In enzymology, a valine—tRNA ligase (EC 6.1.1.9) is an enzyme that catalyzes the chemical reaction
- ATP + L-valine + tRNAVal AMP + diphosphate + L-valyl-tRNAVal
Valine—tRNA ligase | |||||||||
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Identifiers | |||||||||
EC no. | 6.1.1.9 | ||||||||
CAS no. | 9023-47-6 | ||||||||
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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The 3 substrates of this enzyme are ATP, L-valine, and tRNA(Val), whereas its 3 products are AMP, diphosphate, and L-valyl-tRNA(Val).
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-valine:tRNAVal ligase (AMP-forming). Other names in common use include valyl-tRNA synthetase, valyl-transfer ribonucleate synthetase, valyl-transfer RNA synthetase, valyl-transfer ribonucleic acid synthetase, valine transfer ribonucleate ligase, and valine translase. This enzyme participates in valine, leucine and isoleucine biosynthesis and aminoacyl-trna biosynthesis.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1GAX, 1IVS, 1IYW, 1WK9, and 1WKA.
See also
References
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