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Part of the book series: Springer Handbook of Enzymes ((HDBKENZYMES,volume 10))

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Nomenclature

EC number

 6.1.1.27

Systematic name

 O-phospho-l-serine:tRNACys ligase (AMP-forming)

Recommended name

 O-phospho-l-serine-tRNA ligase

Synonyms

 CysRS <1,7> [1]

 SepRS <1,2,3,5> (<1> SepRS-SepCysS binary complex [4]) [2,3,4,5,6,7]

 phosphoseryl-tRNA synthetase <2,3,5> [3,5,6,7]

 Additional information <5> (<5> the enzyme is a class II tRNA synthetase [6]; <5> the enzyme is a class II tRNA synthetase and belongs to the PLP-dependent superfamily of enzymes [3]) [3,6]

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References

  1. Fukunaga, R.; Yokoyama, S.: Structural insights into the first step of RNA-dependent cysteine biosynthesis in archaea. Nat. Struct. Mol. Biol., 14, 272-279 (2007)

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  2. Yuan, J.; Sheppard, K.; Soell, D.: Amino acid modifications on tRNA. Acta Biochim. Biophys. Sin. (Shanghai), 40, 539-553 (2008)

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  3. Hauenstein, S.I.; Perona, J.J.: Redundant synthesis of cysteinyl-tRNACys in Methanosarcina mazei. J. Biol. Chem., 283, 22007-22017 (2008)

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  4. Zhang, C.M.; Liu, C.; Slater, S.; Hou, Y.M.: Aminoacylation of tRNA with phosphoserine for synthesis of cysteinyl-tRNACys. Nat. Struct. Mol. Biol., 15, 507-514 (2008)

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  5. Fukunaga, R.; Harada, Y.; Hirao, I.; Yokoyama, S.: Phosphoserine aminoacylation of tRNA bearing an unnatural base anticodon. Biochem. Biophys. Res. Commun., 372, 480-485 (2008)

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  6. Hauenstein, S.I.; Hou, Y.M.; Perona, J.J.: The homotetrameric phosphoseryl-tRNA synthetase from Methanosarcina mazei exhibits half-of-the-sites activity. J. Biol. Chem., 283, 21997-22006 (2008)

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  7. Kamtekar, S.; Hohn, M.J.; Park, H.S.; Schnitzbauer, M.; Sauerwald, A.; Söll, D.; Steitz, T.A.: Toward understanding phosphoseryl-tRNACys formation: the crystal structure of Methanococcus maripaludis phosphoseryl-tRNA synthetase. Proc. Natl. Acad. Sci. USA, 104, 2620-2625 (2007)

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Correspondence to Dietmar Schomburg .

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Schomburg, D., Schomburg, I. (2013). O-phospho-l-serine-tRNA ligase 6.1.1.27. In: Schomburg, D., Schomburg, I. (eds) Class 3.4–6 Hydrolases, Lyases, Isomerases, Ligases. Springer Handbook of Enzymes, vol 10. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-36260-6_84

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