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6.1.1.20: phenylalanine-tRNA ligase

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

Word Map on EC 6.1.1.20

Reaction

ATP
+
L-phenylalanine
 +
tRNAPhe
=
AMP
 +
diphosphate
 +
L-phenylalanyl-tRNAPhe

Synonyms

CML33, ctPheRS, cytoplasmic phenylalanyl-tRNA synthetase, cytosolic phenylalanyl-tRNA synthetase, cytosolic PheRS, EcPheRS, FARS2, FRS, hcPheRS, HSPC173, L-Phenylalanyl-tRNA synthetase, mitochondrial phenylalanyl-tRNA synthetase, mitochondrial PheRS, mitPheRS, More, mtPheRS, p-azido-phenylalanyl-tRNA synthetase, pAzFRS, Phe-RS, Phenylalanine translase, phenylalanine tRNA synthetase, Phenylalanine--tRNA ligase, Phenylalanine-tRNA synthetase, Phenylalanyl transfer ribonucleic acid synthetase, Phenylalanyl-transfer ribonucleate synthetase, Phenylalanyl-transfer RNA ligase, Phenylalanyl-transfer RNA synthetase, Phenylalanyl-tRNA ligase, Phenylalanyl-tRNA synthetase, PheRS, PheRS-alpha, Synthetase, phenylalanyl-transfer ribonucleate

