Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 6.1.1.15 extracted from

  • Wong, F.C.; Beuning, P.J.; Nagan, M.; Shiba, K.; Musier-Forsyth, K.
    Functional role of the prokaryotic proline-tRNA synthetase insertion domain in amino acid editing (2002), Biochemistry, 41, 7108-7115.
    View publication on PubMed
Search for more literature for 6.1.1.15

Protein Variants

Protein Variants Comment Organism
D350A site-directed mutagenesis, subdomain III mutant, residual remaining aminoaclyation activity, no pre-transfer editing activity Escherichia coli
D378A site-directed mutagenesis, subdomain III mutant, reduced aminoaclyation and pre-transfer editing activity Escherichia coli
D386A site-directed mutagenesis, subdomain III mutant, reduced aminoaclyation and pre-transfer editing activity Escherichia coli
D394A site-directed mutagenesis, subdomain III mutant, reduced aminoaclyation and pre-transfer editing activity Escherichia coli
H369A site-directed mutagenesis, subdomain III mutant, highly reduced reduced aminoaclyation and pre-transfer editing activity, deacetylates Pro-tRNAPro Escherichia coli
H369C site-directed mutagenesis, subdomain III mutant, highly reduced reduced aminoaclyation and pre-transfer editing activity, deacetylates Pro-tRNAPro Escherichia coli
K279A site-directed mutagenesis, subdomain II mutant, reduced aminoaclyation and pre-transfer editing activity Escherichia coli
T257A site-directed mutagenesis, subdomain I mutant, reduced aminoaclyation and pre-transfer editing activity 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
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 class II enzyme, purified recombinant wild-type and mutant enzymes
-

Reaction

Reaction Comment Organism Reaction ID
ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro two-step reaction, Asp350 is involved in the pre-transfer editing of alanine Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-alanine + tRNAPro the enzyme performs 1. misacetylation of tRNAPro, 2. hydrolysis of the misactivated Ala-AMP, i.e. pre-transfer editing, independent of tRNA, and 3. deacetylation of the mischarged Ala-tRNAPro, i.e. post-transfer editing Escherichia coli AMP + diphosphate + L-alanyl-tRNAPro
-
 ?
ATP + L-proline + tRNAPro
-
 Escherichia coli AMP + diphosphate + L-prolyl-tRNAPro
-
 ?
ATP + L-proline + tRNAPro no deacetylation by the wild-type enzyme, but mutants H369C and H369A is able to deacetylate Pro-tRNAPro Escherichia coli AMP + diphosphate + L-prolyl-tRNAPro
-
 ?
additional information the enzyme also performs the ATP-diphosphate exchange reaction Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
Global RNA synthesis factor
-
 Escherichia coli
Pro-tRNA synthetase
-
 Escherichia coli
Proline translase
-
 Escherichia coli
Proline--tRNA ligase
-
 Escherichia coli
Prolyl RNA synthetase
-
 Escherichia coli
Prolyl-transfer ribonucleate synthetase
-
 Escherichia coli
Prolyl-transfer ribonucleic acid synthetase
-
 Escherichia coli
Prolyl-transfer RNA synthetase
-
 Escherichia coli
Prolyl-tRNA synthetase
-
 Escherichia coli
ProRS
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli