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Information on EC 6.1.1.22 - asparagine-tRNA ligase and Organism(s) Homo sapiens and UniProt Accession Q96I59

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Homo sapiens
UNIPROT: Q96I59 not found.
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected 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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Asparaginyl-tRNA synthetase
-
AsnRS
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
Synthetase, asparaginyl-transfer ribonucleate
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
Aminoacylation
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-asparagine:tRNAAsn ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
37211-76-0
-
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-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
show the reaction diagram
-
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
show the reaction diagram
additional information
?
-
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-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
show the reaction diagram
-
-
-
?
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
show the reaction diagram
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
asparaginyl sulfamoyl adenylate
-
i.e. ASNAMS, a non-hydrolyzable analogue of asparaginyl adenylate
LCM01
-
long side-chain derivative of variolin B
LCM02
-
long side-chain derivative of variolin B
NSC114691
-
i.e. 8-chloro-3-(hydroxy(oxido)amino)-6-phenanthridinol
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, 80% inhibition at 0.025 mM
rishirilide B
-
-
additional information
-
no inhibition by NSC35467 at 0.2 mM
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0017
asparaginyl sulfamoyl adenylate
Homo sapiens
-
-
0.4
human angiotensinogen
Homo sapiens
-
-
-
0.5
LCM01
Homo sapiens
-
above
1
LCM02
Homo sapiens
-
above
0.05
NSC114691
Homo sapiens
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
mutations of the mitochondrial asparaginyl-tRNA synthetase cause nonsyndromic deafness and leigh syndrome
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SYNM_HUMAN
477
0
54090
Swiss-Prot
Mitochondrion (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 50000, SDS-PAGE
dimer
coimmunoprecipitation studies of wild-type and mutant
dimer
-
structure analysis using crystal structure
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular modeling of structure
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N381S
mutation decreases NARS2 protein levels in patient fibroblasts and also disrupts dimerization of NARS2
Q274H
the mutation leads to defective oxidative phosphorylation activity involving complex I and IV
V213F
mutation is the underlying cause of nonsyndromic hearing loss, mutation has no effect on oligomerization
Y323*/N381S
mutation results in mitochondrial respiratory chain deficiency and Leigh syndrome, a neurodegenerative disease characterized by symmetric, bilateral lesions in the basal ganglia, thalamus, and brain stem
V213F
the mutation causes nonsyndromic hearing loss
Y323DEL/N381S
the mutations result in mitochondrial respiratory chain deficiency and Leigh syndrome which is a neurodegenerative disease characterized by symmetric, bilateral lesions in the basal ganglia, thalamus, and brain stem
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, functional expression in Escherichia coli
DNA sequence determination and phylogenetic analysis
expression in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
homozygous missense mutation c.822G>C affects the 3 splice site of exon 7, leading to skipping of the whole exon 7 and a part of exon 8 in the NARS2 mRNA. Upon expression in fibroblasts a specific decrease in the amount of charged mt-tRNAAsn is found. Mutation was found in in two siblings born to consanguineous parents, one presenting with mild intellectual disability and epilepsy in childhood, whereas the other had severe myopathy
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shiba, K.; Motegi, H.; Yoshida, M.; Noda, T.
Human asparaginyl-tRNA synthetase: molecular cloning and the inference of the evolutionary history of Asx-tRNA synthetase family
Nucleic Acids Res.
26
5045-5051
1998
Homo sapiens (O43776), Homo sapiens
Manually annotated by BRENDA team
Beaulande, M.; Tarbouriech, N.; Hartlein, M.
Human cytosolic asparaginyl-tRNA synthetase: cDNA sequence, functional expression in Escherichia coli and characterization as human autoantigen
Nucleic Acids Res.
26
521-524
1998
Homo sapiens (O43776), Homo sapiens
Manually annotated by BRENDA team
Sukuru, S.C.; Crepin, T.; Milev, Y.; Marsh, L.C.; Hill, J.B.; Anderson, R.J.; Morris, J.C.; Rohatgi, A.; O'Mahony, G.; Groetli, M.; Danel, F.; Page, M.G.; Haertlein, M.; Cusack, S.; Kron, M.A.; Kuhn, L.A.
Discovering new classes of Brugia malayi asparaginyl-tRNA synthetase inhibitors and relating specificity to conformational change
J. Comput. Aided Mol. Des.
20
159-178
2006
Brugia malayi, Homo sapiens
Manually annotated by BRENDA team
Ramirez, B.L.; Howard, O.M.; Dong, H.F.; Edamatsu, T.; Gao, P.; Hartlein, M.; Kron, M.
Brugia malayi asparaginyl-transfer RNA synthetase induces chemotaxis of human leukocytes and activates G-protein-coupled receptors CXCR1 and CXCR2
J. Infect. Dis.
193
1164-1171
2006
Brugia malayi, Homo sapiens
Manually annotated by BRENDA team
Vanlander, A.V.; Menten, B.; Smet, J.; De Meirleir, L.; Sante, T.; De Paepe, B.; Seneca, S.; Pearce, S.F.; Powell, C.A.; Vergult, S.; Michotte, A.; De Latter, E.; Vantomme, L.; Minczuk, M.; Van Coster, R.
Two siblings with homozygous pathogenic splice-site variant in mitochondrial asparaginyl-tRNA synthetase (NARS2)
Hum. Mutat.
36
222-231
2015
Homo sapiens (Q96I59)
Manually annotated by BRENDA team
Simon, M.; Richard, E.M.; Wang, X.; Shahzad, M.; Huang, V.H.; Qaiser, T.A.; Potluri, P.; Mahl, S.E.; Davila, A.; Nazli, S.; Hancock, S.; Yu, M.; Gargus, J.; Chang, R.; Al-Sheqaih, N.; Newman, W.G.; Abdenur, J.; Starr, A.; Hegde, R.; Dorn, T.; Busch, A.; Park, E.; Wu, J.; Schwenzer, H.; Flierl, A.; Florentz, C.
Mutations of human NARS2, encoding the mitochondrial asparaginyl-tRNA synthetase, cause nonsyndromic deafness and Leigh syndrome
PLoS Genet.
11
e1005097
2015
Homo sapiens, Homo sapiens (Q96I59)
Manually annotated by BRENDA team