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6.1.1.15: proline-tRNA ligase

This is an abbreviated version!
For detailed information about proline-tRNA ligase, go to the full flat file.

Word Map on EC 6.1.1.15

Reaction

ATP
+
L-proline
 +
tRNAPro
=
AMP
 +
diphosphate
 +
L-prolyl-tRNAPro

Synonyms

bifunctional aminoacyl-tRNA synthetase, bifunctional glutamate/proline-tRNA ligase, class II prolyl-tRNA synthetase, class II ProRS, dual-specificity prolyl-cysteinyl-tRNA synthetase, dual-specificity prolyl-tRNA synthetase, EPRS, Global RNA synthesis factor, GluProRS, glutamyl-/prolyl-tRNA synthetase, glutamyl-prolyl tRNA synthetase, glutamyl-prolyl-tRNA synthetase, More, MSMEG_2621, Pro-tRNA synthetase, ProCysRS, Proline translase, Proline--tRNA ligase, proline/cysteine-tRNA ligase, Prolyl RNA synthetase, prolyl tRNA synthetase, prolyl-cysteinyl-tRNA synthetase, Prolyl-transfer ribonucleate synthetase, Prolyl-transfer ribonucleic acid synthetase, Prolyl-transfer RNA synthetase, Prolyl-tRNA synthetase, ProRS, ProRS-Cyt, ProRS-Org, ProRSTT, proS, PRS

ECTree

     6 Ligases
         6.1 Forming carbon-oxygen bonds
             6.1.1 Ligases forming aminoacyl-tRNA and related compounds
                6.1.1.15 proline-tRNA ligase

