Phenylalanine—tRNA ligase
From Wikipedia, the free encyclopedia
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
Phenylalanine—tRNA ligase | |||||||||
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Identifiers | |||||||||
EC no. | 6.1.1.20 | ||||||||
CAS no. | 9055-66-7 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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Ferredoxin-fold anticodon binding domain | |||||||||
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Identifiers | |||||||||
Symbol | FDX-ACB | ||||||||
Pfam | PF03147 | ||||||||
InterPro | IPR005121 | ||||||||
SCOP2 | 1pys / SCOPe / SUPFAM | ||||||||
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The 3 substrates of this enzyme are ATP, L-phenylalanine, and tRNAPhe, whereas its 3 products are AMP, 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 enzymes of the aaRS (Aminoacyl-tRNA synthetase) family. Bacterial and mitochondrial PheRSs share a ferredoxin-fold anticodon binding (FDX-ACB) domain, which represents a canonical double split alpha+beta 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]