Glycine-tRNA ligase

From Wikipedia, the free encyclopedia

In enzymology, a glycine-tRNA ligase (EC 6.1.1.14) is an enzyme that catalyzes the chemical reaction

ATP + glycine + tRNAGly $\rightleftharpoons$ AMP + diphosphate + glycyl-tRNAGly

The 3 substrates of this enzyme are ATP, glycine, and tRNA(Gly), whereas its 3 products are AMP, diphosphate, and glycyl-tRNA(Gly).

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 glycine:tRNAGly ligase (AMP-forming). Other names in common use include glycyl-tRNA synthetase, glycyl-transfer ribonucleate synthetase, glycyl-transfer RNA synthetase, glycyl-transfer ribonucleic acid synthetase, and glycyl translase. This enzyme participates in glycine, serine and threonine 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, 8 structures have been solved for this class of enzymes, with PDB accession codes 1ATI, 1B76, 1GGM, 1J5W, 2PME, 2PMF, 2Q5H, and 2Q5I.

[edit] References

IUBMB entry for 6.1.1.14
BRENDA references for 6.1.1.14 (Recommended.)
PubMed references for 6.1.1.14
PubMed Central references for 6.1.1.14
Google Scholar references for 6.1.1.14
FRASER MJ (1963). "Glycyl-RNA synthetase of rat liver: partial purification and effects of some metal ions on its activity". Can. J. Biochem. Physiol. 41: 1123–33. PMID 13959340.
Niyomporn B, Dahl JL, Strominger JL (1968). "Biosynthesis of the peptidoglycan of bacterial cell walls. IX Purification and properties of glycyl transfer ribonucleic acid synthetase from Staphylococcus aureus". J. Biol. Chem. 243: 773–8. PMID 4295604.