Literature summary for 6.1.1.17 extracted from

Blais, S.P.; Kornblatt, J.A.; Barbeau, X.; Bonnaure, G.; Laguee, P.; Chenevert, R.; Lapointe, J.
tRNAGlu increases the affinity of glutamyl-tRNA synthetase for its inhibitor glutamyl-sulfamoyl-adenosine, an analogue of the aminoacylation reaction intermediate glutamyl-AMP mechanistic and evolutionary implications (2015), PLoS ONE, 10, e0121043 .

Search for more literature for 6.1.1.17

Application

Application	Comment	Organism
drug development	inhibitor glutamyl-sulfamoyl-adenosine, Glu-AMS, derivatives with bactericidal properties and low toxicity for humans can be developed	Escherichia coli

Cloned(Commentary)

Cloned (Comment)	Organism
gene gluS, recombinant overexpression of C-terminally His-tagged GluRS in Escherichia coli	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
5'-O-[N-(L-glutamyl)sulfamoyl]adenosine	i.e. glutamyl-sulfamoyl-adenosine or Glu-AMS, tRNAGlu increases the affinity of glutamyl-tRNA synthetase for its inhibitor glutamyl-sulfamoyl-adenosine, an analogue of the aminoacylation reaction intermediate glutamyl-AMP, thermodynamics of the enzyme-inhibitor interactions, overview. A significant entropic contribution for the interactions between Glu-AMS and GluRS in the absence of tRNA or in the presence of the cognate tRNAGlu or of the non-cognate tRNAPhe is indicated. The large negative enthalpy is the dominant contribution to DELTAGb in the absence of tRNA. The affinity of GluRS for Glu-AMS is not altered in the presence of the non-cognate tRNAPhe, but the dissociation constant Kd is decreased 50fold in the presence of tRNAGlu. Presence of an H-bond between Glu-AMS and the 3'-OH oxygen of the 3'-terminal ribose of tRNAGlu in the Glu-AMS/GluRS/tRNAGlu complex, molecular dynamics study	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P04805	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu	aminoacylation reaction via a two-step mechanism involving a very unstable aa-AMP intermediate	Escherichia coli	a

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
GluRS	-	Escherichia coli
Glutamyl-tRNA synthetase	-	Escherichia coli

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
additional information	-	microcalorimetry analysis at 20°C, 30°C and 37°C, thermodynamics in presence and absence of tRNAGlu and inhibitor Glu-AMS and non-cognate aa-AMP	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Escherichia coli

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.0000028	-	5'-O-[N-(L-glutamyl)sulfamoyl]adenosine	pH and temperature not specified in the publication	Escherichia coli

General Information

General Information	Comment	Organism
evolution	the structures of the active sites of bacterial and mammalian GluRSs differ significantly	Escherichia coli
additional information	homology structure modeling using structures of GluRSs identified from Burkholderia thailandensis and Thermosynechococcus elongatus, Uniprot IDs Q2SX36 and Q8DLI5, respectively, as search template, molecular docking	Escherichia coli

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Release 2023.1 (January 2023)