Phenylalanine—tRNA ligase
| Phenylalanine—tRNA ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
| Ferredoxin-fold anticodon binding domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| |||||||||
In
enzymology, a phenylalanine—tRNA ligase (EC 6.1.1.20) is an enzyme that catalyzes the chemical reaction
- ATP + L-phenylalanine + tRNAPhe AMP + diphosphate + L-phenylalanyl-tRNAPhe
The 3
diphosphate
, and L-phenylalanyl-tRNAPhe.
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-phenylalanine:tRNAPhe ligase (AMP-forming). Other names in common use include phenylalanyl-tRNA synthetase, phenylalanyl-transfer ribonucleate synthetase, phenylalanine-tRNA synthetase, phenylalanyl-transfer RNA synthetase, phenylalanyl-tRNA ligase, phenylalanyl-transfer RNA ligase, L-phenylalanyl-tRNA synthetase, and phenylalanine translase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and aminoacyl-tRNA biosynthesis.
Phenylalanine-tRNA synthetase (PheRS) is known to be among the most complex
motif having no insertions. The FDX-ACB domain displays a typical RNA recognition fold (RRM) formed by the four-stranded antiparallel beta sheet, with two helices packed against it.[1][2][3][4][5]
Structural studies
As of late 2007, 10
structures have been solved for this class of enzymes, with PDB accession codes 1B70, 1B7Y, 1EIY, 1JJC, 1PYS, 2AKW, 2ALY, 2AMC, 2CXI, and 2IY5
.
References
Further reading
- Stulberg MP (1967). "The isolation and properties of phenylalanyl ribonucleic acid synthetase from Escherichia coli B". J. Biol. Chem. 242 (5): 1060–4. PMID 5335910.
