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Literature summary 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

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.15 K279A site-directed mutagenesis 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
-
Homo sapiens
6.1.1.15 additional information
-
additional information
-
Methanocaldococcus jannaschii
6.1.1.15 0.15
-
L-proline pH 7.5, 37°C, mutant K279A Escherichia coli
6.1.1.15 31
-
L-proline pH 7.5, 37°C, mutant K279A Escherichia coli

Metals/Ions

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

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

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.15 Escherichia coli
-
-
-
6.1.1.15 Homo sapiens
-
-
-
6.1.1.15 Methanocaldococcus jannaschii
-
-
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.1.1.15 37
-
assay at Escherichia coli
6.1.1.15 37
-
assay at Homo sapiens
6.1.1.15 37
-
assay at Methanocaldococcus jannaschii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.1.1.15 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
6.1.1.15 0.024
-
L-proline pH 7.5, 37°C, mutant K279A Escherichia coli
6.1.1.15 0.23
-
L-proline pH 7.5, 37°C, mutant K279A Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.15 7
-
assay at Escherichia coli
6.1.1.15 7
-
assay at Homo sapiens
6.1.1.15 7
-
assay at Methanocaldococcus jannaschii

Cofactor

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