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

BRENDA support

Literature summary 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

Protein Variants

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.15 additional information
-
 additional information wild-type and mutant enzyme kinetics Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.15 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.15 ATP + L-proline + tRNAPro
-
 Escherichia coli AMP + diphosphate + L-prolyl-tRNAPro
-
 ?
6.1.1.15 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

EC Number Synonyms Comment Organism
6.1.1.15 Prolyl-tRNA synthetase
-
 Escherichia coli
6.1.1.15 ProRS
-
 Escherichia coli