Literature summary for 6.1.1.7 extracted from

Beebe, K.; Mock, M.; Merriman, E.; Schimmel, P.
Distinct domains of tRNA synthetase recognize the same base pair (2008), Nature, 451, 90-93.

Search for more literature for 6.1.1.7

Protein Variants

Protein Variants	Comment	Organism
DELTA1-437	mutant protein containing a deleted aminoacylation domain: mutant protein is fully active for clearance of Ser-tRNAAla but it is inactive deacylate Ser-tRNAAla	Escherichia coli
DELTA1-437/731-875	mutant protein containing a deleted aminoacylation domain: mutant protein is inactive for clearance of Ser-tRNAAla. Using RNA-binding assays, it is shown that the inactivity of the mutant correlates with a lack of binding of tRNAAla. However, at much higher concentrations, mutant is able of specifically deacylating misacylated tRNAAla. Thus, the catalytic site for editing is not disrupted instead, the reduction in editing activity results from a loss of affinity for tRNA	Escherichia coli
DELTA1-437/R693K	a region important for tRNA-specificity is further localized to a predicted strand-loop-strand motif within the region 438-875. Arg 693 is highly conserved. Mutant R693K has relaxed specificity for tRNAThr, and deacylated Ser-tRNAThr. Thus, the AlaRS editing domain shares a second, independent way to recognize tRNAAla	Escherichia coli
additional information	the needed tRNA interaction energy is further localized to non-specific RNA-binding determinants located in the region between amino acids 808 and 875	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	enzyme contains a second active site which prevents mistranslation (mistaking Ser or Gly for Ala) and which is specially designed for hydrolytic editing	Escherichia coli	?	-	?

Synonyms

Synonyms	Comment	Organism
alanyl-tRNA ligase	-	Escherichia coli

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Release 2023.1 (January 2023)