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ctPheRS
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cytoplasmic type
cytoplasmic phenylalanyl-tRNA synthetase
cytosolic phenylalanyl-tRNA synthetase
L-Phenylalanyl-tRNA synthetase
mitochondrial phenylalanyl-tRNA synthetase
p-azido-phenylalanyl-tRNA synthetase
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phenylalanine tRNA synthetase
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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 synthetase
Synthetase, phenylalanyl-transfer ribonucleate
additional information
the enzyme belongs to class II aminoacyl-tRNA synthetases
CML33
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CML33
Methanobacterium thermoautotrophicus
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cytoplasmic phenylalanyl-tRNA synthetase
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cytoplasmic phenylalanyl-tRNA synthetase
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cytosolic phenylalanyl-tRNA synthetase
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cytosolic phenylalanyl-tRNA synthetase
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FARS2
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FRS
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FRS
Methanobacterium thermoautotrophicus
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hcPheRS
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HSPC173
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HSPC173
Methanobacterium thermoautotrophicus
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L-Phenylalanyl-tRNA synthetase
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L-Phenylalanyl-tRNA synthetase
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L-Phenylalanyl-tRNA synthetase
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L-Phenylalanyl-tRNA synthetase
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-
L-Phenylalanyl-tRNA synthetase
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-
L-Phenylalanyl-tRNA synthetase
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L-Phenylalanyl-tRNA synthetase
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L-Phenylalanyl-tRNA synthetase
Methanobacterium thermoautotrophicus
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L-Phenylalanyl-tRNA synthetase
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-
L-Phenylalanyl-tRNA synthetase
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-
L-Phenylalanyl-tRNA synthetase
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-
L-Phenylalanyl-tRNA synthetase
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-
L-Phenylalanyl-tRNA synthetase
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L-Phenylalanyl-tRNA synthetase
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L-Phenylalanyl-tRNA synthetase
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mitochondrial phenylalanyl-tRNA synthetase
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mitochondrial phenylalanyl-tRNA synthetase
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mtPheRS
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mtPheRS
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mitochondrial type
mtPheRS
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mitochondrial type
Phe-RS
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Phenylalanine translase
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Phenylalanine translase
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Phenylalanine translase
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Phenylalanine translase
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Phenylalanine translase
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Phenylalanine translase
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Phenylalanine translase
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Phenylalanine translase
Methanobacterium thermoautotrophicus
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Phenylalanine translase
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Phenylalanine translase
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Phenylalanine translase
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Phenylalanine translase
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Phenylalanine translase
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Phenylalanine translase
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-
Phenylalanine translase
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Phenylalanine--tRNA ligase
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Phenylalanine--tRNA ligase
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Phenylalanine--tRNA ligase
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Phenylalanine--tRNA ligase
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Phenylalanine--tRNA ligase
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-
Phenylalanine--tRNA ligase
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Phenylalanine--tRNA ligase
-
Phenylalanine--tRNA ligase
Methanobacterium thermoautotrophicus
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Phenylalanine--tRNA ligase
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Phenylalanine--tRNA ligase
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Phenylalanine--tRNA ligase
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Phenylalanine--tRNA ligase
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Phenylalanine--tRNA ligase
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Phenylalanine--tRNA ligase
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Phenylalanine--tRNA ligase
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Phenylalanine-tRNA synthetase
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Phenylalanine-tRNA synthetase
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Phenylalanine-tRNA synthetase
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-
Phenylalanine-tRNA synthetase
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Phenylalanine-tRNA synthetase
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-
Phenylalanine-tRNA synthetase
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-
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Phenylalanine-tRNA synthetase
-
-
Phenylalanine-tRNA synthetase
-
Phenylalanine-tRNA synthetase
-
Phenylalanine-tRNA synthetase
Methanobacterium thermoautotrophicus
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Phenylalanine-tRNA synthetase
-
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Phenylalanine-tRNA synthetase
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-
-
Phenylalanine-tRNA synthetase
-
-
Phenylalanine-tRNA synthetase
-
-
Phenylalanine-tRNA synthetase
-
-
Phenylalanine-tRNA synthetase
-
-
Phenylalanine-tRNA synthetase
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-
-
Phenylalanine-tRNA synthetase
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Phenylalanine-tRNA synthetase
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-
-
Phenylalanine-tRNA synthetase
-
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Phenylalanine-tRNA synthetase
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-
-
Phenylalanine-tRNA synthetase
-
Phenylalanine-tRNA synthetase
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-
Phenylalanine-tRNA synthetase
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Phenylalanine-tRNA synthetase
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Phenylalanyl transfer ribonucleic acid synthetase
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Phenylalanyl transfer ribonucleic acid synthetase
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Phenylalanyl transfer ribonucleic acid synthetase
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Phenylalanyl transfer ribonucleic acid synthetase
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Phenylalanyl transfer ribonucleic acid synthetase
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Phenylalanyl transfer ribonucleic acid synthetase
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Phenylalanyl transfer ribonucleic acid synthetase
-
Phenylalanyl transfer ribonucleic acid synthetase
Methanobacterium thermoautotrophicus
-
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Phenylalanyl transfer ribonucleic acid synthetase
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-
Phenylalanyl transfer ribonucleic acid synthetase
-
-
Phenylalanyl transfer ribonucleic acid synthetase
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Phenylalanyl transfer ribonucleic acid synthetase
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Phenylalanyl transfer ribonucleic acid synthetase
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Phenylalanyl transfer ribonucleic acid synthetase
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Phenylalanyl transfer ribonucleic acid synthetase
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Phenylalanyl-transfer ribonucleate synthetase
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Phenylalanyl-transfer ribonucleate synthetase
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Phenylalanyl-transfer ribonucleate synthetase
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Phenylalanyl-transfer ribonucleate synthetase
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Phenylalanyl-transfer ribonucleate synthetase
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Phenylalanyl-transfer ribonucleate synthetase
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-
Phenylalanyl-transfer ribonucleate synthetase
-
Phenylalanyl-transfer ribonucleate synthetase
-
Phenylalanyl-transfer ribonucleate synthetase
Methanobacterium thermoautotrophicus
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Phenylalanyl-transfer ribonucleate synthetase
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Phenylalanyl-transfer ribonucleate synthetase
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Phenylalanyl-transfer ribonucleate synthetase
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Phenylalanyl-transfer ribonucleate synthetase
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Phenylalanyl-transfer ribonucleate synthetase
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Phenylalanyl-transfer ribonucleate synthetase
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Phenylalanyl-transfer ribonucleate synthetase
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Phenylalanyl-transfer ribonucleate synthetase
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Phenylalanyl-transfer ribonucleate synthetase
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Phenylalanyl-transfer ribonucleate synthetase
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Phenylalanyl-transfer ribonucleate synthetase
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Phenylalanyl-transfer RNA ligase
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Phenylalanyl-transfer RNA ligase
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Phenylalanyl-transfer RNA ligase
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Phenylalanyl-transfer RNA ligase
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Phenylalanyl-transfer RNA ligase
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Phenylalanyl-transfer RNA ligase
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Phenylalanyl-transfer RNA ligase
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Phenylalanyl-transfer RNA ligase
Methanobacterium thermoautotrophicus
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Phenylalanyl-transfer RNA ligase
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Phenylalanyl-transfer RNA ligase
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Phenylalanyl-transfer RNA ligase
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Phenylalanyl-transfer RNA ligase
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Phenylalanyl-transfer RNA ligase
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Phenylalanyl-transfer RNA ligase
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Phenylalanyl-transfer RNA ligase
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Phenylalanyl-transfer RNA synthetase
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Phenylalanyl-transfer RNA synthetase
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Phenylalanyl-transfer RNA synthetase
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Phenylalanyl-transfer RNA synthetase
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Phenylalanyl-transfer RNA synthetase
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-
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Phenylalanyl-transfer RNA synthetase
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Phenylalanyl-transfer RNA synthetase
-
Phenylalanyl-transfer RNA synthetase
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Phenylalanyl-transfer RNA synthetase
-
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Phenylalanyl-transfer RNA synthetase
Methanobacterium thermoautotrophicus
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Phenylalanyl-transfer RNA synthetase
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Phenylalanyl-transfer RNA synthetase
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Phenylalanyl-transfer RNA synthetase
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Phenylalanyl-transfer RNA synthetase
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Phenylalanyl-transfer RNA synthetase
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Phenylalanyl-transfer RNA synthetase
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Phenylalanyl-transfer RNA synthetase
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-
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Phenylalanyl-transfer RNA synthetase
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Phenylalanyl-transfer RNA synthetase
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-
Phenylalanyl-transfer RNA synthetase
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Phenylalanyl-transfer RNA synthetase
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Phenylalanyl-tRNA ligase
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Phenylalanyl-tRNA ligase
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Phenylalanyl-tRNA ligase
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Phenylalanyl-tRNA ligase
-
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Phenylalanyl-tRNA ligase
-
-
Phenylalanyl-tRNA ligase
-
Phenylalanyl-tRNA ligase
-
Phenylalanyl-tRNA ligase
Methanobacterium thermoautotrophicus
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Phenylalanyl-tRNA ligase
-
-
Phenylalanyl-tRNA ligase
-
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Phenylalanyl-tRNA ligase
-
-
Phenylalanyl-tRNA ligase
-
-
Phenylalanyl-tRNA ligase
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Phenylalanyl-tRNA ligase
-
-
Phenylalanyl-tRNA ligase
-
Phenylalanyl-tRNA synthetase
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-
-
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Phenylalanyl-tRNA synthetase
-
Phenylalanyl-tRNA synthetase
-
-
Phenylalanyl-tRNA synthetase
-
Phenylalanyl-tRNA synthetase
-
-
Phenylalanyl-tRNA synthetase
-
-
Phenylalanyl-tRNA synthetase
-
-
Phenylalanyl-tRNA synthetase
-
Phenylalanyl-tRNA synthetase
-
-
-
Phenylalanyl-tRNA synthetase
-
-
Phenylalanyl-tRNA synthetase
-
-
-
Phenylalanyl-tRNA synthetase
-
-
Phenylalanyl-tRNA synthetase
-
Phenylalanyl-tRNA synthetase
-
Phenylalanyl-tRNA synthetase
-
-
Phenylalanyl-tRNA synthetase
Methanobacterium thermoautotrophicus
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Phenylalanyl-tRNA synthetase
-
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Phenylalanyl-tRNA synthetase
-
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Phenylalanyl-tRNA synthetase
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Phenylalanyl-tRNA synthetase
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-
-
Phenylalanyl-tRNA synthetase
-
-
Phenylalanyl-tRNA synthetase
-
Phenylalanyl-tRNA synthetase
-
-
Phenylalanyl-tRNA synthetase
-
-
Phenylalanyl-tRNA synthetase
-
-
Phenylalanyl-tRNA synthetase
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-
-
Phenylalanyl-tRNA synthetase
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Phenylalanyl-tRNA synthetase
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-
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Phenylalanyl-tRNA synthetase
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Phenylalanyl-tRNA synthetase
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-
Phenylalanyl-tRNA synthetase
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Phenylalanyl-tRNA synthetase
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PheRS
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PheRS
Methanobacterium thermoautotrophicus
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PheRS
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649147, 650259, 650263, 650285, 652792, 653011, 667747, 670908, 672054, 694872, 727288
Synthetase, phenylalanyl-transfer ribonucleate
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Synthetase, phenylalanyl-transfer ribonucleate
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Synthetase, phenylalanyl-transfer ribonucleate
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Synthetase, phenylalanyl-transfer ribonucleate
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-
Synthetase, phenylalanyl-transfer ribonucleate
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Synthetase, phenylalanyl-transfer ribonucleate
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-
Synthetase, phenylalanyl-transfer ribonucleate
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Synthetase, phenylalanyl-transfer ribonucleate
-
Synthetase, phenylalanyl-transfer ribonucleate
Methanobacterium thermoautotrophicus
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-
Synthetase, phenylalanyl-transfer ribonucleate
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-
Synthetase, phenylalanyl-transfer ribonucleate
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-
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Synthetase, phenylalanyl-transfer ribonucleate
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-
Synthetase, phenylalanyl-transfer ribonucleate
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-
Synthetase, phenylalanyl-transfer ribonucleate
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Synthetase, phenylalanyl-transfer ribonucleate
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Synthetase, phenylalanyl-transfer ribonucleate
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Synthetase, phenylalanyl-transfer ribonucleate
-
Synthetase, phenylalanyl-transfer ribonucleate
-
-
Synthetase, phenylalanyl-transfer ribonucleate
-
Synthetase, phenylalanyl-transfer ribonucleate
-
-
-
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2'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
2'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
2-chloroadenosine 5'-triphosphate + phenylalanine + tRNAPhe
2-chloroadenosine 5'-monophosphate + diphosphate + phenylalanyl-tRNAPhe
3'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
3'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
ATP + 2 L-phenylalanine + tRNAPhe
AMP + diphosphate + bis-L-phenylalanyl-tRNAPhe
ATP + 2-L-naphthylalanine + tRNAPhe
AMP + diphosphate + 2-L-naphthylalanyl-tRNAPhe
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-
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-
?
ATP + 2-L-tyrosine + tRNAPhe
AMP + diphosphate + 2-L-tyrosyl-tRNAPhe
ATP + 3,4-dihydroxy-L-phenylalanine + tRNAPhe
AMP + diphosphate + 3,4-dihydroxy-L-phenylalanyl-tRNAPhe
ATP + 3-L-tyrosine + tRNAPhe
AMP + diphosphate + 3-L--tyrosyl-tRNAPhe
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-
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?
ATP + 3-L-tyrosine + tRNAPhe
AMP + diphosphate + 3-L-tyrosyl-tRNAPhe
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-
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?