Engineering

Engineering on EC 6.1.1.15 - proline-tRNA ligase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G331A
the mutant shows 6.7fold increased activity compared to the wild type enzyme
G334A
the mutant shows 2.2fold increased activity compared to the wild type enzyme
H366A
the mutant shows 4.4fold increased activity compared to the wild type enzyme
I263A
the mutant shows 2.4fold increased activity compared to the wild type enzyme
I278A
the mutant shows 12.8fold increased activity compared to the wild type enzyme
I333A
the mutant shows 54.7fold increased activity compared to the wild type enzyme
K279A
the mutant shows 2006.3fold increased activity compared to the wild type enzyme
S280A
the mutant shows 2fold increased activity compared to the wild type enzyme
S332A
the mutant shows 1.1fold increased activity compared to the wild type enzyme
T257A
the mutant shows 1.1fold increased activity compared to the wild type enzyme
C443A
-
mutagenesis of C443 to amino acids Ala, Gly and Ser results in significant decreases, 16fold to 225fold in kcat/KmPro, as measured by the ATP-diphosphate exchange assay. The Ala and Gly mutations have relatively small effect, 4fold to 7fold, on the overall aminoacylation reaction, while the activity of the C443 mutant in this same assay is substantially reduced, 80fold
C443G
-
mutagenesis of C443 to amino acids Ala, Gly and Ser results in significant decreases, 16fold to 225fold in kcat/KmPro, as measured by the ATP-diphosphate exchange assay. The Ala and Gly mutations have relatively small effect, 4fold to 7fold, on the overall aminoacylation reaction, while the activity of the C443 mutant in this same assay is substantially reduced, 80fold
C443S
-
mutagenesis of C443 to amino acids Ala, Gly and Ser results in significant decreases, 16fold to 225fold in kcat/KmPro, as measured by the ATP-diphosphate exchange assay. The Ala and Gly mutations have relatively small effect, 4fold to 7fold, on the overall aminoacylation reaction, while the activity of the C443 mutant in this same assay is substantially reduced, 80fold
D198A
-
the overall aminoacylation activity of the mutant is reduced 5.5fold
D350A
-
site-directed mutagenesis, subdomain III mutant, residual remaining aminoaclyation activity, no pre-transfer editing activity
D378A
-
site-directed mutagenesis, subdomain III mutant, reduced aminoaclyation and pre-transfer editing activity
D386A
-
site-directed mutagenesis, subdomain III mutant, reduced aminoaclyation and pre-transfer editing activity
D394A
-
site-directed mutagenesis, subdomain III mutant, reduced aminoaclyation and pre-transfer editing activity
E218A
the mutant activates proline but with a decreased kcat (3fold) and elevated KM value (15fold). Overall proline activation efficiency of this mutant is decreased 45fold compared to the wild type enzyme. The mutant also can charge L-proline onto tRNAPro, albeit with 3fold reduced efficiency
E218A/N305A
-
inactive
E234A
-
the overall aminoacylation activity of the mutant is reduced 2fold
E303A
-
the mutation results in 3fold decrease in L-proline activation. The mutant exhibits a small decrease in the aminoacylation efficiency
E303D
-
the mutation results in 3.1fold decrease in L-proline activation. The mutant exhibits a small decrease in the aminoacylation efficiency
E303K
-
the mutation results in 4.2fold decrease in L-proline activation. The mutant exhibits a small decrease in the aminoacylation efficiency
F415A
-
the aminoacylation activity of the mutant is nearly abolished with rates 70fold slower than the wild type
G217A
the kcat/KM of the mutant is reduced 7fold relative to the wild type enzyme. In contrast, alanine activation by the G217A mutant is not affected compared to the wild type enzyme. A 2fold decrease in alanine activation s observed for the mutant compared to the wild type enzyme. The mutant also can charge L-proline onto tRNAPro, albeit with 3fold reduced efficiency
G412A
-
the overall aminoacylation activity of the mutant is reduced 7fold
H302A
-
the overall aminoacylation activity of the mutant is reduced 2fold
H302A/G412A
-
the overall aminoacylation activity of the mutant is reduced 5.5fold
H366A
-
the mutant shows loss in L-alanine deacylation activity
H369A
-
site-directed mutagenesis, subdomain III mutant, highly reduced reduced aminoaclyation and pre-transfer editing activity, deacetylates Pro-tRNAPro
H369C
-
site-directed mutagenesis, subdomain III mutant, highly reduced reduced aminoaclyation and pre-transfer editing activity, deacetylates Pro-tRNAPro
K279A
K279E
-
the mutation results in 2.7fold reduced L-proline activation. The mutant exhibits wild type aminoacylation efficiency
K279E/E303K
-
the mutant shows 2.3fold reduced L-proline activation. The mutant exhibits wild type aminoacylation efficiency
L266A
-
the mutant shows negligible in L-alanine deacylation at room temperature
N305A
-
the aminoacylation activity of the mutant is nearly abolished with rates 70fold slower than the wild type
N305A/G412A
-
inactive
R144K
-
site-directed mutagenesis, the mutant shows 480fold reduced activity compared to the wild-type enzyme
R144L
-
site-directed mutagenesis, the mutant shows 870fold reduced activity compared to the wild-type enzyme
R146C
-
site-directed mutagenesis, the mutant shows 79fold reduced activity compared to the wild-type enzyme
T257A
-
site-directed mutagenesis, subdomain I mutant, reduced aminoaclyation and pre-transfer editing activity
V143C
-
site-directed mutagenesis, the mutant shows 3fold reduced activity compared to the wild-type enzyme
A57G
-
site-directed mutagenesis, the A57G mutation introduces a BstBI restriction site within the gene, but has no effect on catalytic activity
F1097A
the mutant shows strongly decreased aminoacylation activity compared to the wild type enzyme
F1097W
the mutant shows increased aminoacylation activity compared to the wild type enzyme
R1152K
the mutant shows increased aminoacylation activity compared to the wild type enzyme
R1152L
the mutant shows strongly decreased aminoacylation activity compared to the wild type enzyme
S990A
site-directed mutagenesis, the mutant is unable to rescue virus-infected cells
S990D
site-directed mutagenesis, the mutation markedly inhibits viral replication in cells
E103A
P100A
E103A
-
unaltered thermostability, no remaining prolylation activity, 5% remaining cysteinylation activity compared to the wild-type enzyme
-
P100A
-
unaltered thermostability, loss of 90% cysteinylation activity, unaltered prolylation activity compared to the wild-type enzyme
-
R1152L
catalytically inactive
R201L/R395L/S434A/K435L
catalytic mutant
S886D
phosphomimetic mutant
S886D/S990D
phosphomimetic mutant
S886D/S999D
phosphomimetic mutant
S990A
S990D
S999D
phosphomimetic mutant
R1152L
-
catalytically inactive
-
S990A
-
phosphorylation-resistant mutant
-
S990D
additional information