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・ Argobba special woreda (Afar)
・ Argobba special woreda (Amhara)
・ Argobuccinum
・ Arginine decarboxylase
・ Arginine deiminase
・ Arginine glutamate
・ Arginine kinase
・ Arginine N-succinyltransferase
・ Arginine racemase
・ Arginine repressor ArgR
・ Arginine vasopressin receptor 1A
・ Arginine vasopressin receptor 1B
・ Arginine vasopressin receptor 2
・ Argininemia
・ Arginine—pyruvate transaminase
Arginine—tRNA ligase
・ Argininosuccinate lyase
・ Argininosuccinate synthase
・ Argininosuccinate synthetase 1
・ Argininosuccinic acid
・ Argininosuccinic aciduria
・ Argintari River
・ Argintul River
・ Argintărie River
・ Arginusae
・ Arginylglycylaspartic acid
・ Arginyltransferase
・ Argiocnemis
・ Argiocnemis rubescens
・ Argiocnemis solitaria


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Arginine—tRNA ligase : ウィキペディア英語版
Arginine—tRNA ligase

In enzymology, an arginine-tRNA ligase () is an enzyme that catalyzes the chemical reaction
:ATP + L-arginine + tRNAArg \rightleftharpoons AMP + diphosphate + L-arginyl-tRNAArg
The 3 substrates of this enzyme are ATP, L-arginine, and tRNA(Arg), whereas its 3 products are AMP, diphosphate, and L-arginyl-tRNA(Arg).
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-arginine:tRNAArg ligase (AMP-forming). Other names in common use include arginyl-tRNA synthetase, arginyl-transfer ribonucleate synthetase, arginyl-transfer RNA synthetase, arginyl transfer ribonucleic acid synthetase, arginine-tRNA synthetase, and arginine translase. This enzyme participates in arginine and proline metabolism and aminoacyl-trna biosynthesis.
It contains a conserved domain at the N terminus called arginyl tRNA synthetase N terminal domain or additional domain 1 (Add-1). This domain is about 140 residues long and it has been suggested that it is involved in tRNA recognition.
==Structural studies==

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .

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