ATP + 4-acetyl-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-acetyl-L-phenylalanyl-tRNAPhe
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recombinant mutant T251G, no activity with A294G
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?
ATP + 4-azido-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-azido-L-phenylalanyl-tRNAPhe
ATP + 4-bromo-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-bromo-L-phenylalanyl-tRNAPhe
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recombinant mutant A294G
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?
ATP + 4-cyano-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-cyano-L-phenylalanyl-tRNAPhe
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recombinant mutant A294G
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?
ATP + 4-ethynyl-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-ethynyl-L-phenylalanyl-tRNAPhe
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recombinant mutant A294G
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?
ATP + 4-iodo-L-phenylalanine + amber tRNAPheCUA
AMP + diphosphate + 4-iodo-L-phenylalanyl-amber tRNAPheCUA
ATP + 4-iodo-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-iodo-L-phenylalanyl-tRNAPhe
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recombinant mutant A294G
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?
ATP + benzofuranylalanine + tRNAPhe
AMP + diphosphate + L-benzofuranylalanyl-tRNAPhe
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benzofuranylalanine is a substrate for aminoacylation of tRNAPhe by mutant enzyme with mutation A294G in the alpha-subunit
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?
ATP + DL-m-tyrosine + tRNAPhe
AMP + diphosphate + DL-m-tyrosyl-tRNAPhe
ATP + L-alanine + tRNAPhe
AMP + diphosphate + L-alanyl-tRNAPhe
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-
-
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?
ATP + L-leucine + tRNAPhe
AMP + diphosphate + L-leucyl-tRNAPhe
ATP + L-Phe + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
ATP + L-phenylalanine + (s-pA)tRNAPhe
AMP + diphosphate + L-phenylalanyl-(s-pA)tRNAPhe
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-
-
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?
ATP + L-phenylalanine + (s-pC)tRNAPhe
AMP + diphosphate + L-phenylalanyl-(s-pC)tRNAPhe
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-
-
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?
ATP + L-phenylalanine + (s-pG)tRNAPhe
AMP + diphosphate + L-phenylalanyl-(s-pG)tRNAPhe
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-
-
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?
ATP + L-phenylalanine + (s-pU)tRNAPhe
AMP + diphosphate + L-phenylalanyl-(s-pU)tRNAPhe
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-
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
ATP + L-phenylalanine + tRNAPhe-s6 G76
AMP + diphosphate + L-phenylalanyl-tRNAPhe-s6 G76
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tRNAPhe variant, 370fold reduced activity compared to wild-type tRNAPhe
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?
ATP + L-tryptophan + tRNAPhe
AMP + diphosphate + L-tryptophanyl-tRNAPhe
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-
-
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?
ATP + L-Tyr + tRNAPhe
AMP + diphosphate + L-tyrosyl-tRNAPhe
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cytosolic PheRS contains an editing site, which upon disruption abolishes both cis and trans editing of Tyr-tRNAPhe. Wild-type mitochondrial PheRS lacks cis and trans editing and can synthesisze Tyr-tRNAPhe
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?
ATP + L-tyrosine + tRNAPhe
AMP + diphosphate + L-tyrosinyl-tRNAPhe
-
PheRS misactivates Tyr but is able to correct the mistake using a proofreading editing activity, overview, after evading editing by PheRS, Tyr-tRNAPhe is recognized by elongation factor Tu EF-Tu, involved in translational quality control including substrate selection by aminoacyl-tRNA synthetases, as efficiently as the cognate Phe-tRNAPhe, overview
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-
?
ATP + L-tyrosine + tRNAPhe
AMP + diphosphate + L-tyrosyl-tRNAPhe
GTP + L-phenylalanine + tRNAPhe
GMP + diphosphate + L-phenylalanyl-tRNAPhe
-
40fold lower activity compared to ATP
-
?
N6-methyladenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
N6-methyladenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
additional information
?
-
2'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
2'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
2'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
2'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
2'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
2'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
2'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
2'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
2-chloroadenosine 5'-triphosphate + phenylalanine + tRNAPhe
2-chloroadenosine 5'-monophosphate + diphosphate + phenylalanyl-tRNAPhe
-
-
-
?
2-chloroadenosine 5'-triphosphate + phenylalanine + tRNAPhe
2-chloroadenosine 5'-monophosphate + diphosphate + phenylalanyl-tRNAPhe
-
-
-
?
2-chloroadenosine 5'-triphosphate + phenylalanine + tRNAPhe
2-chloroadenosine 5'-monophosphate + diphosphate + phenylalanyl-tRNAPhe
-
-
-
-
?
2-chloroadenosine 5'-triphosphate + phenylalanine + tRNAPhe
2-chloroadenosine 5'-monophosphate + diphosphate + phenylalanyl-tRNAPhe
-
-
-
?
3'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
3'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
3'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
3'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
3'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
3'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
3'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe
3'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + 2 L-phenylalanine + tRNAPhe
AMP + diphosphate + bis-L-phenylalanyl-tRNAPhe
-
mechanism, formation of bisphenylalanyl-tRNAPhe with tRNA substrates from Thermus thermophilus, isoacceptor I, and from Escherichia coli, yeast and human, the second phenylalanyl residue is attached to tRNA approximately 50 times more slowly than the first one, the presence of modified nucleotides is not necessary for tRNAPhe overcharging
overcharged product cannot be isolated from living cells
ir
ATP + 2 L-phenylalanine + tRNAPhe
AMP + diphosphate + bis-L-phenylalanyl-tRNAPhe
-
mechanism, formation of bisphenylalanyl-tRNAPhe with tRNA substrates from Thermus thermophilus, isoacceptor I, and from Escherichia coli, yeast and human, the second phenylalanyl residue is attached to tRNA approximately 50 times more slowly than the first one, the presence of modified nucleotides is not necessary for tRNAPhe overcharging
overcharged product cannot be isolated from living cells
ir
ATP + 2-L-tyrosine + tRNAPhe
AMP + diphosphate + 2-L-tyrosyl-tRNAPhe
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-
-
-
?
ATP + 2-L-tyrosine + tRNAPhe
AMP + diphosphate + 2-L-tyrosyl-tRNAPhe
-
-
-
-
?
ATP + 3,4-dihydroxy-L-phenylalanine + tRNAPhe
AMP + diphosphate + 3,4-dihydroxy-L-phenylalanyl-tRNAPhe
0.13% activity compared to L-phenylalanine
-
-
?
ATP + 3,4-dihydroxy-L-phenylalanine + tRNAPhe
AMP + diphosphate + 3,4-dihydroxy-L-phenylalanyl-tRNAPhe
0.33% activity compared to L-phenylalanine
-
-
?
ATP + 3,4-dihydroxy-L-phenylalanine + tRNAPhe
AMP + diphosphate + 3,4-dihydroxy-L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + 4-azido-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-azido-L-phenylalanyl-tRNAPhe
-
recombinant mutant A294G
-
?
ATP + 4-azido-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-azido-L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + 4-iodo-L-phenylalanine + amber tRNAPheCUA
AMP + diphosphate + 4-iodo-L-phenylalanyl-amber tRNAPheCUA
-
suppressor tRNAPhe CUA is misacylated with 4-iodo-L-phenylalanine by the mutant at a high magnesium-ion concentration by PheRS mutant A294G
-
-
?
ATP + 4-iodo-L-phenylalanine + amber tRNAPheCUA
AMP + diphosphate + 4-iodo-L-phenylalanyl-amber tRNAPheCUA
-
suppressor tRNAPhe CUA is misacylated with 4-iodo-L-phenylalanine by the mutant at a high magnesium-ion concentration by PheRS mutant A294G
-
-
?
ATP + DL-m-tyrosine + tRNAPhe
AMP + diphosphate + DL-m-tyrosyl-tRNAPhe
1.9% activity compared to L-phenylalanine
-
-
?
ATP + DL-m-tyrosine + tRNAPhe
AMP + diphosphate + DL-m-tyrosyl-tRNAPhe
22% activity compared to L-phenylalanine
-
-
?
ATP + L-leucine + tRNAPhe
AMP + diphosphate + L-leucyl-tRNAPhe
-
-
-
-
?
ATP + L-leucine + tRNAPhe
AMP + diphosphate + L-leucyl-tRNAPhe
-
-
-
-
?
ATP + L-Phe + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-Phe + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-Phe + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-Phe + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
various mutant transcripts of phenylalanine tRNA prepared by an in vitro transcription system are examined. The results indicated that anticodon nucleotides G34, A35 and A36, discriminator base A73 and G20 in the variable pocket are base-specifically recognized by the enzyme
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
various mutant transcripts of phenylalanine tRNA prepared by an in vitro transcription system are examined. The results indicated that anticodon nucleotides G34, A35 and A36, discriminator base A73 and G20 in the variable pocket are base-specifically recognized by the enzyme
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
cognate amino acid charging
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
the enzyme is responsible for synthesizing Phe-tRNAPhe during protein synthesis
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
a two-step reaction, tRNAPhe substrate from Escherichia coli and Saccharomyces cerevisiae, the enzyme contains the dispensable B2 RNA-binding domain that contributes to the post-transfer editing of noncognate aminoacyl-tRNA, the B2 domain does not enhance tRNA folding, overview
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
cognate amino acid charging onto tRNAPheUUU and tRNAPheUUC
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
the enzyme is responsible for synthesizing Phe-tRNAPhe during protein synthesis
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
a two-step reaction, tRNAPhe substrate from Escherichia coli and Saccharomyces cerevisiae, the enzyme contains the dispensable B2 RNA-binding domain that contributes to the post-transfer editing of noncognate aminoacyl-tRNA, the B2 domain does not enhance tRNA folding, overview
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
ir
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
aminoacylates native yeast tRNAPhe
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
activity with mutant yeast tRNAPhe transcripts
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
100% activity
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
the N-terminal coiled-coil structure of the alpha-subunit is involved in the binding of cognate tRNAPhe
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
tRNAPhe substrate from Escherichia coli, two-step reaction, the first step, formation of the aminoacyl-adenylate, is reversible, the second, transfer of the activated amino acid to the tRNA, is not
-
ir
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
charging of cognate amino acid
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
recognition of phenylalanyl-adenylate and substrate binding structure, docking model, overview. Formation of the PheRS-tRNAPhe complex in human mitochondria must be accompanied by considerable rearrangement, i.e. hinge-type rotation through about 160degree, of the anticodon binding domain upon tRNA binding, overview
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Methanobacterium thermoautotrophicus
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
heterologous aminoacylation of tRNA with high selectivity for archaebacterial tRNA
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
natural noncognate amino acids are not transferred to tRNAPhe-C-C-A or tRNAPhe-C-C-A-(3'-NH2)
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
tRNAs from E. coli and bean chloroplast are not aminoacylated
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
natural noncognate amino acids are not transferred to tRNAPhe-C-C-A or tRNAPhe-C-C-A-(3'-NH2)
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
editing mechanism of noncognate aminoacyl-tRNA involving domains B3 and B4 and residues Leu202, Ser211, Asp234, and Thr236, overview
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
activity is restricted to endogenous tRNA, highly specific for L-phenylalanine
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
enzyme is essemtial for poly(Phe) synthesis
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
discrimination between phenylalanine and 18 other naturally occuring amino acids, discrimination factors
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
five major recognition nucleotides: G20, G34, A35, A36, and A73. The noncognate tRNAs are missing a sufficient number of recognition nucleotides or have a structure imcompatible for the formation of a complex with phenylalanine-tRNA ligase
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
structure-activity relationship, overview
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
ir
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
r
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
can incorporate more than one molecule of Phe into tRNAPhe. The hyperaminoacylated tRNAPhe is the bis-2',3'-O-phenylalanyl-tRNAPhe
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
mutant tRNAs with substitutions at position 16, 17, 19, or 20 (in the D loop), 34-36 (in the anticodon loop), 26, 44 (at the top of the anticodon stem), 56 (in the T loop), 73 (in the acceptor end) and at the base pairs 10*25 (in the D stem), 27*43 and 28*42 (in the anticodon). Nucleotide 20 and some tertiary nucleotides, including the conserved G19*C56 base pair, are proposed to participate in stabilization of the precise tRNA conformation required for efficient aminoacylation
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
reaction intermediate aminacyl-AMP stucture
-
r
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
the recognition of Phe through a mixture of van der Waals interactions and hydrogen bonds
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
tRNA substrates from Thermus thermophilus, isoacceptor I, and from Escherichia coli, yeast and human
-
ir
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
two-step reaction, the first step, formation of phenylalanyl-adenylate intermediate, proceeds also within crystals, where the intermediate is bound to the active site involving neighbouring residues Phe258 and Phe260
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
wild-type tRNAPhe substrate, enzyme interacts with the 3'-end of tRNAPhe
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
effect of nucleotide replacement in tRNAPhe on positioning of the acceptor end in the complex with phenylalanine-tRNA synthetase
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
charging of cognate amino acid, conformational changes in tRNAPhe and the catalytic domain are induced by the PheOH-AMP or AMP binding, acceptor arm binding and recognition
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
ir
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
tRNA substrates from Thermus thermophilus, isoacceptor I, and from Escherichia coli, yeast and human
-
ir
ATP + L-tyrosine + tRNAPhe
AMP + diphosphate + L-tyrosyl-tRNAPhe
-
-
-
-
?
ATP + L-tyrosine + tRNAPhe
AMP + diphosphate + L-tyrosyl-tRNAPhe
-
-
-
-
?
ATP + L-tyrosine + tRNAPhe
AMP + diphosphate + L-tyrosyl-tRNAPhe
0.089% activity compared to L-phenylalanine
-
-
?
