Literature summary for 6.1.1.11 extracted from

Gruic-Sovulj, I.; Landeka, I.; Soll, D.; Weygand-Durasevic, I.
tRNA-dependent amino acid discrimination by yeast seryl-tRNA synthetase (2002), Eur. J. Biochem., 269, 5271-5279.

Search for more literature for 6.1.1.11

Activating Compound

Activating Compound	Comment	Organism	Structure
tRNASer	binding to the enzyme enhances the discrimination of the amino acid substrate and the activity, and diminishes the rate of misactivation of threonine, all due to a conformational chage in the enzymes active site	Saccharomyces cerevisiae

Protein Variants

Protein Variants	Comment	Organism
E281D/G291A	reduced activity compared to the wild-type enzyme	Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kinetic changes in presence of several tRNAs, nonchargeable and heterologous ones, in the ATP-diphosphate exchange assay	Saccharomyces cerevisiae
0.0013	-	ATP	ATP-diphosphate exchange assay, wild-type enzyme, pH 7.2, 30°C, in presence of tRNASer	Saccharomyces cerevisiae
0.5	-	L-serine	ATP-diphosphate exchange assay, wild-type enzyme, pH 7.2, 30°C, in absence of tRNASer	Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + L-serine + tRNASer	Saccharomyces cerevisiae	-	AMP + diphosphate + L-seryl-tRNASer	-	?

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	purified recombinant wild-type and mutant enzyme	-

Reaction

Reaction	Comment	Organism	Reaction ID
ATP + L-serine + tRNASer = AMP + diphosphate + L-seryl-tRNASer	tRNA substrate discrimination mechanism	Saccharomyces cerevisiae	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-serine + tRNASer	-	Saccharomyces cerevisiae	AMP + diphosphate + L-seryl-tRNASer	-	?
ATP + L-serine + tRNASer	wild-type and mutant tRNASer substrates, the enzyme complexed with 1 molecule of tRNASer is more specific and more efficient in catalyzing seryl-adenylate formation than the apoenzyme alone	Saccharomyces cerevisiae	AMP + diphosphate + L-seryl-tRNASer	-	?
additional information	about 0.4% misactivation of L-threonine by the enzyme compared to cognate L-serine, rate is decreased by binding of the tRNASer, the enzyme also performs the ATP-diphosphate exchange reaction	Saccharomyces cerevisiae	?	-	?

Synonyms

Synonyms	Comment	Organism
62 kDa RNA-binding protein	-	Saccharomyces cerevisiae
Serine transfer RNA synthetase	-	Saccharomyces cerevisiae
Serine translase	-	Saccharomyces cerevisiae
Serine--tRNA ligase	-	Saccharomyces cerevisiae
SerRS	-	Saccharomyces cerevisiae
SerRSmt	-	Saccharomyces cerevisiae
SERSEC	-	Saccharomyces cerevisiae
Seryl-transfer ribonucleate synthetase	-	Saccharomyces cerevisiae
Seryl-transfer ribonucleic acid synthetase	-	Saccharomyces cerevisiae
Seryl-transfer RNA synthetase	-	Saccharomyces cerevisiae
Seryl-tRNA synthetase	-	Saccharomyces cerevisiae
Synthetase, seryl-transfer ribonucleate	-	Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	additional information	changes in kcat in presence of several tRNAs, nonchargeable and heterologous ones, in the ATP-diphosphate exchange assay	Saccharomyces cerevisiae
3.9	-	ATP	ATP-diphosphate exchange assay, wild-type enzyme, pH 7.2, 30°C, in absence of tRNASer	Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.2	-	assay at	Saccharomyces cerevisiae

Cofactor

Cofactor	Comment	Organism	Structure
ATP	binding to the enzyme is not mediated by tRNA	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)