Serine-tRNA ligase

From Wikipedia, the free encyclopedia

In enzymology, a serine-tRNA ligase (EC 6.1.1.11) is an enzyme that catalyzes the chemical reaction

ATP + L-serine + tRNASer $\rightleftharpoons$ AMP + diphosphate + L-seryl-tRNASer

The 3 substrates of this enzyme are ATP, L-serine, and tRNA(Ser), whereas its 3 products are AMP, diphosphate, and L-seryl-tRNA(Ser).

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-serine:tRNASer ligase (AMP-forming). Other names in common use include seryl-tRNA synthetase, SerRS, seryl-transfer ribonucleate synthetase, seryl-transfer RNA synthetase, seryl-transfer ribonucleic acid synthetase, and serine 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, 13 structures have been solved for this class of enzymes, with PDB accession codes 1SER, 1SES, 1SET, 1SRY, 1WLE, 2CIM, 2CJ9, 2CJA, 2CJB, 2DQ0, 2DQ1, 2DQ2, and 2DQ3.

[edit] References

IUBMB entry for 6.1.1.11
BRENDA references for 6.1.1.11 (Recommended.)
PubMed references for 6.1.1.11
PubMed Central references for 6.1.1.11
Google Scholar references for 6.1.1.11
Katze JR, Konigsberg W (1970). "Purification and properties of seryl transfer ribonucleic acid synthetase from Escherichia coli". J. Biol. Chem. 245: 923–30. PMID 4906848.
Makman MH and Cantoni GL (1965). "Isolation of seryl and phenylalanyl ribonucleic acid synthetases from baker's yeast". Biochemistry 4: 1434–1442. doi:10.1021/bi00883a031.
Webster LT and Davie EW (1961). "Purification and properties of serine-activating enzyme from beef pancreas". J. Biol. Chem. 236: 479–484.
Ohama T, Yang DC, Hatfield DL (1994). "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. doi:10.1006/abbi.1994.1503. PMID 7986071.