ECTree

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

Engineering

Engineering on EC 6.1.1.20 - phenylalanine-tRNA ligase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A450G
T407A
-
the mutant shows normal cocoon production
T407A/A450G
-
the mutant shows decreased cocoon production
T407G
-
the mutant shows decreased cocoon production
A249G/A356W
-
mutant enzyme with A294G mutation in alpha-subunit and A356W mutation in beta-subunit, kcat/Km is 6.6% of wild-type value
A249G/E334A
-
mutant enzyme with A294G mutation in alpha-subunit and E334A mutation in beta-subunit, kcat/Km is 60% of wild-type value
A249G/H265A
-
mutant enzyme with A294G mutation in alpha-subunit and H265A mutation in beta-subunit, kcat/Km is 52% of wild-type value
A249G/H265L
-
mutant enzyme with A294G mutation in alpha-subunit and H265L mutation in beta-subunit, kcat/Km is 63% of wild-type value
A249G/T354W
-
mutant enzyme with A294G mutation in alpha-subunit and T354W mutation in beta-subunit, kcat/Km is 26% of wild-type value
A293X
-
p-fluorophenylalanine-resistant strain with Ala294Ser, Ala293X or Ala295X mutation. Phe293 and Phe295 are not directly involved in substrate binding, but replacements of these residues affect PheRS stability. Exchanges at position 294 alter the binding of Phe, and certain mutants show pronounced changes in specificity towards Phe analogues
A294G
A294S
-
p-fluorophenylalanine-resistant strain with Ala294Ser, Ala293X or Ala295X mutation. Phe293 and Phe295 are not directly involved in substrate binding, but replacements of these residues affect PheRS stability. Exchanges at position 294 alter the binding of Phe, and certain mutants show pronounced changes in specificity towards Phe analogues
A295X
-
p-fluorophenylalanine-resistant strain with Ala294Ser, Ala293X or Ala295X mutation. Phe293 and Phe295 are not directly involved in substrate binding, but replacements of these residues affect PheRS stability. Exchanges at position 294 alter the binding of Phe, and certain mutants show pronounced changes in specificity towards Phe analogues
T251G
-
constructed mutant shows relaxed substrate specificity, efficient incorporation of p-acetylphenylalanine and reactive aryl ketones into protein in the Escherichia coli host
A294G
alphaDELTA1-175
truncated N-terminal domain of the alpha subunit of hcPheRS
alphaDELTA60-170
truncated N-terminal domain of the alpha subunit of hcPheRS
D289Y
the mutant shows 52% of wild type activity
D325Y
-
the mutation is associated with early-onset epilepsy and isolated complex IV deficiency in muscle. The mutant is unable to bind ATP and shows consequently undetectable aminoacylation activity
G273S
inactive
H123P
inactive
H99D
the mutant shows 2.7% of wild type activity
K33C/T351C
mutant, crosslinked catalytic and RNA-binding domains, results in a closed form of mtPheRS that still catalyses ATP-dependent Phe activation, but is no longer able to transfer Phe to tRNA and complete the aminoacylation reaction
N280S
-
the mutant displays wild-type aminoacylation activity and stability with respect to their free energies of unfolding, but are less stable at low pH. It shows no significant loss in secondary structure. The mutant retains less activity than wild-type enzyme after refolding for mitochondrial import
P49A
the mutant shows 78% of wild type activity
R117G
the mutant shows 2.1% of wild type activity
R383C
the mutant shows 43% of wild type activity
R387Q
the mutant shows 86% of wild type activity
S57C
-
the mutant displays wild-type aminoacylation activity and stability with respect to their free energies of unfolding, but are less stable at low pH. It shows no significant loss in secondary structure. The mutant retains less activity than wild-type enzyme after refolding for mitochondrial import
S57C/N280S
-
Ser57 and Asn280 map to positions away from the catalytic center and the anticodon binding domain of hmtPheRS, the mutant does not show significant loss in secondary structure or aminoacylation activity in vitro compared to wild-type enzyme. The S57C/N280S double mutant had remarkable stability even at low pH
T210M
the mutant shows 140% of wild type activity
D286R
-
the mutant shows improvement of activity over the parental enzyme
H283T/P284S/M285D/D286V
-
the mutant shows approximate 8fold improvement of activity over the parental enzyme
P258A/F261P/H283L/M285F/D286Y
-
the mutant shows improvement of activity over the parental enzyme
P284V/D286R
-
the mutant shows improvement of activity over the parental enzyme
A141W
site-directed mutagenesis, the mutant exhibits high tyrosine mischarging activity
D234A
site-directed mutagenesis, the mutant exhibits moderate tyrosine mischarging activity, the mutant PheRS incorrectly hydrolyze the cognate Phe-tRNAPhe
E127A
site-directed mutagenesis, the mutant exhibits low tyrosine mischarging activity
E219A
site-directed mutagenesis, the mutant is similar to the wild-type enzyme
F145A
site-directed mutagenesis, the mutant is similar to the wild-type enzyme
I216A
site-directed mutagenesis, the mutant is similar to the wild-type enzyme
L168A
site-directed mutagenesis, the mutant exhibits moderate tyrosine mischarging activity and shows reduced Tyr-tRNAPhe deacylation activity
L202A
site-directed mutagenesis, the mutant PheRS incorrectly hydrolyze the cognate Phe-tRNAPhe
L210A
site-directed mutagenesis, the mutant is similar to the wild-type enzyme
N217A
site-directed mutagenesis, the mutant exhibits high tyrosine mischarging activity and shows abolished Tyr-tRNAPhe deacylation activity
Q126A
site-directed mutagenesis, the mutant shows reduced Tyr-tRNAPhe deacylation activity
R137A
site-directed mutagenesis, the mutant exhibits low tyrosine mischarging activity and shows reduced Tyr-tRNAPhe deacylation activity
R223A
site-directed mutagenesis, the mutant exhibits moderate tyrosine mischarging activity and shows reduced Tyr-tRNAPhe deacylation activity
S211A
site-directed mutagenesis, the mutant PheRS incorrectly hydrolyze the cognate Phe-tRNAPhe
T221A
site-directed mutagenesis, the mutant is similar to the wild-type enzyme
T236A
site-directed mutagenesis, the mutant PheRS incorrectly hydrolyze the cognate Phe-tRNAPhe
Y189A
site-directed mutagenesis, the mutant exhibits low tyrosine mischarging activity
A333G
-
mtPheRS mutant
G458A
-
ctPheRS mutant
N412G/T415G/S418C/S437F
-
the mutant prefers 2-L-naphthylalanine as substrate
T415G
-
the variant shows 10-fold higher activation activity toward Trp than 2-L-naphthylalanine
additional information