Literature summary for 6.1.1.2 extracted from

Retailleau, P.; Huang, X.; Yin, Y.; Hu, M.; Weinreb, V.; Vachette, P.; Vonrhein, C.; Bricogne, G.; Roversi, P.; Ilyin, V.; Carter, C.W., Jr.
Interconversion of ATP binding and conformational free energies by tryptophanyl-tRNA synthetase: structures of ATP bound to open and closed, pre-transition-state conformations (2003), J. Mol. Biol., 325, 39-63.

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystallization of native enzyme and selenomethionyl enzyme complexed with ATP, L-tryptophan and analogue indolmycin by microdialysis, formation of high-affinity or low-affinity complexes with ATP at 1 mM and 10 mM, respectively, for microclinic crystals: 0.002 ml enzyme solution, containing 4 mg/ml protein and 50% v/v glycerol, plus 2 ml well solution, 42°C, 2 M potassium phosphate, pH 6.6, 20 mM MgCl2, and 2 mM tryptophan or 1 mM ATP, for tetragonal crystals: 35°C, precipitant solution containing 1 M sodium citrate, 10 mM ATP, 10 mM MgCl2, 0.05 mM tryptophanamide, crystal growth within 1 week, X-ray diffraction structure determination at 2.3 A for the selenomethionyl-enzyme and 2.2 A for the native enzyme, structural data and analysis	Geobacillus stearothermophilus

Crystallization (Comment)

Organism

crystallization of native enzyme and selenomethionyl enzyme complexed with ATP, L-tryptophan and analogue indolmycin by microdialysis, formation of high-affinity or low-affinity complexes with ATP at 1 mM and 10 mM, respectively, for microclinic crystals: 0.002 ml enzyme solution, containing 4 mg/ml protein and 50% v/v glycerol, plus 2 ml well solution, 42°C, 2 M potassium phosphate, pH 6.6, 20 mM MgCl2, and 2 mM tryptophan or 1 mM ATP, for tetragonal crystals: 35°C, precipitant solution containing 1 M sodium citrate, 10 mM ATP, 10 mM MgCl2, 0.05 mM tryptophanamide, crystal growth within 1 week, X-ray diffraction structure determination at 2.3 A for the selenomethionyl-enzyme and 2.2 A for the native enzyme, structural data and analysis

Geobacillus stearothermophilus

Inhibitors

Inhibitors	Comment	Organism	Structure
indolmycin	-	Geobacillus stearothermophilus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	diphosphate exchange kinetics show non-reciprocal cooperativity between ATP and Trp	Geobacillus stearothermophilus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	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-tryptophan-tRNATrp	-	?

Organism

Organism	UniProt	Comment	Textmining
Geobacillus stearothermophilus	P00953	purified native and selenomethionyl enzyme	-

Reaction

Reaction	Comment	Organism	Reaction ID
ATP + L-tryptophan + tRNATrp = AMP + diphosphate + L-tryptophyl-tRNATrp	random, bi-bi kinetic scheme mechanism, KMSKS motif loop is involved in the catalytic mechanism	Geobacillus stearothermophilus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-tryptophan + tRNATrp	-	Geobacillus stearothermophilus	AMP + diphosphate + L-tryptophan-tRNATrp	-	?
additional information	enzyme also performs the ATP-diphosphate exchange reaction	Geobacillus stearothermophilus	?	-	?

Subunits

Subunits	Comment	Organism
More	schematic model of subunit and subsite organization of the homodimeric enzyme	Geobacillus stearothermophilus

Synonyms

Synonyms	Comment	Organism
TrpRS	-	Geobacillus stearothermophilus
Tryptophanyl-tRNA synthase	-	Geobacillus stearothermophilus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	ATP-diphosphate exchange assay at	Geobacillus stearothermophilus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	ATP-diphosphate exchange assay at	Geobacillus stearothermophilus

Cofactor

Cofactor	Comment	Organism	Structure
ATP	assemble of the ATP binding site by domain movement, acts as a key allosteric effector on the enzyme, conformational trigger, not requiring tryptophan pocket ligands, enzyme forms high-affinity complexes at low ATP concentration and low-affinity complexes at high ATP concentration	Geobacillus stearothermophilus