Information on EC 6.1.1.22 - asparagine-tRNA ligase and Organism(s) Homo sapiens and UniProt Accession O43776

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This record set is specific for:
Homo sapiens
UNIPROT: O43776


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea


The taxonomic range for the selected organisms is: Homo sapiens

EC NUMBER
COMMENTARY hide
6.1.1.22
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RECOMMENDED NAME
GeneOntology No.
asparagine-tRNA ligase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Aminoacylation
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esterification
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Aminoacylation
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esterification
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
tRNA charging
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aspartate and asparagine metabolism
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Aminoacyl-tRNA biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
L-asparagine:tRNAAsn ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
37211-76-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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mutations of the mitochondrial asparaginyl-tRNA synthetase cause nonsyndromic deafness and leigh syndrome
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
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
?
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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 hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
asparaginyl sulfamoyl adenylate
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i.e. ASNAMS, a non-hydrolyzable analogue of asparaginyl adenylate
LCM01
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long side-chain derivative of variolin B
LCM02
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long side-chain derivative of variolin B
NSC114691
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i.e. 8-chloro-3-(hydroxy(oxido)amino)-6-phenanthridinol
NSC12156
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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
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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
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additional information
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no inhibition by NSC35467 at 0.2 mM
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0017
asparaginyl sulfamoyl adenylate
Homo sapiens;
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0.5
LCM01
Homo sapiens;
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above
1
LCM02
Homo sapiens;
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above
0.05
NSC114691
Homo sapiens;
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Manually annotated by BRENDA team
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primary
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
Homo sapiens;
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 50000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
molecular modeling of structure
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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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N381S
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mutation decreases NARS2 protein levels in patient fibroblasts and also disrupts dimerization of NARS2
Q274H
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the mutation leads to defective oxidative phosphorylation activity involving complex I and IV
Y323*/N381S
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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
Y323DEL/N381S
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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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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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