EC 6.1.1.11 - Serine—tRNA ligase

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IntEnz Enzyme Nomenclature
EC 6.1.1.11

Names

Accepted name:
serine—tRNA ligase
Other names:
SerRS
serine translase
seryl-tRNA synthetase
seryl-transfer RNA synthetase
seryl-transfer ribonucleate synthetase
seryl-transfer ribonucleic acid synthetase
Systematic name:
L-serine:tRNASer ligase (AMP-forming)

Reactions

Comments:

This enzyme also recognizes tRNASec, the special tRNA for selenocysteine, and catalyses the formation of L-seryl-tRNASec, the substrate for EC 2.9.1.1, L-seryl-tRNASec selenium transferase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00363
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004828
CAS Registry Number: 9023-48-7
UniProtKB/Swiss-Prot: (820) [show] [UniProt]

References

  1. Katze, J.R. and Konigsberg, W.
    Purification and properties of seryl transfer ribonucleic acid synthetase from Escherichia coli.
    J. Biol. Chem. 245: 923-930 (1970). [PMID: 4906848]
  2. Makman, M.H. and Cantoni, G.L.
    Isolation of seryl and phenylalanyl ribonucleic acid synthetases from baker's yeast.
    Biochemistry 4: 1434-1442 (1965).
  3. Webster, L.T. and Davie, E.W.
    Purification and properties of serine-activating enzyme from beef pancreas.
    J. Biol. Chem. 236: 479-484 (1961).
  4. Ohama, T., Yang, D.C. and Hatfield, D.L.
    Selenocysteine tRNA and serine tRNA are aminoacylated by the same synthetase, but may manifest different identities with respect to the long extra arm.
    Arch. Biochem. Biophys. 315: 293-301 (1994). [PMID: 7986071]

[EC 6.1.1.11 created 1961, modified 2002]