ATP + L-tyrosine + tRNAPhe
AMP + diphosphate + L-tyrosyl-tRNAPhe
-
-
-
-
?
additional information
?
-
enzyme expression, genes pheS and pheT, is regulated by iron availability
-
?
additional information
?
-
-
enzyme expression, genes pheS and pheT, is regulated by iron availability
-
?
additional information
?
-
-
no activity with L-tryptophan
-
-
?
additional information
?
-
-
ATP-diphosphate exchange
-
-
?
additional information
?
-
-
a number of phenylalanine analogs: tyrosine, leucine, methionine, p-fluorophenylalanine, beta-phenylserine, beta-thien-2-ylalanine, 2-amino-4-methylhex-4-enoic acid, mimosine, N-benzyl-L-phenylalanine, and N-benzyl-D-phenylalanine, can replace phenylalanine in ATP-diphosphate exchange
-
-
?
additional information
?
-
-
synthesis of diadenosine 5',5'''-P1,P4-tetraphosphate
-
-
?
additional information
?
-
-
in vitro selection of small RNAs that bind to E. coli phenylalanyl-tRNA synthetase
-
-
?
additional information
?
-
-
phenylalanyl-tRNA synthetase misactivates tyrosine and subsequently corrects such errors through hydrolysis of tyrosyl-adenylate and Tyr-tRNAPhe. Editing by phenylalanyl-tRNA synthetase is essential for faithful translation of the genetic code
-
-
?
additional information
?
-
-
PheRS editing is the major proofreading step that prevents infiltration of Tyr into Phe codons during translation
-
-
?
additional information
?
-
-
editing activity of the isolated recombinant B3/4 editing domain from PheRS, overview
-
-
?
additional information
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ATP-diphosphate exchange
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additional information
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the enzyme also performs the ATP-diphosphate exchange reaction
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?
additional information
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the enzyme also performs the ATP-diphosphate exchange reaction
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?
additional information
?
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the catalytic function resides in the alpha-subunit, while the beta-subunit provides several binding-like domains for OB, RNP, SH3, and DNA
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?
additional information
?
-
the catalytic function resides in the alpha-subunit, while the beta-subunit provides several binding-like domains for OB, RNP, SH3, and DNA
-
?
additional information
?
-
-
the catalytic function resides in the alpha-subunit, while the beta-subunit provides several binding-like domains for OB, RNP, SH3, and DNA
-
?
additional information
?
-
-
the autoantibody anti-Zo, reactive with phenylalanyltransfer RNA synthetase, immunoprecipitates 155 and 140 kD proteins and is common in children but seems to be associated with malignancy in adults, such as the antisynthetase syndrome, i.e. myositis, ILD, Raynaud's disease, and arthralgias, overview
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?
additional information
?
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-
ATP-diphosphate exchange
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?
additional information
?
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a number of phenylalanine analogs: tyrosine, leucine, methionine, p-fluorophenylalanine, beta-phenylserine, beta-thien-2-ylalanine, 2-amino-4-methylhex-4-enoic acid, mimosine, N-benzyl-L-phenylalanine, and N-benzyl-D-phenylalanine, can replace phenylalanine in ATP-diphosphate exchange
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?
additional information
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a number of phenylalanine-analogous can replace phenylalanine in ATP-diphosphate exchange: methionine, p-fluorophenylalanine, beta-phenylserine, beta-thien-1-ylalanine, 2-amino-4-methylhex-4-enoic acid, ochratoxin A
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?
additional information
?
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synthesis of diadenosine 5',5'''-P1,P4-tetraphosphate
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?
additional information
?
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ATP-diphosphate exchange
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?
additional information
?
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a number of phenylalanine analogs: tyrosine, leucine, methionine, p-fluorophenylalanine, beta-phenylserine, beta-thien-2-ylalanine, 2-amino-4-methylhex-4-enoic acid, mimosine, N-benzyl-L-phenylalanine, and N-benzyl-D-phenylalanine, can replace phenylalanine in ATP-diphosphate exchange
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?
additional information
?
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synthesis of diadenosine 5',5'''-P1,P4-tetraphosphate
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?
additional information
?
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editing activity of the isolated recombinant B3/4 editing domain from PheRS, overview
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?
additional information
?
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ATP-diphosphate exchange
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?
additional information
?
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ATP-diphosphate exchange
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?
additional information
?
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a number of phenylalanine analogs: tyrosine, leucine, methionine, p-fluorophenylalanine, beta-phenylserine, beta-thien-2-ylalanine, 2-amino-4-methylhex-4-enoic acid, mimosine, N-benzyl-L-phenylalanine, and N-benzyl-D-phenylalanine, can replace phenylalanine in ATP-diphosphate exchange
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?
additional information
?
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synthesis of diadenosine 5',5'''-P1,P4-tetraphosphate
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?
additional information
?
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very low activity with L-DOPA and 4-L-tyrosine
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?
additional information
?
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phylogenetic analysis
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?
additional information
?
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no activity with tRNAPhe-s4 U76, a tRNA variant harboring a 4-thiouridine residue in the 3'-end
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?
additional information
?
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the enzyme interacts with DNA, more efficiently with single-stranded than with double-stranded DNA, the binding site for DNA is located near the interface between the alpha and beta subunits and is distinct from the tRNAPhe binding site
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?
additional information
?
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the enzyme probably interacts with DNA
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?
additional information
?
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the enzyme specifically binds certain Thermus thermophilus DNA sequences, accession number Y15464, of the genomic DNA
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?
additional information
?
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the enzyme specifically binds certain Thermus thermophilus DNA sequences, accession number Y15464, of the genomic DNA
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?
additional information
?
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the enzyme might by its DNA binding capacity be involved in cellular processes of cell proliferation
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?
additional information
?
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the enzyme might by its DNA binding capacity be involved in cellular processes of cell proliferation
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?
additional information
?
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tRNAPhe binding structure determination: CCA end orientation is stabilized by extensive base-specific interactions of A76 and C75 with the protein and by intra-RNA interactions of A73 with adjacent nucleotides, the 4-amino group of the bulged out C75 is trapped by two negatively charged residues of the beta-subunit, Glubeta31 and Aspbeta33, highly conserved in eubacterial PheRSs, the position of the A76 base is stabilized by interactions with HisR212 of motif 2 (universally conserved in PheRSs) and class II-invariant ArgR321 of motif 3, overview
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?
additional information
?
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editing activity of the isolated recombinant B3/4 editing domain from PheRS, overview
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + 4-azido-L-phenylalanine + tRNAPhe
AMP + diphosphate + 4-azido-L-phenylalanyl-tRNAPhe
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
ATP + L-tyrosine + tRNAPhe
AMP + diphosphate + L-tyrosinyl-tRNAPhe
-
PheRS misactivates Tyr but is able to correct the mistake using a proofreading editing activity, overview, after evading editing by PheRS, Tyr-tRNAPhe is recognized by elongation factor Tu EF-Tu, involved in translational quality control including substrate selection by aminoacyl-tRNA synthetases, as efficiently as the cognate Phe-tRNAPhe, overview
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?
additional information
?
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
cognate amino acid charging
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
the enzyme is responsible for synthesizing Phe-tRNAPhe during protein synthesis
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
the enzyme is responsible for synthesizing Phe-tRNAPhe during protein synthesis
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
-
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
-
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
ir
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
Methanobacterium thermoautotrophicus
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-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
-
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
enzyme is essemtial for poly(Phe) synthesis
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
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ir
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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-
-
r
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
ir
additional information
?
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enzyme expression, genes pheS and pheT, is regulated by iron availability
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?
additional information
?
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enzyme expression, genes pheS and pheT, is regulated by iron availability
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?
additional information
?
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phenylalanyl-tRNA synthetase misactivates tyrosine and subsequently corrects such errors through hydrolysis of tyrosyl-adenylate and Tyr-tRNAPhe. Editing by phenylalanyl-tRNA synthetase is essential for faithful translation of the genetic code
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?
additional information
?
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PheRS editing is the major proofreading step that prevents infiltration of Tyr into Phe codons during translation
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?
additional information
?
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the catalytic function resides in the alpha-subunit, while the beta-subunit provides several binding-like domains for OB, RNP, SH3, and DNA
-
?
additional information
?
-
the catalytic function resides in the alpha-subunit, while the beta-subunit provides several binding-like domains for OB, RNP, SH3, and DNA
-
?
additional information
?
-
-
the catalytic function resides in the alpha-subunit, while the beta-subunit provides several binding-like domains for OB, RNP, SH3, and DNA
-
?
additional information
?
-
-
the autoantibody anti-Zo, reactive with phenylalanyltransfer RNA synthetase, immunoprecipitates 155 and 140 kD proteins and is common in children but seems to be associated with malignancy in adults, such as the antisynthetase syndrome, i.e. myositis, ILD, Raynaud's disease, and arthralgias, overview
-
-
?
additional information
?
-
phylogenetic analysis
-
?
additional information
?
-
the enzyme might by its DNA binding capacity be involved in cellular processes of cell proliferation
