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Literature summary for 6.1.1.15 extracted from

  • Splan, K.E.; Ignatov, M.E.; Musier-Forsyth, K.
    Transfer RNA modulates the editing mechanism used by class II prolyl-tRNA synthetase (2008), J. Biol. Chem., 283, 7128-7134.
    View publication on PubMed
Search for more literature for 6.1.1.15

Protein Variants

Protein Variants Comment Organism
K279A site-directed mutagenesis Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Homo sapiens
additional information
-
 additional information
-
 Methanocaldococcus jannaschii
0.15
-
 L-proline pH 7.5, 37°C, mutant K279A Escherichia coli
31
-
 L-proline pH 7.5, 37°C, mutant K279A Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Escherichia coli
Mg2+
-
 Homo sapiens
Mg2+
-
 Methanocaldococcus jannaschii

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
-
 ?
ATP + L-proline + tRNAPro Homo sapiens
-
 AMP + diphosphate + L-prolyl-tRNAPro
-
 ?
ATP + L-proline + tRNAPro Methanocaldococcus jannaschii
-
 AMP + diphosphate + L-prolyl-tRNAPro
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Homo sapiens
-
-
-
Methanocaldococcus jannaschii
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-alanine + tRNAPro mutant K279A, low activity Escherichia coli AMP + diphosphate + L-alanyl-tRNAPro
-
 ?
ATP + L-proline + tRNAPro
-
 Escherichia coli AMP + diphosphate + L-prolyl-tRNAPro
-
 ?
ATP + L-proline + tRNAPro
-
 Homo sapiens AMP + diphosphate + L-prolyl-tRNAPro
-
 ?
ATP + L-proline + tRNAPro
-
 Methanocaldococcus jannaschii AMP + diphosphate + L-prolyl-tRNAPro
-
 ?
additional information determination of Pro-AMP and Ala-AMP hydrolysis activities of wild-type and mutant enzymes, overview Escherichia coli ?
-
 ?
additional information determination of Pro-AMP and Ala-AMP hydrolysis activities, overview Homo sapiens ?
-
 ?
additional information determination of Pro-AMP and Ala-AMP hydrolysis activities, overview Methanocaldococcus jannaschii ?
-
 ?

Synonyms

Synonyms Comment Organism
Prolyl-tRNA synthetase
-
 Escherichia coli
Prolyl-tRNA synthetase
-
 Homo sapiens
Prolyl-tRNA synthetase
-
 Methanocaldococcus jannaschii
ProRS
-
 Escherichia coli
ProRS
-
 Homo sapiens
ProRS
-
 Methanocaldococcus jannaschii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli
37
-
 assay at Homo sapiens
37
-
 assay at Methanocaldococcus jannaschii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information the rate of AMP formation of K279A ProRS in the presence of alanine is 0.034 s-1, which is at least 20 times faster than the rate of nonenzymatic hydrolysis Escherichia coli
0.024
-
 L-proline pH 7.5, 37°C, mutant K279A Escherichia coli
0.23
-
 L-proline pH 7.5, 37°C, mutant K279A Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Escherichia coli
7
-
 assay at Homo sapiens
7
-
 assay at Methanocaldococcus jannaschii

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli
ATP
-
 Homo sapiens
ATP
-
 Methanocaldococcus jannaschii