Literature summary for 6.1.1.17 extracted from

Nureki, O.; Vassylyev, D.G.; Katayanagi, K.; Shimizu, T.; Sekine, S.i.; Kigawa, T.; Miyazawa, T.; Yokoyama, S.; Morikawa, K.
Architectures of class-defining and specific domains of glutamyl-tRNA synthetase (1995), Science, 267, 1958-1965.

Search for more literature for 6.1.1.17

Crystallization (Commentary)

Crystallization (Comment)	Organism
architectures of class-defining and specific domains	Thermus thermophilus

Protein Variants

Protein Variants	Comment	Organism
additional information	mutant enzymes with higher Km and lower turnover numbers	Thermus thermophilus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	Km-values of mutant enzymes	Thermus thermophilus
0.00273	-	tRNAGlu	wild-type enzyme	Thermus thermophilus
0.023	-	ATP	wild-type enzyme	Thermus thermophilus
0.12	-	L-Glu	wild-type	Thermus thermophilus

Organism

Organism	UniProt	Comment	Textmining
Thermus thermophilus	-	wild-type and mutant enzymes	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-glutamate + tRNAGlu	-	Thermus thermophilus	AMP + diphosphate + L-glutamyl-tRNAGlu	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	additional information	turnover numbers of wild-type and mutant enzymes	Thermus thermophilus

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Release 2023.1 (January 2023)