Tryptophan—tRNA ligase

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tryptophan-tRNA ligase
EC number
CAS number 9023-44-3
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO

In enzymology, a tryptophan-tRNA ligase (EC is an enzyme that catalyzes the chemical reaction

ATP + L-tryptophan + tRNATrp AMP + diphosphate + L-tryptophyl-tRNATrp

The 3 substrates of this enzyme are ATP, L-tryptophan, and tRNA(Trp), whereas its 3 products are AMP, diphosphate, and L-tryptophyl-tRNATrp.

This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-tryptophan:tRNATrp ligase (AMP-forming). Other names in common use include tryptophanyl-tRNA synthetase, L-tryptophan-tRNATrp ligase (AMP-forming), tryptophanyl-transfer ribonucleate synthetase, tryptophanyl-transfer ribonucleic acid synthetase, tryptophanyl-transfer RNA synthetase, tryptophanyl ribonucleic synthetase, tryptophanyl-transfer ribonucleic synthetase, tryptophanyl-tRNA synthase, tryptophan translase, and TrpRS. This enzyme participates in tryptophan metabolism and aminoacyl-trna biosynthesis.

Structural studies[edit]

As of late 2007, 21 structures have been solved for this class of enzymes, with PDB accession codes 1D2R, 1I6K, 1I6L, 1I6M, 1M83, 1MAU, 1MAW, 1MB2, 1O5T, 1R6T, 1R6U, 1ULH, 1YIA, 1YID, 2A4M, 2AKE, 2AZX, 2DR2, 2G36, 2IP1, and 2OV4.


  • DAVIE EW, KONINGSBERGER VV, LIPMANN F (1956). "The isolation of a tryptophan-activating enzyme from pancreas". Arch. Biochem. Biophys. 65 (1): 21&ndash, 38. doi:10.1016/0003-9861(56)90173-4. PMID 13373404.
  • Preddie EC (1969). "Tryptophanyl transfer ribonucleic acid synthetase from bovine pancreas. II. The chemically different subunits". J. Biol. Chem. 244 (14): 3958&ndash, 68. PMID 5805407.
  • Wong KK, Meister A, Moldave K (1959). "Enzymic formation of ribonucleic acid-amino acid from synthetic aminoacyladenylate and ribonucleic acid". Biochim. Biophys. Acta. 36: 531&ndash, 533. doi:10.1016/0006-3002(59)90196-9. PMID 13845797.