Literature summary for 6.1.1.12 extracted from

Bernier, S.; Akochy, P.M.; Lapointe, J.; Chenevert, R.
Synthesis and aminoacyl-tRNA synthetase inhibitory activity of aspartyl adenylate analogs (2005), Bioorg. Med. Chem., 13, 69-75.

Search for more literature for 6.1.1.12

Inhibitors

Inhibitors	Comment	Organism	Structure
(3S)-3-amino-5-((((2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl)oxy)(hydroxy)phosphoryl)-4-oxopentanoic acid	-	Escherichia coli
5'-O-[N-(L-aspartyl)sulfamoyl]adenosine	-	Escherichia coli
L-aspartol adenylate	-	Escherichia coli
L-aspartyl adenylate	-	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-aspartate + tRNAAsp	-	Escherichia coli	AMP + diphosphate + L-aspartyl-tRNAAsp	-	?

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.000015	-	5'-O-[N-(L-aspartyl)sulfamoyl]adenosine	pH 7.5, 37°C	Escherichia coli
0.000123	-	(3S)-3-amino-5-((((2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl)oxy)(hydroxy)phosphoryl)-4-oxopentanoic acid	-	Escherichia coli
0.045	-	L-aspartol adenylate	pH 7.5, 37°C	Escherichia coli

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Release 2023.1 (January 2023)