Literature summary for 6.1.1.17 extracted from

Saha, R.; Dasgupta, S.; Basu, G.; Roy, S.
A chimaeric glutamyl:glutaminyl-tRNA synthetase: Implications for evolution (2009), Biochem. J., 417, 449-455.

Search for more literature for 6.1.1.17

Protein Variants

Protein Variants	Comment	Organism
additional information	construction of constructed a chimaeric protein, cGluGlnRS, consisting of the catalytic domain, GluRS, and the anticodon binding domain of Escherichia coli GlnRS. cGluGlnRS shows detectable activity of glutamylation of Escherichia coli tRNAGlu and is capable of complementing an Escherichia coli temperature-sensitive GluRS strain at non-permissive temperatures. Both cGluGlnRS and N-terminal residues 1-314 of GluRS bind Escherichia coli tRNAglu with native GluRS-like affinity, suggesting that the anticodon-binding domain in cGluGlnRS enhances kcat for glutamylation. The kcat value of cGluGlnRS is approx. 500fold lower than that of GluRS, whereas the Km value is only moderately higher at the same solution conditions	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0019	-	tRNAGlu	wild-type	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P04805	-	-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.0058	-	tRNAGlu	wild-type	Escherichia coli

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Release 2023.1 (January 2023)