Literature summary for 6.1.1.12 extracted from

Martin, F.; Sharples, G.J.; LLoyd, R.G.; Eiler, S.; Moras, D.; Gangloff, J.; Eriani, G.
Characterization of a thermosensitive Escherichia coli aspartyl-tRNA synthetase mutant (1997), J. Bacteriol., 179, 3691-3696.

Search for more literature for 6.1.1.12

Crystallization (Commentary)

Crystallization (Comment)	Organism
of enzyme complexed with its cognate tRNA	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
P555S	thermosensitive mutant, resulting in substitution of Pro 555 by Ser. Pro555Ser lowers the stability of the functional configuration of both the acylation and the amino acid activation sites but has no significant effect on substrate binding	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0006	-	tRNAAsp	wild-type enzyme	Escherichia coli
0.06	-	Asp	wild-type enzyme	Escherichia coli
0.09	-	ATP	wild-type enzyme	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	overproducing strain, wild-type and thermosensitive mutant, resulting in substitution of Pro555 by Ser	-

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	-	?

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
additional information	-	thermosensitive mutant, resulting in substitution of Pro 555 by Ser	Escherichia coli
42	-	half-life: 22 min for tRNA aminoacylation, 68 min for ATP/diphosphate exchange	Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
2	8	Asp	mutant enzyme	Escherichia coli
18	-	Asp	wild-type enzyme	Escherichia coli

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)