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Literature summary for 6.1.1.15 extracted from

  • Kumar, S.; Das, M.; Hadad, C.M.; Musier-Forsyth, K.
    Substrate specificity of bacterial prolyl-tRNA synthetase editing domain is controlled by a tunable hydrophobic pocket (2012), J. Biol. Chem., 287, 3175-3184.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.1.15

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Escherichia coli

Protein Variants

Protein Variants Comment Organism
H366A the mutant shows loss in L-alanine deacylation activity Escherichia coli
L266A the mutant shows negligible in L-alanine deacylation at room temperature Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-proline + tRNAPro Escherichia coli
-
 AMP + diphosphate + L-prolyl-tRNAPro
-
 r

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Talon cobalt affinity resin column chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-alanine + tRNAPro
-
 Escherichia coli AMP + diphosphate + L-alanyl-tRNAPro
-
 r
ATP + L-cysteine + tRNAPro
-
 Escherichia coli AMP + diphosphate + L-cysteinyl-tRNAPro
-
 r
ATP + L-proline + tRNAPro
-
 Escherichia coli AMP + diphosphate + L-prolyl-tRNAPro
-
 r

Synonyms

Synonyms Comment Organism
Prolyl-tRNA synthetase
-
 Escherichia coli
ProRS
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli