mutations of human NARS2, encoding the mitochondrial asparaginyl-tRNA synthetase, cause nonsyndromic deafness and Leigh syndrome.
Diffuse Cerebral Sclerosis of Schilder
Novel variants in the NARS2 gene as a cause of infantile-onset severe epilepsy leading to fatal refractory status epilepticus: case study and literature review.
Diffuse Cerebral Sclerosis of Schilder
PARS2 and NARS2 mutations in infantile-onset neurodegenerative disorder.
Diffuse Cerebral Sclerosis of Schilder
Whole exome sequencing reveals mutations in NARS2 and PARS2, encoding the mitochondrial asparaginyl-tRNA synthetase and prolyl-tRNA synthetase, in patients with Alpers syndrome.
Elephantiasis, Filarial
Brugia malayi Asparaginyl - tRNA Synthetase Stimulates Endothelial Cell Proliferation, Vasodilation and Angiogenesis.
Elephantiasis, Filarial
Expression, localization and alternative function of cytoplasmic asparaginyl-tRNA synthetase in Brugia malayi.
Elephantiasis, Filarial
Immune Response to Brugia malayi Asparaginyl-tRNA Synthetase in Balb/c Mice and Human Clinical Samples of Lymphatic Filariasis.
Elephantiasis, Filarial
Tirandamycins from Streptomyces sp. 17944 Inhibiting the Parasite Brugia malayi Asparagine tRNA Synthetase.
Epilepsy
Lethal NARS2-Related Disorder Associated With Rapidly Progressive Intractable Epilepsy and Global Brain Atrophy.
Epilepsy
Novel variants in the NARS2 gene as a cause of infantile-onset severe epilepsy leading to fatal refractory status epilepticus: case study and literature review.
Filariasis
Virtual screening of traditional Chinese medicine (TCM) database: identification of fragment-like lead molecules for filariasis target asparaginyl-tRNA synthetase.
Hallux Valgus
Novel phenotype and genotype spectrum of NARS2 and literature review of previous mutations.
Hearing Loss
Mutations of human NARS2, encoding the mitochondrial asparaginyl-tRNA synthetase, cause nonsyndromic deafness and Leigh syndrome.
Intellectual Disability
PARS2 and NARS2 mutations in infantile-onset neurodegenerative disorder.
Leigh Disease
Mutations of human NARS2, encoding the mitochondrial asparaginyl-tRNA synthetase, cause nonsyndromic deafness and Leigh syndrome.
Lung Diseases, Interstitial
Anti-KS: identification of autoantibodies to asparaginyl-transfer RNA synthetase associated with interstitial lung disease.
Microcephaly
De Novo and Bi-allelic Pathogenic Variants in NARS1 Cause Neurodevelopmental Delay Due to Toxic Gain-of-Function and Partial Loss-of-Function Effects.
Mitochondrial Diseases
Novel phenotype and genotype spectrum of NARS2 and literature review of previous mutations.
Mitral Valve Prolapse
Novel phenotype and genotype spectrum of NARS2 and literature review of previous mutations.
Myositis
Do tissue levels of autoantigenic aminoacyl-tRNA synthetase predict clinical disease?
Myositis
Histidyl-tRNA synthetase and asparaginyl-tRNA synthetase, autoantigens in myositis, activate chemokine receptors on T lymphocytes and immature dendritic cells.
Neoplasms
Identification of hub genes and key pathways associated with the progression of gynecological cancer.
Neurodegenerative Diseases
Erratum: PARS2 and NARS2 mutations in infantile-onset neurodegenerative disorder.
Neurodegenerative Diseases
Lethal NARS2-Related Disorder Associated With Rapidly Progressive Intractable Epilepsy and Global Brain Atrophy.
Neurodegenerative Diseases
Novel variants in the NARS2 gene as a cause of infantile-onset severe epilepsy leading to fatal refractory status epilepticus: case study and literature review.
Neurodegenerative Diseases
PARS2 and NARS2 mutations in infantile-onset neurodegenerative disorder.
Osteoarthropathy, Secondary Hypertrophic
Novel phenotype and genotype spectrum of NARS2 and literature review of previous mutations.
Paraplegia
Novel variants in the NARS2 gene as a cause of infantile-onset severe epilepsy leading to fatal refractory status epilepticus: case study and literature review.
Peripheral Nervous System Diseases
De Novo and Bi-allelic Pathogenic Variants in NARS1 Cause Neurodevelopmental Delay Due to Toxic Gain-of-Function and Partial Loss-of-Function Effects.
Seizures
De Novo and Bi-allelic Pathogenic Variants in NARS1 Cause Neurodevelopmental Delay Due to Toxic Gain-of-Function and Partial Loss-of-Function Effects.
Status Epilepticus
Novel variants in the NARS2 gene as a cause of infantile-onset severe epilepsy leading to fatal refractory status epilepticus: case study and literature review.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE