Tryptophan-tRNA ligase

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In enzymology, a tryptophan-tRNA ligase (EC 6.1.1.2) is an enzyme that catalyzes the chemical reaction

ATP + L-tryptophan + tRNATrp $\rightleftharpoons$ 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, specifically 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

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.

[edit] References

IUBMB entry for 6.1.1.2
BRENDA references for 6.1.1.2 (Recommended.)
PubMed references for 6.1.1.2
PubMed Central references for 6.1.1.2
Google Scholar references for 6.1.1.2
DAVIE EW, KONINGSBERGER VV, LIPMANN F (1956). "The isolation of a tryptophan-activating enzyme from pancreas". Arch. Biochem. Biophys. 65: 21–38. 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: 3958–68. PMID 5805407.
Wong KK, Meister A and Moldave K (1959). "Enzymic formation of ribonucleic acid-amino acid from synthetic aminoacyladenylate and ribonucleic acid". Biochim. Biophys. Acta 36: 531–533. doi:10.1016/0006-3002(59)90196-9.