Text Size:AAA

AARS / alanyl-tRNA synthetase  ELISA Products

All AARS Reagents

AARS / alanyl-tRNA synthetase Related Area

AARS / alanyl-tRNA synthetase Related Pathways

    AARS / alanyl-tRNA synthetase Related Protein, Antibody, cDNA Gene, and ELISA Kits

    AARS / alanyl-tRNA synthetase Related Protein, Antibody, cDNA Gene, and ELISA Kits

    Featured Reagent Products

    AARS / alanyl-tRNA synthetase Summary & Protein Information

    AARS / alanyl-tRNA synthetase Background

    Gene Summary: The human alanyl-tRNA synthetase (AARS) belongs to a family of tRNA synthases, of the class II enzymes. Class II tRNA synthases evolved early in evolution and are highly conserved. This is reflected by the fact that 498 of the 968-residue polypeptide human AARS shares 41% identity witht the E.coli protein. tRNA synthases are the enzymes that interpret the RNA code and attach specific aminoacids to the tRNAs that contain the cognate trinucleotide anticodons. They consist of a catalytic domain which interacts with the amino acid acceptor-T psi C helix of the tRNA, and a second domain which interacts with the rest of the tRNA structure. [provided by RefSeq, Jul 2008]
    General information above from NCBI
    Catalytic activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). {ECO:0000255|HAMAP-Rule:MF_03133}.
    Cofactor: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03133}; ; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03133};
    Subunit structure: Monomer.
    Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs. {ECO:0000255|HAMAP-Rule:MF_03133}.; The C-terminal C-Ala domain (residues 756 to 968), along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs. The human domain can be used in vitro to replace the corresponding domain in E.coli. {ECO:0000269|PubMed:19661429}.
    Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03133}.
    Post-translational: ISGylated. {ECO:0000255|HAMAP-Rule:MF_03133, ECO:0000269|PubMed:16139798}.
    Involvement in disease: DISEASE: Charcot-Marie-Tooth disease 2N (CMT2N) [MIM:613287]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced. {ECO:0000269|PubMed:20045102, ECO:0000269|PubMed:22009580, ECO:0000269|PubMed:22206013}. Note=The disease is caused by mutations affecting the gene represented in this entry.
    Sequence similarity: Belongs to the class-II aminoacyl-tRNA synthetase family. {ECO:0000255|HAMAP-Rule:MF_03133}.
    General information above from UniProt

    Alanyl-tRNA synthetase (AARS) belongs to the family of ligases, specifically those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. This enzyme participates in alanine and aspartate metabolism and aminoacyl-tRNA biosynthesis. Alanyl-tRNA synthetase (AlaRS) catalyzes synthesis of Ala-tRNA (Ala) and hydrolysis of mis-acylated Ser- and Gly-tRNA (Ala) at 2 different catalytic sites. Their role is not confined to catalyze the attachment of amino acids to transfer RNAs and thereby establish the rules of genetic code by virtue of matching the nucleotide triplet of anticodon with cognate amino acid. Under apoptotic conditions in cell culture, the full-length enzyme is secreted, and the two cytokine activities can be generated by leukocyte elastase, an extracellular protease. Secretion of this tRNA synthetase may contribute to apoptosis both by arresting translation and producing needed cytokines. This protein could be an attractive target of drugs against bacterial, fungal and parasitic infections. 

    AARS / alanyl-tRNA synthetase Alternative Name

    CMT2N, [homo-sapiens]
    cytoplasmic,alanine tRNA ligase 1,alaRS,CMT2N, [human]
    sti,AI316495,alanine-tRNA ligase,alanyl-tRNA synthetase,alaRS,C76919,MGC37368, [mouse]
    sti,C76919,AI316495, [mus-musculus]

    AARS / alanyl-tRNA synthetase Related Studies

  • Wakasugi K, et al. (1999) Two Distinct Cytokines Released from a Human Aminoacyl-tRNA Synthetase. Science. 284 (5411): 147-51.
  • Sokabe M, et al. (2009) The structure of alanyl-tRNA synthetase with editing domain. Proc Natl Acad Sci . 106 (27): 11028-33.
  • Skupinska M, et al. (2009) AARS--the etiological factor and the attractive target of many disorders. Postepy Biochem. 55 (4): 373-84.