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
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6.1.1.20
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aminoacylation
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synthetases
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aminoacyl-trna
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phenylalanylation
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thermophilus
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thermus
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anticodon
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aarss
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proofreading
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phe-trnaphe
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noncognate
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tyrosyl-trna
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misacylated
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seryl-trna
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threonyl-trna
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misaminoacylated
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mischarging
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trna-phe
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aminoacyladenylate
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valyl-trna
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alphabeta2
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biotechnology
- 6.1.1.20
- aminoacylation
- synthetases
- aminoacyl-trna
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phenylalanylation
- thermophilus
- thermus
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anticodon
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aarss
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proofreading
- phe-trnaphe
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noncognate
- tyrosyl-trna
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misacylated
- seryl-trna
- threonyl-trna
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misaminoacylated
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mischarging
- trna-phe
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aminoacyladenylate
- valyl-trna
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alphabeta2
- biotechnology
Reaction
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
6.1.1.20 phenylalanine-tRNA ligaseAdvanced search results
results (
results (Turnover Number
Turnover Number on EC 6.1.1.20 - phenylalanine-tRNA ligase
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TURNOVER NUMBER [1/s] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.03
2-L-naphthylalanine
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mutant enzyme N412G/T415G/S418C/S437F, at pH 7.6, temperature not specified in the publication
0.0035
L-tryptophan
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mutant enzyme N412G/T415G/S418C/S437F, at pH 7.6, temperature not specified in the publication
0.057
3,4-dihydroxy-L-phenylalanine
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.16
3,4-dihydroxy-L-phenylalanine
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in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.23
3,4-dihydroxy-L-phenylalanine
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
2.9
ATP
ATP-diphosphate exchange reaction, mitochondrial isozyme, pH 7.3, 37°C
0.052
DL-m-tyrosine
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.65
DL-m-tyrosine
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.975
L-Phe
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mutant enzyme with A294G mutation in alpha-subunit and T354W mutation in beta-subunit
2.645
L-Phe
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mutant enzyme with A294G mutation in alpha-subunit and E334A mutation in beta-subunit
2.88
L-Phe
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mutant enzyme with A294G mutation in alpha-subunit and H265A mutation in beta-subunit
3 - 6
L-Phe
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mutant enzyme with A294G mutation in alpha-subunit and E334A mutation in beta-subunit
3.12
L-Phe
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mutant enzyme with A294G mutation in alpha-subunit and A356W mutation in beta-subunit
3.3
L-Phe
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mutant enzyme with A294G mutation in alpha-subunit and H265L mutation in beta-subunit
6.08
L-Phe
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mutant enzyme with A294G mutation in alpha-subunit and T354W mutation in beta-subunit
0.005
L-phenylalanine
mitochondrial chimeric enzyme with implanted editing module from Escherichia coli phenylalanine-tRNA synthetase, at pH 8.5 and 37°C
0.0095
L-phenylalanine
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mutant enzyme N412G/T415G/S418C/S437F, at pH 7.6, temperature not specified in the publication
0.075
L-phenylalanine
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.87
L-phenylalanine
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
1.1
L-phenylalanine
ATP-diphosphate exchange reaction, recombinant mitochondrial isozyme, pH 7.3, 37°C
1.12
L-phenylalanine
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in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.033
L-tyrosine
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.077
tRNAPhe
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pH 7.2, 37°C, full-length PheRSA294G, substrate from Saccharomyces cerevisiae
0.11
tRNAPhe
aminoacylation reaction, recombinant mitochondrial isozyme, pH 7.5, 37°C
0.11
tRNAPhe
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pH 7.2, 37°C, truncated mutant PheRSDELTAB2A294G, substrate from Saccharomyces cerevisiae
0.78
tRNAPhe
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pH 7.2, 37°C, truncated mutant PheRSDELTAB2A294G, substrate from Escherichia coli
0.82
tRNAPhe
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pH 7.2, 37°C, full-length PheRSA294G, substrate from Escherichia coli
additional information
additional information
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turnover numbers for tRNA mutants
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additional information
additional information
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turnover numbers for mutant yeast tRNAPhe transcripts
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additional information
additional information
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turnover numbers for mutant yeast tRNAPhe transcripts
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additional information
additional information
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turnover numbers for aminoacylation of tRNAPhe-C-C-A or tRNAPhe-C-C-A(3'NH2) with various amino acids
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additional information
additional information
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turnover-number of tRNAPheG34A is 10% of wild-type value, turnover-number of tRNAPheG34C/A35U is 31% of wild-type value, turnover-number of tRNAPheA36C is 4.2% of wild-type value, turnover-number of tRNAPheU20A is identical to wild-type value, turnover-number of tRNAPheG44C is 2.1% of wild-type value, turnover-number of tRNAPheG19U/C56G is 1.7% of wild-type value
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