-
?
additional information
?
-
-
the enzyme might by its DNA binding capacity be involved in cellular processes of cell proliferation
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2R,3R,3aS,5aR,10R,10aR)-N-(3,4-dichlorophenyl)-10-hydroxy-4-oxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
-
-
(2R,3R,3aS,5aR,10S,10aR)-N-(3,4-dichlorophenyl)-10-hydroxy-4-oxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
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-
(2R,3R,3aS,5aS,10aR)-N-(3,4-dichlorophenyl)-4,10-dioxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
-
IC50: 0.0026 mM; IC50: 0.0031 mM
(2R,3R,3aS,5aS,10R,10aS)-N-(3,4-dichlorophenyl)-10-hydroxy-4-oxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
-
IC50: 0.00047 mM; IC50: 0.00051 mM
(2R,3R,3aS,5aS,10S,10aS)-N-(3,4-dichlorophenyl)-10-hydroxy-4-oxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
-
IC50: 0.00017 mM; IC50: 0.00026 mM
(2Z)-2-(cyclopropylimino)-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
(2Z)-2-[(3-chlorophenyl)imino]-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
(3a'R,6a'S)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
(3a'R,6a'S)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
(3a'S,6a'R)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
(3a'S,6a'R)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
(3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
(3aR,6aS)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
(3aS,6aR)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
(3aS,6aR)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
(3aS,6aR)-5-[4-chloro-3-(trifluoromethyl)phenyl]-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
(3R,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
(3R,4S,5R)-4-[(3,4-dichlorophenyl)carbamoyl]-1',3'-dioxo-5-phenyl-1',3',4,5-tetrahydro-3H-spiro[furan-2,2'-indene]-3-carboxylic acid
-
IC50: 0.011 mM; IC50: 0.033 mM
(3S,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
(4-[4-[(3-chlorobenzyl)oxy]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
(4-[4-[2-(3-chlorophenyl)-2-hydroxyethyl]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetic acid
1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)[2,2'-binaphthalene]-8,8'-dicarbaldehyde
1-(3-bromophenyl)-2-[(2-methoxybenzyl)amino]ethanol
-
IC50: 110 nM
1-(3-chlorophenyl)-2-[(2-phenoxybenzyl)amino]ethanol
-
IC50: 31 nM
1-(3-iodophenyl)-2-[(2-phenoxybenzyl)amino]ethanol
-
IC50: 32 nM
1-(3-methoxyphenyl)-2-[(2-phenoxybenzyl)amino]ethanol
-
IC50: 83 nM
1-(3-[[4-(3,5-dichlorophenyl)piperazin-1-yl]sulfonyl]phenyl)-3-(1,3-thiazol-2-yl)urea
1-(4-bromothiophen-2-yl)-2-[(2-methoxybenzyl)amino]ethanol
-
IC50: 50 nM
1-(4-bromothiophen-2-yl)-2-[(2-phenoxybenzyl)amino]ethanol
-
IC50: 120 nM
1-(4-bromothiophen-2-yl)-2-[(2-[[4-(methylsulfonyl)benzyl]oxy]benzyl)amino]ethanol
-
IC50: 26 nM
1-(4-bromothiophen-2-yl)-2-[[2-(2-hydroxyethoxy)benzyl]amino]ethanol
-
IC50: 8 nM
1-(4-bromothiophen-2-yl)-2-[[2-(but-3-en-1-yloxy)benzyl]amino]ethanol
-
IC50: 18 nM
1-(4-bromothiophen-2-yl)-2-[[2-(methoxymethoxy)benzyl]amino]ethanol
-
IC50: 35 nM
1-(4-bromothiophen-2-yl)-2-[[2-(pyridin-2-ylmethoxy)benzyl]amino]ethanol
-
IC50: 43 nM
1-(4-bromothiophen-2-yl)-2-[[2-(pyridin-3-ylmethoxy)benzyl]amino]ethanol
-
IC50: 18 nM
1-(4-bromothiophen-2-yl)-2-[[2-(pyridin-4-ylmethoxy)benzyl]amino]ethanol
-
IC50: 16 nM
1-[3-(hydroxymethyl)phenyl]-2-[(2-phenoxybenzyl)amino]ethanol
-
IC50: 570 nM
1-[3-[(4-pyridin-2-ylpiperazin-1-yl)sulfonyl]phenyl]-3-(1,3-thiazol-2-yl)urea
-
binding structure and inhibition mechanism, the inhibitor molecule binds with ring A deep inside the enzyme, and ring B in the place that is occupied by the aromatic ring of phenylalanine, overview
1-[4-[(3-chlorobenzyl)oxy]-3-methylbenzoyl]piperidine-4-carboxamide
1-[4-[2-(3-chlorophenyl)ethyl]-3-methylbenzoyl]piperidine-4-carboxamide
1-[[2-(3-chlorophenyl)-1-methyl-4-oxo-1,4-dihydroquinazolin-6-yl]carbonyl]piperidine-4-carboxamide
2-(3-methoxyphenyl)-5-(trifluoromethyl)-1H-imidazole
2-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetamide
2-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)ethanol
2-chloro-N-(3-chlorophenyl)-4-[(4-methyl-3-oxopiperazin-1-yl)carbonyl]benzenesulfonamide
2-phenylacetamidine
-
competitive with respect to phenylalanine
2-[(2-methoxybenzyl)amino]-1-(3-methylphenyl)ethanol
-
IC50: 110 nM
2-[(2-methoxybenzyl)amino]-1-[3-(trifluoromethoxy)phenyl]ethanol
-
IC50: 190 nM
2-[(2-methoxybenzyl)amino]-1-[3-(trifluoromethyl)phenyl]ethanol
-
IC50: 160 nM
2-[(2-methylbenzyl)amino]-1-[3-(trifluoromethyl)phenyl]ethanol
-
IC50: 790 nM
2-[(4-chlorophenoxy)methyl]-N-(2-sulfamoylethyl)-1,3-thiazole-4-carboxamide
2-[(4-chlorophenoxy)methyl]-N-(cyanomethyl)-1,3-thiazole-4-carboxamide
2-[([2-hydroxy-2-[3-(trifluoromethyl)phenyl]ethyl]amino)methyl]benzoic acid
-
IC50: 2500 nM
2-[([2-hydroxy-2-[3-(trifluoromethyl)phenyl]ethyl]amino)methyl]phenol
-
IC50: 100 nM
2-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-(3-hydroxypropyl)acetamide
-
IC50: 110 nM
2-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-ethylacetamide
-
IC50: 32 nM
2-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]acetamide
-
IC50: 42 nM
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazole
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfanyl)-1,3,4-oxadiazole
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfinyl)-1,3,4-oxadiazole
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfonyl)-1,3,4-oxadiazole
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-ethyl-1,3,4-oxadiazole
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-methyl-1,3,4-oxadiazole
2-[3-[(4-chloropyridin-2-yl)amino]phenoxy]-N-(1,1-dioxo-1l6-thiolan-3-yl)acetamide
2-[3-[(4-chloropyridin-2-yl)amino]phenoxy]-N-methylacetamide
2-[3-[(4-cyanopyridin-2-yl)amino]phenoxy]-N-methylacetamide
2-[4-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]butyl]-1H-isoindole-1,3(2H)-dione
-
IC50: 22 nM
2-[[2-(1H-benzimidazol-2-ylmethoxy)benzyl]amino]-1-(4-bromothiophen-2-yl)ethanol
-
IC50: 26 nM
2-[[2-(2-aminoethoxy)benzyl]amino]-1-(4-bromothiophen-2-yl)ethanol
-
IC50: 220 nM
2-[[2-(4-aminobutoxy)benzyl]amino]-1-(4-bromothiophen-2-yl)ethanol
-
IC50: 22 nM
2-[[2-(benzyloxy)benzyl]amino]-1-(4-bromothiophen-2-yl)ethanol
-
IC50: 10 nM
2-[[2-(benzyloxy)benzyl]amino]-1-[3-(trifluoromethyl)phenyl]ethanol
-
IC50: 50 nM
2-[[2-(difluoromethoxy)benzyl]amino]-1-[3-(trifluoromethyl)phenyl]ethanol
-
IC50: 260 nM
2-[[2-(prop-2-en-1-yloxy)benzyl]amino]-1-[3-(trifluoromethyl)phenyl]ethanol
-
IC50: 58 nM
3'-Deoxyadenosine 5'-triphosphate
3'-Methyladenosine 5'-triphosphate
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(1-hydroxypropan-2-yl)benzamide
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(4-hydroxybutyl)benzamide
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(cyclopropylmethyl)benzamide
3-chloro-4-[(3-chlorobenzyl)oxy]-N-[2-(ethylamino)ethyl]-N-methylbenzenesulfonamide
3-chloro-4-[(3-chlorobenzyl)oxy]-N-[2-(morpholin-4-yl)ethyl]benzamide
3-chloro-N-[2-methyl-4-[(4-methyl-3-oxopiperazin-1-yl)carbonyl]phenyl]benzenesulfonamide
3-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-(3-hydroxypropyl)propanamide
-
IC50: 25 nM
3-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-[2-(methylamino)-2-oxoethyl]propanamide
-
IC50: 36 nM
3-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]propanoic acid
-
IC50: 58 nM
4-(3-chloro-4-[[(3-chlorophenyl)sulfinyl]methyl]benzoyl)-1-methylpiperazin-2-one
4-(3-chloro-4-[[(3-chlorophenyl)sulfonyl]methyl]benzoyl)-1-methylpiperazin-2-one
4-chloro-5-[(3-chlorobenzyl)oxy]-2-(1,3,4-oxadiazol-2-yl)pyridine
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(1-ethyl-1H-pyrazol-5-yl)pyridine-2-carboxamide
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(1-hydroxypropan-2-yl)pyridine-2-carboxamide
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(4-hydroxybutyl)pyridine-2-carboxamide
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(4-hydroxycyclohexyl)pyridine-2-carboxamide
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(cyclopropylmethyl)pyridine-2-carboxamide
4-chloro-5-[(3-chlorobenzyl)oxy]-N-[2-(morpholin-4-yl)ethyl]pyridine-2-carboxamide
4-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-(3-hydroxypropyl)butanamide
-
IC50: 26 nM
4-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-[2-(methylamino)-2-oxoethyl]butanamide
-
IC50: 30 nM
4-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]butanoic acid
-
IC50: 43 nM
4-[3-chloro-4-[(3-chlorobenzyl)oxy]benzoyl]-1-methylpiperazin-2-one
5-(3-methoxyphenyl)-3-(trifluoromethyl)-1H-pyrazole
5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-amine
5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazole-2-carboxamide
5-[4-chloro-5-[(3-chlorobenzyl)oxy]pyridin-2-yl]-1,3,4-oxadiazol-2-amine
5-[4-chloro-5-[(3-chlorobenzyl)oxy]pyridin-2-yl]-1,3,4-oxadiazole-2-carboxamide
Alkylamides of phenylalanine
-
the inhibitor constant decreases with increasing length of the alkyl chain
benzylguanidine
-
competitive with respect to phenylalanine
E. coli tRNAPhe
-
inhibition by formation of a tight complex of the enzyme with the diphosphate formed during the aminoacylation
-
ethyl [3-[3-(difluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetate
ethyl [3-[3-(trifluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetate
L-phenylalanyl-5'-adenylate
-
-
L-phenylalanyl-adenylate
-
-
methyl 3-chloro-4-[(3,4-difluorobenzyl)oxy]benzoate
methyl 3-chloro-4-[(3-chlorobenzyl)oxy]benzoate
methyl 3-chloro-4-[(3-fluorobenzyl)oxy]benzoate
methyl 4-[(1R,2R)-2-(3-chlorophenyl)-1,2-dihydroxyethyl]-3-methylbenzoate
methyl 4-[(1S,2S)-2-(3-chlorophenyl)-1,2-dihydroxyethyl]-3-methylbenzoate
methyl 4-[(3-chlorobenzoyl)amino]-3-methylbenzoate
methyl 4-[(3-chlorobenzyl)(methyl)amino]-3-methylbenzoate
methyl 4-[(3-chlorobenzyl)amino]-3-methylbenzoate
methyl 4-[(3-chlorobenzyl)oxy]-3-methylbenzoate
methyl 4-[(3-chlorobenzyl)oxy]benzoate
methyl 4-[(3-chlorophenyl)carbamoyl]benzoate
methyl 4-[(E)-2-(3-chlorophenyl)ethenyl]-3-methylbenzoate
methyl 4-[[(3-chlorophenyl)(methyl)amino]methyl]benzoate
methyl 4-[[(3-chlorophenyl)amino]methyl]benzoate
N-(1,1-dioxo-1l6-thiolan-3-yl)-2-[(4-methylphenoxy)methyl]-1,3-thiazole-4-carboxamide
N-(1-[3-chloro-4-[(4-chlorobenzyl)oxy]benzyl]pyrrolidin-3-yl)acetamide
N-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetamide
N-benzyl-D-amphetamine
-
most potent competitive inhibitor, selectivity for bacterial enzyme
N-benzylbenzamidine
-
competitive with respect to phenylalanine
N-[2-(1H-indol-3-yl)ethyl]-3-[(1,3-thiazol-2-ylcarbamoyl)amino]benzenesulfonamide
N-[2-(1H-indol-3-yl)ethyl]-3-[[(1,3-thiazol-2-yl)carbamoyl]amino]benzene-1-sulfonamide
N-[2-[1-(methanesulfonyl)cyclopropyl]ethyl]-2-[3-[3-(trifluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetamide
N-[3-[4-(pyridin-2-yl)piperazine-1-sulfonyl]phenyl]-N'-1,3-thiazol-2-ylurea
N2-[[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]acetyl]-N-methylglycinamide
-
IC50: 120 nM
N6-Benzyladenosine 5'-triphosphate
Ochrotoxine A
-
cometitive
phenyl-thiazolylurea-sulfonamides
phenyl-thiazolylurea-sulfonamido-aminoethyl-chloroindol
phenyl-thiazolylurea-sulfonamido-aminoethyl-chloroindole
-
-
phenyl-thiazolylurea-sulfonamido-aminoethylindol
phenyl-thiazolylurea-sulfonamido-aminoethylindole
-
strong inhibition, competitive to L-phenylalanine, cytotoxic effects on CHO cells and bacteria
tRNAPhe Cp75
-
tRNAPhe with cytosine phosphate residue at position 75
-
tRNAPhe s4-U75
-
tRNAPhe with 4-thiouridine residue at position 75
-
tRNAPhe s4-U76
-
tRNAPhe with 4-thiouridine residue at position 76
-
tRNAPhe s4-U77
-
tRNAPhe with 4-thiouridine residue at position 77
-
tRNAPhe s4-Up77
-
tRNAPhe with 4-thiouridine phosphate residue at position 77
-
[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]acetonitrile
-
IC50: 49 nM
[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl](4-methylpiperazin-1-yl)methanone
[3-chloro-4-[(3-chlorophenoxy)methyl]phenyl](4-methylpiperazin-1-yl)methanone
[4-([3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]sulfonyl)piperazin-1-yl](4-methylphenyl)methanone
[4-[1-(3-chlorophenyl)-2-hydroxyethyl]-3-methylphenyl](4-methylpiperazin-1-yl)methanone
(2Z)-2-(cyclopropylimino)-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
-
competitive with respect to Phe, selective for bacterial Phe-RS versus human Phe-RS, IC50: 0.002 mM
(2Z)-2-(cyclopropylimino)-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
-
competitive with respect to Phe, selective for bacterial Phe-RS versus human Phe-RS, IC50: 0.00017 mM
(2Z)-2-(cyclopropylimino)-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
-
competitive with respect to Phe, selective for bacterial Phe-RS versus human Phe-RS, IC50: 0.0016 mM
(2Z)-2-[(3-chlorophenyl)imino]-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
-
IC50: 600 nM
