Literature summary for 6.1.1.9 extracted from

Chang, C.P.; Lin, G.; Chen, S.J.; Chiu, W.C.; Chen, W.H.; Wang, C.C.
Promoting the formation of an active synthetase/tRNA complex by a nonspecific tRNA-binding domain (2008), J. Biol. Chem., 283, 30699-30706.

Search for more literature for 6.1.1.9

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Saccharomyces cerevisiae as a His-tagged fusion protein	Homo sapiens
expressed in Saccharomyces cerevisiae as a His-tagged fusion protein	Saccharomyces cerevisiae

Protein Variants

Protein Variants	Comment	Organism
DELTA1-97	an N-domain-deleted yeast valyltRNA synthetase mutant (DELTA1-97) form Saccharomyces cerevisiae can be rescued by fusion of the equivalent domain from its human homologue	Homo sapiens
DELTA1-97	deletion of N-terminal polypeptide extension of 97 residues, which is absent in bacteria, severely impairs tRNA binding, aminoacylation, and complementation activities of the enzyme. This N-domain-deleted yeast valyl-tRNA synthetase mutant can be rescued by fusion of the equivalent domain from its human homologue	Saccharomyces cerevisiae
DELTA32-71	deletion of a lysine rich insert impairs aminoacylation activity of the enzyme in vitro but aminoacylation activity is still significantly higher than in DELTA1-97 mutant. Km: 0.001 mM (L-valyl-tRNAVal), kcast: 0.06/sec (L-valyl-tRNAVal)	Saccharomyces cerevisiae
additional information	fusion of the N-terminal 97 residue domain of human ValRS to Escherichia coli glutaminyl-tRNA synthetase enables the otherwise inactive prokaryotic enzyme to function as a yeast enzyme in vivo. Different from the native yeast enzyme, which shows different affinities toward mixed tRNA populations, the fusion enzyme exhibites similar binding affinities for all yeast tRNAs	Homo sapiens
additional information	fusion of the N-terminal 97 residue domain of the yeast enzyme or its human counterpart to Escherichia coli glutaminyl-tRNA synthetase enables the otherwise inactive prokaryotic enzyme to function as a yeast enzyme in vivo. Different from the native yeast enzyme, which shows different affinities toward mixed tRNA populations, the fusion enzyme exhibites similar binding affinities for all yeast tRNAs	Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0002	-	L-valyl-tRNAVal	-	Saccharomyces cerevisiae
0.001	-	L-valyl-tRNAVal	DELTA32-71 mutant	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-
Saccharomyces cerevisiae	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
using Ni-NTA chromatography	Homo sapiens
using Ni-NTA chromatography	Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-valine + tRNAVal	-	Homo sapiens	AMP + diphosphate + L-valyl-tRNAVal	-	?
ATP + L-valine + tRNAVal	-	Saccharomyces cerevisiae	AMP + diphosphate + L-valyl-tRNAVal	-	?

Synonyms

Synonyms	Comment	Organism
ValRS	-	Homo sapiens
ValRS	-	Saccharomyces cerevisiae
Valyl-tRNA synthetase	-	Homo sapiens
Valyl-tRNA synthetase	-	Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.06	-	L-valyl-tRNAVal	DELTA32-71 mutant	Saccharomyces cerevisiae
0.2	-	L-valyl-tRNAVal	-	Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.9	-	assay at	Homo sapiens
7.9	-	assay at	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)