Proline-tRNA ligase

From Wikipedia, the free encyclopedia

In enzymology, a proline-tRNA ligase (EC 6.1.1.15) is an enzyme that catalyzes the chemical reaction

ATP + L-proline + tRNAPro $\rightleftharpoons$ AMP + diphosphate + L-prolyl-tRNAPro

The 3 substrates of this enzyme are ATP, L-proline, and tRNA(Pro), whereas its 3 products are AMP, diphosphate, and L-prolyl-tRNA(Pro).

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-proline:tRNAPro ligase (AMP-forming). Other names in common use include prolyl-tRNA synthetase, prolyl-transferRNA synthetase, prolyl-transfer ribonucleate synthetase, proline translase, prolyl-transfer ribonucleic acid synthetase, prolyl-s-RNA synthetase, and prolinyl-tRNA ligase. This enzyme participates in arginine and proline 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, 15 structures have been solved for this class of enzymes, with PDB accession codes 1H4Q, 1H4S, 1H4T, 1HC7, 1NJ1, 1NJ2, 1NJ5, 1NJ6, 1NJ8, 2I4L, 2I4M, 2I4N, 2I4O, 2J3L, and 2J3M.

[edit] References

IUBMB entry for 6.1.1.15
BRENDA references for 6.1.1.15 (Recommended.)
PubMed references for 6.1.1.15
PubMed Central references for 6.1.1.15
Google Scholar references for 6.1.1.15
Norton SJ (1964). "Purification and properties of the prolyl RNA synthetase of Escherichia coli". Arch. Biochem. Biophys. 106: 147–152. doi:10.1016/0003-9861(64)90167-5.
Peterson PJ and Fowden L (1965). "Purification, properties and comparative specificities of the enzyme prolyl-transfer ribonucleic acid synthetase from Phaseolus aureus and Polygonatum multiflorum". Biochem. J. 97: 112–124.