(2Z)-2-[(3-chlorophenyl)imino]-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
-
IC50: 10 nM
(2Z)-2-[(3-chlorophenyl)imino]-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
-
IC50: 70 nM
(3a'R,6a'S)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
-
IC50: 40 nM, high selectivity over the human enzyme
(3a'R,6a'S)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
-
IC50: 40 nM, high selectivity over the human enzyme
(3a'R,6a'S)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
-
IC50: 0.00099 mM, high selectivity over the human enzyme
(3a'R,6a'S)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
-
IC50: 0.00073 mM, high selectivity over the human enzyme
(3a'S,6a'R)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
-
IC50: 0.004 mM, high selectivity over the human enzyme
(3a'S,6a'R)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
-
IC50: 0.003 mM, high selectivity over the human enzyme
(3a'S,6a'R)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
-
IC50: 0.0087 mM, high selectivity over the human enzyme
(3a'S,6a'R)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
-
IC50: 0.0061 mM, high selectivity over the human enzyme
(3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 0.00085 mM, high selectivity over the human enzyme
(3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 0.00056 mM, high selectivity over the human enzyme
(3aR,6aS)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 0.00022 mM, high selectivity over the human enzyme
(3aR,6aS)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 0.00007 mM, high selectivity over the human enzyme
(3aS,6aR)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 5 nM, high selectivity over the human enzyme
(3aS,6aR)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 2 nM, high selectivity over the human enzyme
(3aS,6aR)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 0.0083 mM, high selectivity over the human enzyme
(3aS,6aR)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 0.0137 mM, high selectivity over the human enzyme
(3aS,6aR)-5-[4-chloro-3-(trifluoromethyl)phenyl]-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 0.032 mM, high selectivity over the human enzyme
(3aS,6aR)-5-[4-chloro-3-(trifluoromethyl)phenyl]-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 0.045 mM, high selectivity over the human enzyme
(3R,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 5 nM
(3R,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 130 nM
(3R,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 4 nM
(3S,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 820 nM
(3S,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
-
IC50: 3200 nM
(4-[4-[(3-chlorobenzyl)oxy]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
-
-
(4-[4-[(3-chlorobenzyl)oxy]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
-
-
(4-[4-[2-(3-chlorophenyl)-2-hydroxyethyl]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
-
-
(4-[4-[2-(3-chlorophenyl)-2-hydroxyethyl]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
-
-
(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetic acid
-
-
(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetic acid
-
-
1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)[2,2'-binaphthalene]-8,8'-dicarbaldehyde
-
-
1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)[2,2'-binaphthalene]-8,8'-dicarbaldehyde
-
-
1-(3-[[4-(3,5-dichlorophenyl)piperazin-1-yl]sulfonyl]phenyl)-3-(1,3-thiazol-2-yl)urea
-
IC50: 15 nM
1-(3-[[4-(3,5-dichlorophenyl)piperazin-1-yl]sulfonyl]phenyl)-3-(1,3-thiazol-2-yl)urea
-
IC50: 15 nM
1-(3-[[4-(3,5-dichlorophenyl)piperazin-1-yl]sulfonyl]phenyl)-3-(1,3-thiazol-2-yl)urea
-
IC50: 50 nM
1-[4-[(3-chlorobenzyl)oxy]-3-methylbenzoyl]piperidine-4-carboxamide
-
-
1-[4-[(3-chlorobenzyl)oxy]-3-methylbenzoyl]piperidine-4-carboxamide
-
-
1-[4-[2-(3-chlorophenyl)ethyl]-3-methylbenzoyl]piperidine-4-carboxamide
-
-
1-[4-[2-(3-chlorophenyl)ethyl]-3-methylbenzoyl]piperidine-4-carboxamide
-
-
1-[[2-(3-chlorophenyl)-1-methyl-4-oxo-1,4-dihydroquinazolin-6-yl]carbonyl]piperidine-4-carboxamide
-
-
1-[[2-(3-chlorophenyl)-1-methyl-4-oxo-1,4-dihydroquinazolin-6-yl]carbonyl]piperidine-4-carboxamide
-
-
2',3'-Ribodeoxy-ATP
-
-
2-(3-methoxyphenyl)-5-(trifluoromethyl)-1H-imidazole
-
-
2-(3-methoxyphenyl)-5-(trifluoromethyl)-1H-imidazole
-
-
2-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetamide
-
-
2-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetamide
-
-
2-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)ethanol
-
-
2-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)ethanol
-
-
2-chloro-N-(3-chlorophenyl)-4-[(4-methyl-3-oxopiperazin-1-yl)carbonyl]benzenesulfonamide
-
-
2-chloro-N-(3-chlorophenyl)-4-[(4-methyl-3-oxopiperazin-1-yl)carbonyl]benzenesulfonamide
-
-
2-[(4-chlorophenoxy)methyl]-N-(2-sulfamoylethyl)-1,3-thiazole-4-carboxamide
-
-
2-[(4-chlorophenoxy)methyl]-N-(2-sulfamoylethyl)-1,3-thiazole-4-carboxamide
-
-
2-[(4-chlorophenoxy)methyl]-N-(cyanomethyl)-1,3-thiazole-4-carboxamide
-
-
2-[(4-chlorophenoxy)methyl]-N-(cyanomethyl)-1,3-thiazole-4-carboxamide
-
-
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazole
-
-
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazole
-
-
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfanyl)-1,3,4-oxadiazole
-
-
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfanyl)-1,3,4-oxadiazole
-
-
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfinyl)-1,3,4-oxadiazole
-
-
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfinyl)-1,3,4-oxadiazole
-
-
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfonyl)-1,3,4-oxadiazole
-
-
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfonyl)-1,3,4-oxadiazole
-
-
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-ethyl-1,3,4-oxadiazole
-
-
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-ethyl-1,3,4-oxadiazole
-
-
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-methyl-1,3,4-oxadiazole
-
-
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-methyl-1,3,4-oxadiazole
-
-
2-[3-[(4-chloropyridin-2-yl)amino]phenoxy]-N-(1,1-dioxo-1l6-thiolan-3-yl)acetamide
-
-
2-[3-[(4-chloropyridin-2-yl)amino]phenoxy]-N-(1,1-dioxo-1l6-thiolan-3-yl)acetamide
-
-
2-[3-[(4-chloropyridin-2-yl)amino]phenoxy]-N-methylacetamide
-
-
2-[3-[(4-chloropyridin-2-yl)amino]phenoxy]-N-methylacetamide
-
-
2-[3-[(4-cyanopyridin-2-yl)amino]phenoxy]-N-methylacetamide
-
-
2-[3-[(4-cyanopyridin-2-yl)amino]phenoxy]-N-methylacetamide
-
-
3'-Deoxyadenosine 5'-triphosphate
-
-
3'-Deoxyadenosine 5'-triphosphate
-
-
3'-Deoxyadenosine 5'-triphosphate
-
-
3'-Methyladenosine 5'-triphosphate
-
-
3'-Methyladenosine 5'-triphosphate
-
-
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(1-hydroxypropan-2-yl)benzamide
-
-
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(1-hydroxypropan-2-yl)benzamide
-
-
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(4-hydroxybutyl)benzamide
-
-
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(4-hydroxybutyl)benzamide
-
-
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(cyclopropylmethyl)benzamide
-
-
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(cyclopropylmethyl)benzamide
-
-
3-chloro-4-[(3-chlorobenzyl)oxy]-N-[2-(ethylamino)ethyl]-N-methylbenzenesulfonamide
-
-
3-chloro-4-[(3-chlorobenzyl)oxy]-N-[2-(ethylamino)ethyl]-N-methylbenzenesulfonamide
-
-
3-chloro-4-[(3-chlorobenzyl)oxy]-N-[2-(morpholin-4-yl)ethyl]benzamide
-
-
3-chloro-4-[(3-chlorobenzyl)oxy]-N-[2-(morpholin-4-yl)ethyl]benzamide
-
-
3-chloro-N-[2-methyl-4-[(4-methyl-3-oxopiperazin-1-yl)carbonyl]phenyl]benzenesulfonamide
-
-
3-chloro-N-[2-methyl-4-[(4-methyl-3-oxopiperazin-1-yl)carbonyl]phenyl]benzenesulfonamide
-
-
4-(3-chloro-4-[[(3-chlorophenyl)sulfinyl]methyl]benzoyl)-1-methylpiperazin-2-one
-
-
4-(3-chloro-4-[[(3-chlorophenyl)sulfinyl]methyl]benzoyl)-1-methylpiperazin-2-one
-
-
4-(3-chloro-4-[[(3-chlorophenyl)sulfonyl]methyl]benzoyl)-1-methylpiperazin-2-one
-
-
4-(3-chloro-4-[[(3-chlorophenyl)sulfonyl]methyl]benzoyl)-1-methylpiperazin-2-one
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-2-(1,3,4-oxadiazol-2-yl)pyridine
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-2-(1,3,4-oxadiazol-2-yl)pyridine
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(1-ethyl-1H-pyrazol-5-yl)pyridine-2-carboxamide
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(1-ethyl-1H-pyrazol-5-yl)pyridine-2-carboxamide
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(1-hydroxypropan-2-yl)pyridine-2-carboxamide
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(1-hydroxypropan-2-yl)pyridine-2-carboxamide
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(4-hydroxybutyl)pyridine-2-carboxamide
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(4-hydroxybutyl)pyridine-2-carboxamide
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(4-hydroxycyclohexyl)pyridine-2-carboxamide
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(4-hydroxycyclohexyl)pyridine-2-carboxamide
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(cyclopropylmethyl)pyridine-2-carboxamide
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(cyclopropylmethyl)pyridine-2-carboxamide
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-N-[2-(morpholin-4-yl)ethyl]pyridine-2-carboxamide
-
-
4-chloro-5-[(3-chlorobenzyl)oxy]-N-[2-(morpholin-4-yl)ethyl]pyridine-2-carboxamide
-
-
4-[3-chloro-4-[(3-chlorobenzyl)oxy]benzoyl]-1-methylpiperazin-2-one
-
-
4-[3-chloro-4-[(3-chlorobenzyl)oxy]benzoyl]-1-methylpiperazin-2-one
-
-
5-(3-methoxyphenyl)-3-(trifluoromethyl)-1H-pyrazole
-
-
5-(3-methoxyphenyl)-3-(trifluoromethyl)-1H-pyrazole
-
-
5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-amine
-
-
5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-amine
-
-
5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazole-2-carboxamide
-
-
5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazole-2-carboxamide
-
-
5-[4-chloro-5-[(3-chlorobenzyl)oxy]pyridin-2-yl]-1,3,4-oxadiazol-2-amine
-
-
5-[4-chloro-5-[(3-chlorobenzyl)oxy]pyridin-2-yl]-1,3,4-oxadiazol-2-amine
-
-
5-[4-chloro-5-[(3-chlorobenzyl)oxy]pyridin-2-yl]-1,3,4-oxadiazole-2-carboxamide
-
-
5-[4-chloro-5-[(3-chlorobenzyl)oxy]pyridin-2-yl]-1,3,4-oxadiazole-2-carboxamide
-
-
BPP_03B04
-
-
chloramphenicol
-
-
ethyl [3-[3-(difluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetate
-
-
ethyl [3-[3-(difluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetate
-
-
ethyl [3-[3-(trifluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetate
-
-
ethyl [3-[3-(trifluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetate
-
-
Methicillin
-
-
methyl 3-chloro-4-[(3,4-difluorobenzyl)oxy]benzoate
-
-
methyl 3-chloro-4-[(3,4-difluorobenzyl)oxy]benzoate
-
-
methyl 3-chloro-4-[(3-chlorobenzyl)oxy]benzoate
-
-
methyl 3-chloro-4-[(3-chlorobenzyl)oxy]benzoate
-
-
methyl 3-chloro-4-[(3-fluorobenzyl)oxy]benzoate
-
-
methyl 3-chloro-4-[(3-fluorobenzyl)oxy]benzoate
-
-
methyl 4-[(1R,2R)-2-(3-chlorophenyl)-1,2-dihydroxyethyl]-3-methylbenzoate
-
-
methyl 4-[(1R,2R)-2-(3-chlorophenyl)-1,2-dihydroxyethyl]-3-methylbenzoate
-
-
methyl 4-[(1S,2S)-2-(3-chlorophenyl)-1,2-dihydroxyethyl]-3-methylbenzoate
-
-
methyl 4-[(1S,2S)-2-(3-chlorophenyl)-1,2-dihydroxyethyl]-3-methylbenzoate
-
-
methyl 4-[(3-chlorobenzoyl)amino]-3-methylbenzoate
-
-
methyl 4-[(3-chlorobenzoyl)amino]-3-methylbenzoate
-
-
methyl 4-[(3-chlorobenzyl)(methyl)amino]-3-methylbenzoate
-
-
methyl 4-[(3-chlorobenzyl)(methyl)amino]-3-methylbenzoate
-
-
methyl 4-[(3-chlorobenzyl)amino]-3-methylbenzoate
-
-
methyl 4-[(3-chlorobenzyl)amino]-3-methylbenzoate
-
-
methyl 4-[(3-chlorobenzyl)oxy]-3-methylbenzoate
-
-
methyl 4-[(3-chlorobenzyl)oxy]-3-methylbenzoate
-
-
methyl 4-[(3-chlorobenzyl)oxy]benzoate
-
-
methyl 4-[(3-chlorobenzyl)oxy]benzoate
-
-
methyl 4-[(3-chlorophenyl)carbamoyl]benzoate
-
-
methyl 4-[(3-chlorophenyl)carbamoyl]benzoate
-
-
methyl 4-[(E)-2-(3-chlorophenyl)ethenyl]-3-methylbenzoate
-
-
methyl 4-[(E)-2-(3-chlorophenyl)ethenyl]-3-methylbenzoate
-
-
methyl 4-[[(3-chlorophenyl)(methyl)amino]methyl]benzoate
-
-
methyl 4-[[(3-chlorophenyl)(methyl)amino]methyl]benzoate
-
-
methyl 4-[[(3-chlorophenyl)amino]methyl]benzoate
-
-
methyl 4-[[(3-chlorophenyl)amino]methyl]benzoate
-
-
muciproin
-
-
N-(1,1-dioxo-1l6-thiolan-3-yl)-2-[(4-methylphenoxy)methyl]-1,3-thiazole-4-carboxamide
-
-
N-(1,1-dioxo-1l6-thiolan-3-yl)-2-[(4-methylphenoxy)methyl]-1,3-thiazole-4-carboxamide
-
-
N-(1-[3-chloro-4-[(4-chlorobenzyl)oxy]benzyl]pyrrolidin-3-yl)acetamide
-
-
N-(1-[3-chloro-4-[(4-chlorobenzyl)oxy]benzyl]pyrrolidin-3-yl)acetamide
-
-
N-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetamide
-
-
N-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetamide
-
-
N-[2-(1H-indol-3-yl)ethyl]-3-[(1,3-thiazol-2-ylcarbamoyl)amino]benzenesulfonamide
-
IC50: 8 nM
N-[2-(1H-indol-3-yl)ethyl]-3-[(1,3-thiazol-2-ylcarbamoyl)amino]benzenesulfonamide
-
IC50: 8 nM
