EC Number   |
Protein Variants |
Reference |
|---|
    6.1.1.22 | 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 |
392 |
| 6.1.1.22 | more |
downregulation of NARS by siRNA in MC3T3-E1 and primary mouse calvarial cells |
702933 |
| 6.1.1.22 | more |
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 |
745056 |
| 6.1.1.22 | more |
the recombinant human enzyme does not induce leukocyte chemotaxis of HEK-293T cells transfected with G-protein-coupled receptors CXCR1 or CXCR2, overview |
675227 |
| 6.1.1.22 | more |
treatment of HEK-293T cells expressing CXCR2 with the filarial AsnRS, recombinantly expressed in Escherichia coli, parasite AsnRS is chemotactic for human neutrophils and eosinophils, blocks CXCL1-induced calcium flux, and induces mitogen-activated protein kinase, overview |
675227 |
| 6.1.1.22 | N381S |
mutation decreases NARS2 protein levels in patient fibroblasts and also disrupts dimerization of NARS2 |
746169 |
| 6.1.1.22 | 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 |
387 |
| 6.1.1.22 | Q274H |
the mutation leads to defective oxidative phosphorylation activity involving complex I and IV |
745056 |
| 6.1.1.22 | R83A |
site-directed mutagenesis, active site amino acid binding mutant, structure analysis in comparison to the wild-type enzyme |
675391 |
| 6.1.1.22 | V213F |
mutation is the underlying cause of nonsyndromic hearing loss, mutation has no effect on oligomerization |
746169 |
