Phenylalanyl-tRNA synthetase beta chain is an enzyme that in humans is encoded by the FARSBgene.[1][2]
This gene encodes a highly conserved enzyme that belongs to the aminoacyl-tRNA synthetase class IIc subfamily. This enzyme comprises the regulatory beta subunits that form a tetramer with two catalytic alpha subunits. In the presence of ATP, this tetramer is responsible for attaching L-phenylalanine to the terminal adenosine of the appropriate tRNA. A pseudogene located on chromosome 10 has been identified.[2]
References
↑Rodova M, Ankilova V, Safro MG (Apr 1999). "Human phenylalanyl-tRNA synthetase: cloning, characterization of the deduced amino acid sequences in terms of the structural domains and coordinately regulated expression of the alpha and beta subunits in chronic myeloid leukemia cells". Biochem Biophys Res Commun. 255 (3): 765–73. doi:10.1006/bbrc.1999.0141. PMID10049785.
Archambault de Vencay J, Thomes JC, Julien R (1978). "Phenylalanyl-tRNA synthetase of the human placenta. Evidence for different enzymatic forms in equilibrium". FEBS Lett. 89 (1): 98–102. doi:10.1016/0014-5793(78)80531-6. PMID658405.
Moor N, Linshiz G, Safro M (2002). "Cloning and expression of human phenylalanyl-tRNA synthetase in Escherichia coli: comparative study of purified recombinant enzymes". Protein Expr. Purif. 24 (2): 260–7. doi:10.1006/prep.2001.1560. PMID11858721.
Moor N, Lavrik O, Favre A, Safro M (2003). "Prokaryotic and eukaryotic tetrameric phenylalanyl-tRNA synthetases display conservation of the binding mode of the tRNA(Phe) CCA end". Biochemistry. 42 (36): 10697–708. doi:10.1021/bi034732q. PMID12962494.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID14702039.
Yu XY, Finn J, Hill JM, et al. (2004). "A series of spirocyclic analogues as potent inhibitors of bacterial phenylalanyl-tRNA synthetases". Bioorg. Med. Chem. Lett. 14 (5): 1339–42. doi:10.1016/j.bmcl.2003.11.081. PMID14980694.
Vasil'eva IA, Bogachev VS, Favre A, et al. (2005). "Role of low-molecular-weight substrates in functional binding of the tRNAPhe acceptor end by phenylalanyl-tRNA synthetase". Biochemistry Mosc. 69 (2): 143–53. doi:10.1023/B:BIRY.0000018944.53390.44. PMID15000680.