Literature summary for 6.1.1.2 extracted from

Pham, Y.; Li, L.; Kim, A.; Erdogan, O.; Weinreb, V.; Butterfoss, G.L.; Kuhlman, B.; Carter, C.W.
A minimal TrpRS catalytic domain supports sense/antisense ancestry of class I and II aminoacyl-tRNA synthetases (2007), Mol. Cell, 25, 851-862.

Search for more literature for 6.1.1.2

Cloned(Commentary)

Cloned (Comment)	Organism
DNA and amino acid sequence determination and anaylsis, genetic structure, aaRS domain organization and sequence conservation and the sense/antisense coding hypothesis, overview, expression of FLAG-tagged wild-type and mutant enzymes and isolated catalytic domains in Escherichia coli strain BL21(DE3) inclusion bodies	Geobacillus stearothermophilus

Protein Variants

Protein Variants	Comment	Organism
D146A	site-directed mutagensis, the mutant shows highly reduced activity compared to the wild-type enzyme	Geobacillus stearothermophilus
additional information	construction of a catalytically active wild-type and mutant TrpRS minimal catalytic domains, structures, overview	Geobacillus stearothermophilus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Geobacillus stearothermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + L-tryptophan + tRNATrp	Geobacillus stearothermophilus	-	AMP + diphosphate + L-tryptophanyl-tRNATrp	-	?

Organism

Organism	UniProt	Comment	Textmining
Geobacillus stearothermophilus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant FLAG-tagged wild-type and mutant enzymes and isolated catalytic domains from Escherichia coli strain BL21(DE3) soluble fraction by anti-FALG immunoaffinity chromatography and dialysis	Geobacillus stearothermophilus

Renatured (Commentary)

Renatured (Comment)	Organism
recombinant FLAG-tagged wild-type and mutant enzymes and isolated catalytic domains from Escherichia coli strain BL21(DE3) inclusion bodies by dilution in solubilization buffer containing 20 mM HEPES, pH 7.8, 6 M urea, 50 mM or 250 mM KCl, 5 mM MgCl2, 1 mM EDTA, 1 mM PMSF, 1 mM 2-mercaptoethanol, 5% glycerol, and dialysis	Geobacillus stearothermophilus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	-	Geobacillus stearothermophilus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-tryptophan + tRNATrp	-	Geobacillus stearothermophilus	AMP + diphosphate + L-tryptophanyl-tRNATrp	-	?
additional information	TrpRS MCD catalytic activity verifies a key prediction of the Rodin-Ohno hypothesis, overview	Geobacillus stearothermophilus	?	-	?

Subunits

Subunits	Comment	Organism
More	primary sequence analysis and comparison to other class I and to class II aminoacyl-tRNA transferases, aaRS domain organization and sequence conservation and the sense/antisense coding hypothesis, overview	Geobacillus stearothermophilus

Synonyms

Synonyms	Comment	Organism
More	the enzyme belongs to the class I aminoacyl-tRNA transferases	Geobacillus stearothermophilus
TrpRS	-	Geobacillus stearothermophilus
Tryptophanyl-tRNA synthetase	-	Geobacillus stearothermophilus

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Geobacillus stearothermophilus

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Release 2023.1 (January 2023)