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6.1.1.22: asparagine-tRNA ligase

This is an abbreviated version!
For detailed information about asparagine-tRNA ligase, go to the full flat file.

Word Map on EC 6.1.1.22

Reaction

ATP
+
L-asparagine
 +
tRNAAsn
=
AMP
 +
diphosphate
 +
L-asparaginyl-tRNAAsn

Synonyms

AS-AR, AsnRS, Asparagine synthetase A, Asparagine translase, asparagine tRNA synthetase, Asparagine--tRNA ligase, Asparaginyl transfer ribonucleic acid synthetase, Asparaginyl transfer RNA synthetase, asparaginyl tRNA synthetase, Asparaginyl-transfer ribonucleate synthetase, asparaginyl-transfer RNA synthetase, Asparaginyl-tRNA synthetase, Asparagyl-transfer RNA synthetase, class IIb asparaginyl-tRNA synthetase, More, NARS, NARS2, NRS, Potentially protective 63 kDa antigen, PYRAB02460, Synthetase, asparaginyl-transfer ribonucleate

ECTree

     6 Ligases
         6.1 Forming carbon-oxygen bonds
             6.1.1 Ligases forming aminoacyl-tRNA and related compounds
                6.1.1.22 asparagine-tRNA ligase

Engineering

Engineering on EC 6.1.1.22 - asparagine-tRNA ligase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L65A
-
the mutant strain lys65a produces an enzyme with greater temperature lability in vitro, a higher temperature-independent Km for Asn, and a lower temperature-dependent catalytic capacity than the enzyme from the wild-type strain
P231L
-
temperature-sensitive mutant HO202, P231L replacement leads to a change in aminoacylation activity. 50fold increased Km for Asn compared to the wild-type, and 8fold increase for ATP in ATP-diphosphate exchange. Significantly increased Km-values for Asn and ATP in aminoacylation. Pro-231 does not seem to be implicated directly in substrate binding. Instead it seems to have a structural role on the positioning of the loop formed by the motif 2
Y426F
-
wild-type and mutant enzymes Y426F and Y426S. Y426S replacement leads to a 15fold increase in Km for ATP, while all the other kinetic parameters remain unchanged. Y426F replacement does not affect the kinetic behaviour of the enzyme
Y426S
-
wild-type and mutant enzymes Y426F and Y426S. Y426S replacement leads to a 15fold increase in Km for ATP, while all the other kinetic parameters remain unchanged. Y426F replacement does not affect the kinetic behaviour of the enzyme
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
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
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
R83A
site-directed mutagenesis, active site amino acid binding mutant, structure analysis in comparison to the wild-type enzyme
additional information