Proline—tRNA ligase
| Proline—tRNA ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In
- ATP + L-proline + tRNAPro AMP + diphosphate + L-prolyl-tRNAPro
The 3
diphosphate, and L-prolyl-tRNA(Pro)
.
This enzyme participates in arginine and proline metabolism and aminoacyl-trna biosynthesis.
Nomenclature
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-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.
References
Further reading
- Norton SJ (July 1964). "Purification and Properties of the Prolyl RNA Synthetase of Escherichia Coli". Archives of Biochemistry and Biophysics. 106: 147–52. PMID 14217147.
- Peterson PJ, Fowden L (October 1965). "Purification, properties and comparative specificities of the enzyme prolyl-transfer ribonucleic acid synthetase from Phaseolus aureus and Polygonatum multiflorum". The Biochemical Journal. 97 (1): 112–24. PMID 16749091.