N-[2-(1H-indol-3-yl)ethyl]-3-[(1,3-thiazol-2-ylcarbamoyl)amino]benzenesulfonamide
-
IC50: 50 nM
N-[2-(1H-indol-3-yl)ethyl]-3-[[(1,3-thiazol-2-yl)carbamoyl]amino]benzene-1-sulfonamide
-
-
N-[2-(1H-indol-3-yl)ethyl]-3-[[(1,3-thiazol-2-yl)carbamoyl]amino]benzene-1-sulfonamide
-
-
N-[2-[1-(methanesulfonyl)cyclopropyl]ethyl]-2-[3-[3-(trifluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetamide
-
-
N-[2-[1-(methanesulfonyl)cyclopropyl]ethyl]-2-[3-[3-(trifluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetamide
-
-
N-[3-[4-(pyridin-2-yl)piperazine-1-sulfonyl]phenyl]-N'-1,3-thiazol-2-ylurea
-
-
N-[3-[4-(pyridin-2-yl)piperazine-1-sulfonyl]phenyl]-N'-1,3-thiazol-2-ylurea
-
-
N6-Benzyladenosine 5'-triphosphate
-
-
N6-Benzyladenosine 5'-triphosphate
-
-
phenyl-thiazolylurea-sulfonamides
-
strong inhibition, several derivatives, competitive to L-phenylalanine
phenyl-thiazolylurea-sulfonamides
-
strong inhibition, several derivatives, competitive to L-phenylalanine, cytotoxic effect
phenyl-thiazolylurea-sulfonamides
-
strong inhibition, several derivatives, competitive to L-phenylalanine, cytotoxic effect
phenyl-thiazolylurea-sulfonamides
-
strong inhibition, several derivatives, competitive to L-phenylalanine, cytotoxic effect
phenyl-thiazolylurea-sulfonamides
-
strong inhibition, several derivatives, competitive to L-phenylalanine, cytotoxic effect
phenyl-thiazolylurea-sulfonamido-aminoethyl-chloroindol
-
-
phenyl-thiazolylurea-sulfonamido-aminoethyl-chloroindol
-
-
phenyl-thiazolylurea-sulfonamido-aminoethyl-chloroindol
-
-
phenyl-thiazolylurea-sulfonamido-aminoethyl-chloroindol
-
-
phenyl-thiazolylurea-sulfonamido-aminoethylindol
-
strong inhibition, competitive to L-phenylalanine, cytotoxic effects on CHO cells and bacteria
phenyl-thiazolylurea-sulfonamido-aminoethylindol
-
strong inhibition, competitive to L-phenylalanine, cytotoxic effects on CHO cells and bacteria
phenyl-thiazolylurea-sulfonamido-aminoethylindol
-
strong inhibition, competitive to L-phenylalanine, cytotoxic effects on CHO cells and bacteria
phenyl-thiazolylurea-sulfonamido-aminoethylindol
-
strong inhibition, competitive to L-phenylalanine, cytotoxic effects on CHO cells and bacteria
PheOH-AMP
-
-
PheOH-AMP
-
L-phenylalaninyl-5'-adenylate, a nonhydrolyzable phenylalanyladenylate analogue, conformational changes in tRNAPhe and the catalytic domain are induced by the PheOH-AMP binding: the motif 2 loop and a helical loop, residues 139-152 of the alpha-subunit, undergo coordinated displacement, Metalpha148 of the helical loop adopts a conformation preventing the 2'-OH group of A76 from approaching the alpha-carbonyl carbon of PheOH-AMP, the unfavorable position of the terminal ribose stems from the absence of the R-carbonyl oxygen in the analogue, overview
Zn2+
-
inhibition is fully reversible by the addition of zinc-complexing agents
Zn2+
-
inhibition of tRNAPhe aminoacylation, required for conversion of ATP into diadenosine 5',5'''-P1,P4-tetraphosphate
Zn2+
-
inhibition of tRNAPhe aminoacylation, required for conversion of ATP into diadenosine 5',5'''-P1,P4-tetraphosphate
[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl](4-methylpiperazin-1-yl)methanone
-
-
[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl](4-methylpiperazin-1-yl)methanone
-
-
[3-chloro-4-[(3-chlorophenoxy)methyl]phenyl](4-methylpiperazin-1-yl)methanone
-
-
[3-chloro-4-[(3-chlorophenoxy)methyl]phenyl](4-methylpiperazin-1-yl)methanone
-
-
[4-([3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]sulfonyl)piperazin-1-yl](4-methylphenyl)methanone
-
-
[4-([3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]sulfonyl)piperazin-1-yl](4-methylphenyl)methanone
-
-
[4-[1-(3-chlorophenyl)-2-hydroxyethyl]-3-methylphenyl](4-methylpiperazin-1-yl)methanone
-
-
[4-[1-(3-chlorophenyl)-2-hydroxyethyl]-3-methylphenyl](4-methylpiperazin-1-yl)methanone
-
-
additional information
the activity of the recombinant enzyme is not affected by L-phenylalanine
-
additional information
-
the activity of the recombinant enzyme is not affected by L-phenylalanine
-
additional information
-
the autoantibody anti-Zo, reactive with phenylalanyltransfer RNA synthetase, immunoprecipitates 155 and 140 kD proteins and is common in children but seems to be associated with malignancy in adults, such as the antisynthetase syndrome, i.e. myositis, ILD, Raynauds disease, and arthralgias, overview
-
additional information
-
the rate of overcharging of the tRNAPhe is dependenton the buffer system used
-
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Brain Diseases
Biophysical characterization Of Alpers encephalopathy associated mutants of human mitochondrial phenylalanyl-tRNA synthetase.
Brain Diseases
Clinical findings in a patient with FARS2 mutations and early-infantile-encephalopathy with epilepsy.
Brain Diseases
Early-onset epileptic encephalopathy with migrating focal seizures associated with a FARS2 homozygous nonsense variant.
Brain Diseases
FARS2 deficiency; new cases, review of clinical, biochemical, and molecular spectra, and variants interpretation based on structural, functional, and evolutionary significance.
Brain Diseases
FARS2 mutation and epilepsy: Possible link with early-onset epileptic encephalopathy.
Brain Diseases
FARS2 mutations presenting with pure spastic paraplegia and lesions of the dentate nuclei.
Brain Diseases
FARS2 Mutations: More Than Two Phenotypes? A Case Report.
Brain Diseases
Mitochondrial phenylalanyl-tRNA synthetase mutations underlie fatal infantile Alpers encephalopathy.
Brain Diseases
Mutations in FARS2 and non-fatal mitochondrial dysfunction in two siblings.
Brain Diseases
Novel FARS2 variants in patients with early onset encephalopathy with or without epilepsy associated with long survival.
Carcinoma, Hepatocellular
A comparison of phenylalanyl-tRNA synthetase from rat liver and a minimal deviation hepatoma.
Carcinoma, Hepatocellular
Effects of ochratoxin A metabolites on yeast phenylalanyl-tRNA synthetase and on the growth and in vivo protein synthesis of hepatoma cells.
Cardiovascular Diseases
Developmental Angiogenesis Requires the Mitochondrial Phenylalanyl-tRNA Synthetase.
Cystic Fibrosis
Improving the phenotype risk score as a scalable approach to identifying patients with Mendelian disease.
Cytochrome-c Oxidase Deficiency
Mutation of the human mitochondrial phenylalanine-tRNA synthetase causes infantile-onset epilepsy and cytochrome c oxidase deficiency.
Dermatomyositis
Autoantibodies and their significance in myositis.
Diabetes Mellitus
Genetic polymorphisms associated with oxaliplatin-induced peripheral neurotoxicity in Japanese patients with colorectal cancer.
Diffuse Cerebral Sclerosis of Schilder
Mitochondrial phenylalanyl-tRNA synthetase mutations underlie fatal infantile Alpers encephalopathy.
Diffuse Cerebral Sclerosis of Schilder
Novel Compound Heterozygous Mutations Expand the Recognized Phenotypes of FARS2-Linked Disease.
Drug Resistant Epilepsy
A patient with juvenile-onset refractory status epilepticus caused by two novel compound heterozygous mutations in FARS2 gene.
Drug Resistant Epilepsy
Novel Compound Heterozygous Mutations Expand the Recognized Phenotypes of FARS2-Linked Disease.
Dysarthria
Mutations in FARS2 and non-fatal mitochondrial dysfunction in two siblings.
Dysphonia
FARS2 Causing Complex Hereditary Spastic Paraplegia With Dysphonia: Expanding the Disease Spectrum.
Epilepsies, Myoclonic
Novel FARS2 variants in patients with early onset encephalopathy with or without epilepsy associated with long survival.
Epilepsy
Clinical findings in a patient with FARS2 mutations and early-infantile-encephalopathy with epilepsy.
Epilepsy
Early-onset epileptic encephalopathy with migrating focal seizures associated with a FARS2 homozygous nonsense variant.
Epilepsy
FARS2 mutation and epilepsy: Possible link with early-onset epileptic encephalopathy.
Epilepsy
Mitochondrial phenylalanyl-tRNA synthetase mutations underlie fatal infantile Alpers encephalopathy.
Epilepsy
Mutation of the human mitochondrial phenylalanine-tRNA synthetase causes infantile-onset epilepsy and cytochrome c oxidase deficiency.
Epilepsy
Mutations in FARS2 and non-fatal mitochondrial dysfunction in two siblings.
Epilepsy
Novel FARS2 variants in patients with early onset encephalopathy with or without epilepsy associated with long survival.
Leigh Disease
Novel Compound Heterozygous Mutations Expand the Recognized Phenotypes of FARS2-Linked Disease.
Leukemia, Myelogenous, Chronic, BCR-ABL Positive
Human phenylalanyl-tRNA synthetase: cloning, characterization of the deduced amino acid sequences in terms of the structural domains and coordinately regulated expression of the alpha and beta subunits in chronic myeloid leukemia cells.
Leukemia, Myeloid
Expression of a gene encoding a tRNA synthetase-like protein is enhanced in tumorigenic human myeloid leukemia cells and is cell cycle stage- and differentiation-dependent.
Lung Diseases, Interstitial
Autoantibodies and their significance in myositis.
Malaria
Plasmodium falciparum mitochondria import tRNAs along with an active phenylalanyl-tRNA synthetase.
Mitochondrial Diseases
A patient with juvenile-onset refractory status epilepticus caused by two novel compound heterozygous mutations in FARS2 gene.
Mitochondrial Diseases
Clinical findings in a patient with FARS2 mutations and early-infantile-encephalopathy with epilepsy.
Mitochondrial Diseases
Mutation of the human mitochondrial phenylalanine-tRNA synthetase causes infantile-onset epilepsy and cytochrome c oxidase deficiency.
Mitochondrial Diseases
Mutations in FARS2 and non-fatal mitochondrial dysfunction in two siblings.
Muscle Hypotonia
Novel FARS2 variants in patients with early onset encephalopathy with or without epilepsy associated with long survival.
Muscle Spasticity
Novel FARS2 variants in patients with early onset encephalopathy with or without epilepsy associated with long survival.
Myoclonus
Novel Compound Heterozygous Mutations Expand the Recognized Phenotypes of FARS2-Linked Disease.
Neoplasms
Autoantibodies and their significance in myositis.
Neoplasms
Contribution of upregulated aminoacyl-tRNA biosynthesis to metabolic dysregulation in gastric cancer.
Neurodegenerative Diseases
A Newly Identified Missense Mutation in FARS2 Causes Autosomal-Recessive Spastic Paraplegia.
Pancreatic Neoplasms
Phenotype risk scores (PheRS) for pancreatic cancer using time-stamped electronic health record data: Discovery and validation in two large biobanks.
Paraplegia
A Newly Identified Missense Mutation in FARS2 Causes Autosomal-Recessive Spastic Paraplegia.
Paraplegia
Biophysical characterization Of Alpers encephalopathy associated mutants of human mitochondrial phenylalanyl-tRNA synthetase.
Paraplegia
FARS2 deficiency; new cases, review of clinical, biochemical, and molecular spectra, and variants interpretation based on structural, functional, and evolutionary significance.
Paraplegia
FARS2 mutations presenting with pure spastic paraplegia and lesions of the dentate nuclei.
Paraplegia
FARS2 Mutations: More Than Two Phenotypes? A Case Report.
Paraplegia
New insights into the phenotype of FARS2 deficiency.
Paraplegia
Novel FARS2 variants in patients with early onset encephalopathy with or without epilepsy associated with long survival.
phenylalanine-trna ligase deficiency
Developmental Angiogenesis Requires the Mitochondrial Phenylalanyl-tRNA Synthetase.
phenylalanine-trna ligase deficiency
FARS2 deficiency; new cases, review of clinical, biochemical, and molecular spectra, and variants interpretation based on structural, functional, and evolutionary significance.
phenylalanine-trna ligase deficiency
FARSA mutations mimic phenylalanyl-tRNA synthetase deficiency caused by FARSB defects.
phenylalanine-trna ligase deficiency
Metabolic stroke-like episode in a child with FARS2 mutation and SARS-CoV-2 positive cerebrospinal fluid.
phenylalanine-trna ligase deficiency
New insights into the phenotype of FARS2 deficiency.
Seizures
Clinical findings in a patient with FARS2 mutations and early-infantile-encephalopathy with epilepsy.
Seizures
Early-onset epileptic encephalopathy with migrating focal seizures associated with a FARS2 homozygous nonsense variant.
Spastic Paraplegia, Hereditary
FARS2 Causing Complex Hereditary Spastic Paraplegia With Dysphonia: Expanding the Disease Spectrum.
Starvation
Regulation of E.coli phenylalanyl-tRNA synthetase operon in vivo.
Status Epilepticus
A patient with juvenile-onset refractory status epilepticus caused by two novel compound heterozygous mutations in FARS2 gene.
Tremor
Mutations in FARS2 and non-fatal mitochondrial dysfunction in two siblings.
Tuberculosis
Re-discovery of PF-3845 as a new chemical scaffold inhibiting phenylalanyl-tRNA synthetase in Mycobacterium tuberculosis.
Tuberculosis
Rediscovery of PF-3845 as a new chemical scaffold inhibiting phenylalanyl-tRNA synthetase in Mycobacterium tuberculosis.
