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

BRENDA support

Literature summary for 6.1.1.15 extracted from

  • Bartholow, T.G.; Sanford, B.L.; Cao, B.; Schmit, H.L.; Johnson, J.M.; Meitzner, J.; Bhattacharyya, S.; Musier-Forsyth, K.; Hati, S.
    Strictly conserved lysine of prolyl-tRNA synthetase editing domain facilitates binding and positioning of misacylated tRNAPro (2014), Biochemistry, 53, 1059-1068.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.1.15

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli SG13009 (pREP4) cells Escherichia coli

Protein Variants

Protein Variants Comment Organism
E303A the mutation results in 3fold decrease in L-proline activation. The mutant exhibits a small decrease in the aminoacylation efficiency Escherichia coli
E303D the mutation results in 3.1fold decrease in L-proline activation. The mutant exhibits a small decrease in the aminoacylation efficiency Escherichia coli
E303K the mutation results in 4.2fold decrease in L-proline activation. The mutant exhibits a small decrease in the aminoacylation efficiency Escherichia coli
K279E the mutation results in 2.7fold reduced L-proline activation. The mutant exhibits wild type aminoacylation efficiency Escherichia coli
K279E/E303K the mutant shows 2.3fold reduced L-proline activation. The mutant exhibits wild type aminoacylation efficiency Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.18
-
 L-proline wild type enzyme, at pH 7.5 and 22°C Escherichia coli
0.19
-
 L-proline mutant enzyme K297E/E303K, at pH 7.5 and 22°C Escherichia coli
0.199
-
 L-proline mutant enzyme E303D, at pH 7.5 and 22°C Escherichia coli
0.216
-
 L-proline mutant enzyme E303A, at pH 7.5 and 22°C Escherichia coli
0.22
-
 L-proline mutant enzyme K297E, at pH 7.5 and 22°C Escherichia coli
0.3
-
 L-proline mutant enzyme E303K, at pH 7.5 and 22°C Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Talon cobalt affinity resin column chromatography Escherichia coli

Substrates and Products (Substrate)

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

Synonyms

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.6
-
 L-proline mutant enzyme E303D, at pH 7.5 and 22°C Escherichia coli
5.1
-
 L-proline mutant enzyme E303K, at pH 7.5 and 22°C Escherichia coli
5.2
-
 L-proline mutant enzyme E303A, at pH 7.5 and 22°C Escherichia coli
5.7
-
 L-proline mutant enzyme K297E, at pH 7.5 and 22°C Escherichia coli
5.9
-
 L-proline mutant enzyme K297E/E303K, at pH 7.5 and 22°C Escherichia coli
12.6
-
 L-proline wild type enzyme, at pH 7.5 and 22°C Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
17
-
 L-proline mutant enzyme E303K, at pH 7.5 and 22°C Escherichia coli
23
-
 L-proline mutant enzyme E303D, at pH 7.5 and 22°C Escherichia coli
24
-
 L-proline mutant enzyme E303A, at pH 7.5 and 22°C Escherichia coli
26
-
 L-proline mutant enzyme K297E, at pH 7.5 and 22°C Escherichia coli
31
-
 L-proline mutant enzyme K297E/E303K, at pH 7.5 and 22°C Escherichia coli
71
-
 L-proline wild type enzyme, at pH 7.5 and 22°C Escherichia coli