Literature summary for 6.1.1.9 extracted from

Fukai, S.; Nureki, O.; Sekine, S.; Shimada, A.; Vassylyev, D.G.; Yokoyama, S.
Mechanism of molecular interactions for tRNA(Val) recognition by valyl-tRNA synthetase (2003), RNA, 9, 100-111.

Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	loss of the electrostatically interactions between the coiled-coil domain of the enzyme and base A20 and tertiary bas pair G19.C56 increases the Km for the tRNA by 28fold and the kcat for aminoacylation by 19fold	Thermus thermophilus

Cloned(Commentary)

Cloned (Comment)	Organism
overexpression of wild-type and mutant emnzymes in Escherichia coli strain JM109(DE3)	Thermus thermophilus

Crystallization (Commentary)

Crystallization (Comment)	Organism
enzyme complexed with tRNAVal and valyl-adenylate, hanging-drop vapour diffusion method, 20°C, 1 month, equal volumes of protein and crystallization solution: 50 mM N-(2-acetoamide)iminodiacetic acid sodium salt buffer, pH 6.5, 2% 2-propanol, 0.1 M lithium sulfate, 12% PEG4000, equilibration against reservoir solution: 50 mM N-(2-acetoamide)iminodiacetic acid sodium salt buffer, pH 6.5, 2% propanol, 0.1 M lithium sulfate, and 14% PEG 4000, ligand-free crystals by macro-seeding, X-ray diffraction structure determination at 2.9 A resolution, and analysis	Thermus thermophilus

Crystallization (Comment)

Organism

enzyme complexed with tRNAVal and valyl-adenylate, hanging-drop vapour diffusion method, 20°C, 1 month, equal volumes of protein and crystallization solution: 50 mM N-(2-acetoamide)iminodiacetic acid sodium salt buffer, pH 6.5, 2% 2-propanol, 0.1 M lithium sulfate, 12% PEG4000, equilibration against reservoir solution: 50 mM N-(2-acetoamide)iminodiacetic acid sodium salt buffer, pH 6.5, 2% propanol, 0.1 M lithium sulfate, and 14% PEG 4000, ligand-free crystals by macro-seeding, X-ray diffraction structure determination at 2.9 A resolution, and analysis

Thermus thermophilus

Protein Variants

Protein Variants	Comment	Organism
additional information	a C-treminally truncated mutant enzyme shows highly reduced activity compared to the wild-type enzyme	Thermus thermophilus
R818A/R843A	slightly reduced activity compared to the wild-type enzyme with tRNAValCAC mutant substrate	Thermus thermophilus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
additional information	-	additional information	Km for tRNAVal mutants, loss of the electrostatically interactions between the coiled-coil domain of the enzyme and base A20 and tertiary bas pair G19.C56 increases the Km for the tRNA by 28fold	Thermus thermophilus
0.0015	-	tRNAVal	wild-type enzyme, pH 7.7, 65°C	Thermus thermophilus
0.031	-	tRNAVal	C-terminally truncated mutant enzyme, pH 7.7, 65°C	Thermus thermophilus
0.042	-	tRNAVal	R818A/R843A mutant enzyme, pH 7.7, 65°C	Thermus thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + L-valine + tRNAVal	Thermus thermophilus	-	AMP + diphosphate + L-valyl-tRNAVal	-	?

Organism

Organism	UniProt	Comment	Textmining
Thermus thermophilus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant from Escherichia coli strain JM109(DE3)	Thermus thermophilus

Reaction

Reaction	Comment	Organism	Reaction ID
ATP + L-valine + tRNAVal = AMP + diphosphate + L-valyl-tRNAVal	mechanism and structural basis of molecular interactions of the enzyme with the C34A35C36 anticodon for tRNAVal recognition by the enzyme	Thermus thermophilus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
ATP + L-valine + tRNAVal	-	Thermus thermophilus	AMP + diphosphate + L-valyl-tRNAVal	-	?
ATP + L-valine + tRNAVal	wild-type tRNAVal substrate and mutant forms, the anticodon loop structure of the tRNA is important for substrate recognition	Thermus thermophilus	AMP + diphosphate + L-valyl-tRNAVal	-	?
additional information	loss of the electrostatically interactions between the coiled-coil domain of the enzyme and base A20 and tertiary bas pair G19.C56 increases the Km for the tRNA by 28fold and the kcat for aminoacylation by 19fold	Thermus thermophilus	?	-	?

Synonyms

Synonyms	Comment	Organism
G7a	-	Thermus thermophilus
Synthetase, valyl-transfer ribonucleate	-	Thermus thermophilus
Valine transfer ribonucleate ligase	-	Thermus thermophilus
Valine translase	-	Thermus thermophilus
Valine--tRNA ligase	-	Thermus thermophilus
ValRS	-	Thermus thermophilus
Valyl transfer ribonucleic acid synthetase	-	Thermus thermophilus
Valyl-transfer ribonucleate synthetase	-	Thermus thermophilus
Valyl-transfer RNA synthetase	-	Thermus thermophilus
Valyl-tRNA ligase	-	Thermus thermophilus
Valyl-tRNA synthetase	-	Thermus thermophilus

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism
additional information	-	additional information	kcat for tRNAVal mutants, loss of the electrostatically interactions between the coiled-coil domain of the enzyme and base A20 and tertiary bas pair G19.C56 increases the kcat for aminoacylation by 19fold	Thermus thermophilus
0.36	-	tRNAVal	C-terminally truncated mutant enzyme, pH 7.7, 65°C	Thermus thermophilus
4.3	-	tRNAVal	R818A/R843A mutant enzyme, pH 7.7, 65°C	Thermus thermophilus
6.7	-	tRNAVal	wild-type enzyme, pH 7.7, 65°C	Thermus thermophilus

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Thermus thermophilus