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0.00016
(s-pA)tRNAPhe
-
-
-
0.00017
(s-pG)tRNAPhe
-
-
-
0.085 - 0.4
2'-deoxyadenosine 5'-triphosphate
0.05 - 0.2
2-Chloroadenosine 5'-triphosphate
1.54
2-deoxyadenosine 5'-triphosphate
-
aminoacylation
2
2-L-naphthylalanine
-
mutant enzyme N412G/T415G/S418C/S437F, at pH 7.6, temperature not specified in the publication
0.3107
2-L-tyrosine
-
at pH 7.5 and 37°C
0.3
3'-deoxadenosine 5'-triphosphate
-
cytoplasmic
0.82 - 1
3'-Deoxyadenosine 5'-triphosphate
0.38 - 0.65
3,4-dihydroxy-L-phenylalanine
1.15
3-L-tyrosine
-
at pH 7.5 and 37°C
923
benzofuranylalanine
-
-
0.012 - 0.13
DL-m-tyrosine
0.00048 - 11
L-phenylalanine
1.4
L-tryptophan
-
mutant enzyme N412G/T415G/S418C/S437F, at pH 7.6, temperature not specified in the publication
0.86
L-Tyr
-
pH 7.2, 37°C, cytosolic enzyme
0.81
N6-methyladenosine 5'-triphosphate
-
aminoacylation
additional information
additional information
-
0.085
2'-deoxyadenosine 5'-triphosphate
-
mitochondrial
0.125
2'-deoxyadenosine 5'-triphosphate
-
-
0.19
2'-deoxyadenosine 5'-triphosphate
-
cytoplasmic
0.4
2'-deoxyadenosine 5'-triphosphate
-
cytoplasmic
0.05
2-Chloroadenosine 5'-triphosphate
-
aminoacylation
0.096
2-Chloroadenosine 5'-triphosphate
-
mitochondrial
0.11
2-Chloroadenosine 5'-triphosphate
-
-
0.16
2-Chloroadenosine 5'-triphosphate
-
cytoplasmic
0.16
2-Chloroadenosine 5'-triphosphate
-
mitochondrial
0.2
2-Chloroadenosine 5'-triphosphate
-
-
0.2
2-Chloroadenosine 5'-triphosphate
-
mitochondrial, 3'-deoxyadenosine 5'-triphosphate
0.2
2-Chloroadenosine 5'-triphosphate
-
cytoplasmic, 2'-deoxyadenosine 5'-triphosphate
0.82
3'-Deoxyadenosine 5'-triphosphate
-
aminoacylation
1
3'-Deoxyadenosine 5'-triphosphate
-
mitochondrial
0.38
3,4-dihydroxy-L-phenylalanine
-
in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.6
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
0.65
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
0.0058
ATP
-
-
0.055
ATP
-
ATP, , mitochondrial, aminoacylation
0.055
ATP
-
mitochondrial
0.06
ATP
-
aminoacylation
0.065
ATP
-
aminoacylation
0.065
ATP
-
mitochondrial
0.08
ATP
-
cytoplasmic, aminoacylation
0.122
ATP
-
recombinant enzyme, pH 7.9, 22°C
0.14
ATP
-
ATP, , cytoplasmic, aminoacylation
0.147
ATP
-
native enzyme, pH 7.9, 22°C
0.2
ATP
-
at pH 7.5 and 37°C
0.225
ATP
-
at pH 7.5 and 37°C
0.62
ATP
-
mitochondrial, ATP-diphosphate exchange
0.7
ATP
-
mitochondrial, ATP-diphosphate exchange
0.84
ATP
-
cytoplasmic, ATP-diphosphate exchange
0.9
ATP
-
cytoplasmic, ATP-diphosphate exchange
2.5
ATP
ATP-diphosphate exchange reaction, recombinant mitochondrial isozyme, pH 7.3, 37°C
0.012
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
0.13
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
0.0018
L-Phe
-
-
0.0042
L-Phe
-
pH 7.2, 37°C, mitochondrial enzyme
0.0103
L-Phe
-
wild-type enzyme
0.0212
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit
0.0225
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and T354W mutation in beta-subunit
0.0261
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and E334A mutation in beta-subunit
0.0282
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and A356W mutation in beta-subunit
0.03
L-Phe
-
pH 7.2, 37°C, cytosolic enzyme
0.0312
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and H265L mutation in beta-subunit
0.0331
L-Phe
-
mutant enzyme with A294G mutation in alpha-subunit and H265A mutation in beta-subunit
0.00048
L-phenylalanine
-
pH 7.8, 60°C
0.00057
L-phenylalanine
mitochondrial chimeric enzyme with implanted editing module from Escherichia coli phenylalanine-tRNA synthetase, at pH 8.5 and 37°C
0.00084
L-phenylalanine
wild type mitochondrial enzyme, at pH 8.5 and 37°C
0.00094
L-phenylalanine
-
recombinant enzyme, pH 7.9, 22°C
0.0012
L-phenylalanine
-
native enzyme, pH 7.9, 22°C
0.0015
L-phenylalanine
-
25°C
0.0015
L-phenylalanine
-
pH 7.8, 70°C
0.0017
L-phenylalanine
-
in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.002
L-phenylalanine
-
wild-type EcPheRS
0.0024
L-phenylalanine
wild type enzyme, at pH 8.5 and 37°C
0.0026
L-phenylalanine
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.003
L-phenylalanine
-
wild-type ctPheRS
0.0032
L-phenylalanine
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.0045
L-phenylalanine
-
mutant A294G EcPheRS
0.0049
L-phenylalanine
-
pH 7.2, 37°C, truncated mutant PheRSDELTAB2A294G
0.005
L-phenylalanine
-
wild-type mtPheRS
0.0053
L-phenylalanine
-
pH 7.2, 37°C, full-length PheRSA294G
0.0056
L-phenylalanine
mutant enzyme H99D, at pH 8.5 and 37°C
0.012
L-phenylalanine
mutant enzyme R117G, at pH 8.5 and 37°C
0.017
L-phenylalanine
-
mutant A333G mtPheRS
0.021
L-phenylalanine
-
at pH 7.5 and 37°C
0.033
L-phenylalanine
ATP-diphosphate exchange reaction, recombinant mitochondrial isozyme, pH 7.3, 37°C
0.0423
L-phenylalanine
-
at pH 7.5 and 37°C
0.048
L-phenylalanine
-
at pH 7.5 and 37°C
0.233
L-phenylalanine
-
mutant G458A ctPheRS
11
L-phenylalanine
-
mutant enzyme N412G/T415G/S418C/S437F, at pH 7.6, temperature not specified in the publication
0.32
L-tyrosine
-
mutant A294G EcPheRS
0.637
L-tyrosine
-
wild-type ctPheRS
0.66
L-tyrosine
-
mutant A333G mtPheRS
1.155
L-tyrosine
-
wild-type mtPheRS
1.9
L-tyrosine
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
2.2
L-tyrosine
-
wild-type EcPheRS
3
L-tyrosine
-
mutant G458A ctPheRS
0.00045
Phe
-
-
0.0094
Phe
-
cytoplasmic, aminoacylation
0.011
Phe
-
mitochondrial, aminoacylation
0.012
Phe
-
mitochondrial, aminoacylation
0.013
Phe
-
cytoplasmic, aminoacylation
0.029
Phe
-
mitochondrial, ATP-diphosphate exchange
0.033
Phe
-
cytoplasmic, ATP-diphosphate exchange
0.034
Phe
-
mitochondrial, ATP-diphosphate exchange
0.038
Phe
-
mitochondrial, ATP-diphosphate exchange
0.000066
tRNAPhe
-
-
0.0001
tRNAPhe
-
recombinant heterodimer, pH 8.0, 25°C
0.00011
tRNAPhe
-
recombinant His-tagged heterodimer, pH 8.0, 25°C
0.00012
tRNAPhe
-
substrate from yeast, , aminoacylation
0.00017
tRNAPhe
-
substrate from yeast
0.0002
tRNAPhe
-
substrate from calf liver, , cytoplasmic, aminoacylation
0.00036
tRNAPhe
mutant enzyme T210M, at pH 8.5 and 37°C
0.00042
tRNAPhe
-
cytoplasmic enzyme, aminoacylation
0.00042
tRNAPhe
-
mitochondrial enzyme, calf liver tRNAPhe
0.00052
tRNAPhe
-
substrate from calf liver, , mitochondrial, aminoacylation
0.00058
tRNAPhe
-
substrate from calf liver, , mitochondrial, aminoacylation
0.00065
tRNAPhe
-
substrate from yeast, , aminoacylation
0.00078
tRNAPhe
-
substrate from yeast, , mitochondrial, aminoacylation
0.00094
tRNAPhe
-
at pH 7.5 and 37°C
0.001
tRNAPhe
mutant enzyme D289Y, at pH 8.5 and 37°C
0.0011
tRNAPhe
mutant enzyme P49A, at pH 8.5 and 37°C
0.0012
tRNAPhe
-
at pH 7.5 and 37°C
0.0012
tRNAPhe
wild type enzyme, at pH 8.5 and 37°C
0.0012
tRNAPhe
mutant enzyme R387Q, at pH 8.5 and 37°C
0.0021
tRNAPhe
mutant enzyme R383C, at pH 8.5 and 37°C
0.0022
tRNAPhe
-
pH 7.2, 37°C, full-length PheRSA294G, substrate from Saccharomyces cerevisiae
0.0025
tRNAPhe
-
pH 7.2, 37°C, truncated mutant PheRSDELTAB2A294G, substrate from Escherichia coli
0.0027
tRNAPhe
-
pH 7.2, 37°C, full-length PheRSA294G, substrate from Escherichia coli
0.0032
tRNAPhe
-
substrate from E. coli
0.0041
tRNAPhe
-
pH 7.2, 37°C, truncated mutant PheRSDELTAB2A294G, substrate from Saccharomyces cerevisiae
0.018
tRNAPhe
aminoacylation reaction, recombinant mitochondrial isozyme, pH 7.5, 37°C
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
Km value for aminoacylation of tRNAPhe-C-C-A or tRNAPhe-C-C-A(3'NH2) with various amino acids
-
additional information
additional information
-
Km-value for tRNA mutants
-
additional information
additional information
-
Km-values for mutant yeast tRNAPhe transcripts
-
additional information
additional information
-
Km-values for mutant yeast tRNAPhe transcripts
-
additional information
additional information
-
negative cooperativity exists in the binding of all substrates
-
additional information
additional information
-
kinetics, binding energies in the active conformation
-
additional information
additional information
-
aminoacylation kinetics with Phe and Tyr
-
additional information
additional information
-
full-length PheRSA294G and truncated mutant PheRSDELTAB2A294G show comparable kinetics for in vitro aminoacylation, kinetics, overview
-
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0.000067 - 0.0037
(4-[4-[(3-chlorobenzyl)oxy]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
0.00028 - 0.011
(4-[4-[2-(3-chlorophenyl)-2-hydroxyethyl]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
0.000011 - 0.00011
(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetic acid
0.00083 - 0.00098
1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)[2,2'-binaphthalene]-8,8'-dicarbaldehyde
0.00015
1-[4-[(3-chlorobenzyl)oxy]-3-methylbenzoyl]piperidine-4-carboxamide
-
-
0.00036 - 0.046
1-[4-[2-(3-chlorophenyl)ethyl]-3-methylbenzoyl]piperidine-4-carboxamide
0.064
1-[[2-(3-chlorophenyl)-1-methyl-4-oxo-1,4-dihydroquinazolin-6-yl]carbonyl]piperidine-4-carboxamide
0.0000017 - 0.000126
2-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetamide
0.0000031 - 0.000087
2-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)ethanol
0.064
2-chloro-N-(3-chlorophenyl)-4-[(4-methyl-3-oxopiperazin-1-yl)carbonyl]benzenesulfonamide
0.23
2-phenylacetamidine
-
-
0.000011 - 0.000156
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazole
0.0000055 - 0.000081
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfanyl)-1,3,4-oxadiazole
0.0000015 - 0.000036
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfinyl)-1,3,4-oxadiazole
0.0000021 - 0.000053
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfonyl)-1,3,4-oxadiazole
0.000011 - 0.000076
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-ethyl-1,3,4-oxadiazole
0.0000066 - 0.000095
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-methyl-1,3,4-oxadiazole
0.000029 - 0.000483
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(1-hydroxypropan-2-yl)benzamide
0.000022 - 0.000254
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(4-hydroxybutyl)benzamide
0.000057 - 0.000393
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(cyclopropylmethyl)benzamide
0.0000019 - 0.000079
3-chloro-4-[(3-chlorobenzyl)oxy]-N-[2-(ethylamino)ethyl]-N-methylbenzenesulfonamide
0.000014 - 0.000438
3-chloro-4-[(3-chlorobenzyl)oxy]-N-[2-(morpholin-4-yl)ethyl]benzamide
0.064
3-chloro-N-[2-methyl-4-[(4-methyl-3-oxopiperazin-1-yl)carbonyl]phenyl]benzenesulfonamide
0.0024 - 0.023
4-(3-chloro-4-[[(3-chlorophenyl)sulfinyl]methyl]benzoyl)-1-methylpiperazin-2-one
0.064
4-(3-chloro-4-[[(3-chlorophenyl)sulfonyl]methyl]benzoyl)-1-methylpiperazin-2-one
0.000012 - 0.000097
4-chloro-5-[(3-chlorobenzyl)oxy]-2-(1,3,4-oxadiazol-2-yl)pyridine
0.000024 - 0.000034
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(1-ethyl-1H-pyrazol-5-yl)pyridine-2-carboxamide
0.000043 - 0.000046
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(1-hydroxypropan-2-yl)pyridine-2-carboxamide
0.000016 - 0.000034
