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Literature summary for 6.1.1.15 extracted from

  • Burke, B.; An, S.; Musier-Forsyth, K.
    Functional guanine-arginine interaction between tRNAPro and prolyl-tRNA synthetase that couples binding and catalysis (2008), Biochim. Biophys. Acta, 1784, 1222-1225.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.1.15

Protein Variants

Protein Variants Comment Organism
R144K site-directed mutagenesis, the mutant shows 480fold reduced activity compared to the wild-type enzyme Escherichia coli
R144L site-directed mutagenesis, the mutant shows 870fold reduced activity compared to the wild-type enzyme Escherichia coli
R146C site-directed mutagenesis, the mutant shows 79fold reduced activity compared to the wild-type enzyme Escherichia coli
V143C site-directed mutagenesis, the mutant shows 3fold reduced activity compared to the wild-type enzyme Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information wild-type and mutant enzyme kinetics 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
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-proline + tRNAPro
-
 Escherichia coli AMP + diphosphate + L-prolyl-tRNAPro
-
 ?
ATP + L-proline + tRNAPro the enzyme recognizes specific bases of tRNAPro in both the anticodon domain, which mediate initial complex formation, and in the acceptor stem, which is proximal to the site of catalysis, analysis of the molecular interaction between ProRS and the acceptor stem of cognate tRNAPro interaction involves the critical residue R144 in the active site and G72 in the acceptor stem, aminoacylation of G72A-tRNAPro is reduced 170fold compared to wild-type tRNAPro when assayed with wild-type ProRS, whereas only a 2.6fold decrease is observed with mutant R144K ProRS, activity of wild-type and mutant enzymes with wild-type and mutant tRNAs, overview Escherichia coli AMP + diphosphate + L-prolyl-tRNAPro
-
 ?

Synonyms

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