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(4-hydroxybutyl)pyridine-2-carboxamide
0.0000015 - 0.000028
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(4-hydroxycyclohexyl)pyridine-2-carboxamide
0.00003 - 0.00005
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(cyclopropylmethyl)pyridine-2-carboxamide
0.000008 - 0.000065
4-chloro-5-[(3-chlorobenzyl)oxy]-N-[2-(morpholin-4-yl)ethyl]pyridine-2-carboxamide
0.000038 - 0.0013
4-[3-chloro-4-[(3-chlorobenzyl)oxy]benzoyl]-1-methylpiperazin-2-one
0.0000023 - 0.000042
5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-amine
0.0000026 - 0.000081
5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazole-2-carboxamide
0.00005
5-[4-chloro-5-[(3-chlorobenzyl)oxy]pyridin-2-yl]-1,3,4-oxadiazol-2-amine
-
-
0.0000027 - 0.00006
5-[4-chloro-5-[(3-chlorobenzyl)oxy]pyridin-2-yl]-1,3,4-oxadiazole-2-carboxamide
0.077
benzylguanidine
-
-
0.00083 - 0.00098
BPP_03B04
0.0136 - 0.15
DL-m-tyrosine
0.085 - 0.089
L-phenylalanyl-5'-adenylate
3.4
L-tyrosine
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.043 - 0.045
L-tyrosyl-adenylate
0.0000087 - 0.00012
methyl 3-chloro-4-[(3,4-difluorobenzyl)oxy]benzoate
0.000017 - 0.000091
methyl 3-chloro-4-[(3-chlorobenzyl)oxy]benzoate
0.00003 - 0.00016
methyl 3-chloro-4-[(3-fluorobenzyl)oxy]benzoate
0.064
methyl 4-[(1R,2R)-2-(3-chlorophenyl)-1,2-dihydroxyethyl]-3-methylbenzoate
0.0065 - 0.064
methyl 4-[(1S,2S)-2-(3-chlorophenyl)-1,2-dihydroxyethyl]-3-methylbenzoate
0.064
methyl 4-[(3-chlorobenzoyl)amino]-3-methylbenzoate
0.00017 - 0.0035
methyl 4-[(3-chlorobenzyl)(methyl)amino]-3-methylbenzoate
0.0035 - 0.0061
methyl 4-[(3-chlorobenzyl)amino]-3-methylbenzoate
0.000034 - 0.000097
methyl 4-[(3-chlorobenzyl)oxy]-3-methylbenzoate
0.0031 - 0.012
methyl 4-[(3-chlorobenzyl)oxy]benzoate
0.064
methyl 4-[(3-chlorophenyl)carbamoyl]benzoate
0.00013 - 0.002
methyl 4-[(E)-2-(3-chlorophenyl)ethenyl]-3-methylbenzoate
0.064
methyl 4-[[(3-chlorophenyl)(methyl)amino]methyl]benzoate
0.057 - 0.064
methyl 4-[[(3-chlorophenyl)amino]methyl]benzoate
0.00024 - 0.0022
N-(1-[3-chloro-4-[(4-chlorobenzyl)oxy]benzyl]pyrrolidin-3-yl)acetamide
0.0000013 - 0.000028
N-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetamide
0.00014
N-benzyl-D-amphetamine
-
-
0.058
N-benzylbenzamidine
-
-
0.000021
phenyl-thiazolylurea-sulfonamido-aminoethylindole
-
pH 7.6, 22°C
0.00069
tRNAPhe Cp75
-
25°C
-
0.00071
tRNAPhe s4-U75
-
25°C
-
0.00064
tRNAPhe s4-U76
-
25°C
-
0.0004
tRNAPhe s4-U77
-
25°C
-
0.00035
tRNAPhe s4-Up77
-
25°C
-
0.00015 - 0.0023
[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl](4-methylpiperazin-1-yl)methanone
0.00084
[3-chloro-4-[(3-chlorophenoxy)methyl]phenyl](4-methylpiperazin-1-yl)methanone
-
-
0.0000019 - 0.000012
[4-([3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]sulfonyl)piperazin-1-yl](4-methylphenyl)methanone
0.0064 - 0.064
[4-[1-(3-chlorophenyl)-2-hydroxyethyl]-3-methylphenyl](4-methylpiperazin-1-yl)methanone
additional information
additional information
-
0.000067
(4-[4-[(3-chlorobenzyl)oxy]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
-
-
0.0037
(4-[4-[(3-chlorobenzyl)oxy]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
-
-
0.00028
(4-[4-[2-(3-chlorophenyl)-2-hydroxyethyl]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
-
-
0.011
(4-[4-[2-(3-chlorophenyl)-2-hydroxyethyl]-3-methylbenzoyl]piperazin-1-yl)(tetrahydrofuran-2-yl)methanone
-
-
0.000011
(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetic acid
-
-
0.00011
(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetic acid
-
-
0.00083
1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)[2,2'-binaphthalene]-8,8'-dicarbaldehyde
-
at pH 7.5 and 37°
0.00098
1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)[2,2'-binaphthalene]-8,8'-dicarbaldehyde
-
at pH 7.5 and 37°
0.00036
1-[4-[2-(3-chlorophenyl)ethyl]-3-methylbenzoyl]piperidine-4-carboxamide
-
-
0.046
1-[4-[2-(3-chlorophenyl)ethyl]-3-methylbenzoyl]piperidine-4-carboxamide
-
-
0.064
1-[[2-(3-chlorophenyl)-1-methyl-4-oxo-1,4-dihydroquinazolin-6-yl]carbonyl]piperidine-4-carboxamide
-
larger than 0.064
0.064
1-[[2-(3-chlorophenyl)-1-methyl-4-oxo-1,4-dihydroquinazolin-6-yl]carbonyl]piperidine-4-carboxamide
-
larger than 0.064
0.0000017
2-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetamide
-
-
0.000126
2-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetamide
-
-
0.0000031
2-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)ethanol
-
-
0.000087
2-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)ethanol
-
-
0.064
2-chloro-N-(3-chlorophenyl)-4-[(4-methyl-3-oxopiperazin-1-yl)carbonyl]benzenesulfonamide
-
larger than 0.064
0.064
2-chloro-N-(3-chlorophenyl)-4-[(4-methyl-3-oxopiperazin-1-yl)carbonyl]benzenesulfonamide
-
larger than 0.064
0.000011
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazole
-
-
0.000156
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazole
-
-
0.0000055
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfanyl)-1,3,4-oxadiazole
-
-
0.000081
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfanyl)-1,3,4-oxadiazole
-
-
0.0000015
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfinyl)-1,3,4-oxadiazole
-
-
0.000036
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfinyl)-1,3,4-oxadiazole
-
-
0.0000021
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfonyl)-1,3,4-oxadiazole
-
-
0.000053
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-(methylsulfonyl)-1,3,4-oxadiazole
-
-
0.000011
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-ethyl-1,3,4-oxadiazole
-
-
0.000076
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-ethyl-1,3,4-oxadiazole
-
-
0.0000066
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-methyl-1,3,4-oxadiazole
-
-
0.000095
2-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-5-methyl-1,3,4-oxadiazole
-
-
0.000029
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(1-hydroxypropan-2-yl)benzamide
-
-
0.000483
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(1-hydroxypropan-2-yl)benzamide
-
-
0.000022
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(4-hydroxybutyl)benzamide
-
-
0.000254
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(4-hydroxybutyl)benzamide
-
-
0.000057
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(cyclopropylmethyl)benzamide
-
-
0.000393
3-chloro-4-[(3-chlorobenzyl)oxy]-N-(cyclopropylmethyl)benzamide
-
-
0.0000019
3-chloro-4-[(3-chlorobenzyl)oxy]-N-[2-(ethylamino)ethyl]-N-methylbenzenesulfonamide
-
-
0.000079
3-chloro-4-[(3-chlorobenzyl)oxy]-N-[2-(ethylamino)ethyl]-N-methylbenzenesulfonamide
-
-
0.000014
3-chloro-4-[(3-chlorobenzyl)oxy]-N-[2-(morpholin-4-yl)ethyl]benzamide
-
-
0.000438
3-chloro-4-[(3-chlorobenzyl)oxy]-N-[2-(morpholin-4-yl)ethyl]benzamide
-
-
0.064
3-chloro-N-[2-methyl-4-[(4-methyl-3-oxopiperazin-1-yl)carbonyl]phenyl]benzenesulfonamide
-
larger than 0.064
0.064
3-chloro-N-[2-methyl-4-[(4-methyl-3-oxopiperazin-1-yl)carbonyl]phenyl]benzenesulfonamide
-
larger than 0.064
0.0024
4-(3-chloro-4-[[(3-chlorophenyl)sulfinyl]methyl]benzoyl)-1-methylpiperazin-2-one
-
-
0.023
4-(3-chloro-4-[[(3-chlorophenyl)sulfinyl]methyl]benzoyl)-1-methylpiperazin-2-one
-
-
0.064
4-(3-chloro-4-[[(3-chlorophenyl)sulfonyl]methyl]benzoyl)-1-methylpiperazin-2-one
-
larger than 0.064
0.064
4-(3-chloro-4-[[(3-chlorophenyl)sulfonyl]methyl]benzoyl)-1-methylpiperazin-2-one
-
larger than 0.064
0.000012
4-chloro-5-[(3-chlorobenzyl)oxy]-2-(1,3,4-oxadiazol-2-yl)pyridine
-
-
0.000097
4-chloro-5-[(3-chlorobenzyl)oxy]-2-(1,3,4-oxadiazol-2-yl)pyridine
-
-
0.000024
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(1-ethyl-1H-pyrazol-5-yl)pyridine-2-carboxamide
-
-
0.000034
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(1-ethyl-1H-pyrazol-5-yl)pyridine-2-carboxamide
-
-
0.000043
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(1-hydroxypropan-2-yl)pyridine-2-carboxamide
-
-
0.000046
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(1-hydroxypropan-2-yl)pyridine-2-carboxamide
-
-
0.000016
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(4-hydroxybutyl)pyridine-2-carboxamide
-
-
0.000034
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(4-hydroxybutyl)pyridine-2-carboxamide
-
-
0.0000015
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(4-hydroxycyclohexyl)pyridine-2-carboxamide
-
-
0.000028
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(4-hydroxycyclohexyl)pyridine-2-carboxamide
-
-
0.00003
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(cyclopropylmethyl)pyridine-2-carboxamide
-
-
0.00005
4-chloro-5-[(3-chlorobenzyl)oxy]-N-(cyclopropylmethyl)pyridine-2-carboxamide
-
-
0.000008
4-chloro-5-[(3-chlorobenzyl)oxy]-N-[2-(morpholin-4-yl)ethyl]pyridine-2-carboxamide
-
-
0.000065
4-chloro-5-[(3-chlorobenzyl)oxy]-N-[2-(morpholin-4-yl)ethyl]pyridine-2-carboxamide
-
-
0.000038
4-[3-chloro-4-[(3-chlorobenzyl)oxy]benzoyl]-1-methylpiperazin-2-one
-
-
0.0013
4-[3-chloro-4-[(3-chlorobenzyl)oxy]benzoyl]-1-methylpiperazin-2-one
-
-
0.0000023
5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-amine
-
-
0.000042
5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-amine
-
-
0.0000026
5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazole-2-carboxamide
-
-
0.000081
5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazole-2-carboxamide
-
-
0.0000027
5-[4-chloro-5-[(3-chlorobenzyl)oxy]pyridin-2-yl]-1,3,4-oxadiazole-2-carboxamide
-
-
0.00006
5-[4-chloro-5-[(3-chlorobenzyl)oxy]pyridin-2-yl]-1,3,4-oxadiazole-2-carboxamide
-
-
0.00083
BPP_03B04
-
at pH 7.5 and 37°C
0.00098
BPP_03B04
-
at pH 7.5 and 37°C
0.0136
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
0.15
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
0.085
L-phenylalanyl-5'-adenylate
-
versus ATP
0.089
L-phenylalanyl-5'-adenylate
-
versus L-Phe
0.043
L-tyrosyl-adenylate
-
versus ATP
0.045
L-tyrosyl-adenylate
-
versus L-Phe
0.0000087
methyl 3-chloro-4-[(3,4-difluorobenzyl)oxy]benzoate
-
-
0.00012
methyl 3-chloro-4-[(3,4-difluorobenzyl)oxy]benzoate
-
-
0.000017
methyl 3-chloro-4-[(3-chlorobenzyl)oxy]benzoate
-
-
0.000091
methyl 3-chloro-4-[(3-chlorobenzyl)oxy]benzoate
-
-
0.00003
methyl 3-chloro-4-[(3-fluorobenzyl)oxy]benzoate
-
-
0.00016
methyl 3-chloro-4-[(3-fluorobenzyl)oxy]benzoate
-
-
0.064
methyl 4-[(1R,2R)-2-(3-chlorophenyl)-1,2-dihydroxyethyl]-3-methylbenzoate
-
larger than 0.064
0.064
methyl 4-[(1R,2R)-2-(3-chlorophenyl)-1,2-dihydroxyethyl]-3-methylbenzoate
-
larger than 0.064
0.0065
methyl 4-[(1S,2S)-2-(3-chlorophenyl)-1,2-dihydroxyethyl]-3-methylbenzoate
-
-
0.064
methyl 4-[(1S,2S)-2-(3-chlorophenyl)-1,2-dihydroxyethyl]-3-methylbenzoate
-
larger than 0.064
0.064
methyl 4-[(3-chlorobenzoyl)amino]-3-methylbenzoate
-
larger than 0.064
0.064
methyl 4-[(3-chlorobenzoyl)amino]-3-methylbenzoate
-
larger than 0.064
0.00017
methyl 4-[(3-chlorobenzyl)(methyl)amino]-3-methylbenzoate
-
-
0.0035
methyl 4-[(3-chlorobenzyl)(methyl)amino]-3-methylbenzoate
-
-
0.0035
methyl 4-[(3-chlorobenzyl)amino]-3-methylbenzoate
-
-
0.0061
methyl 4-[(3-chlorobenzyl)amino]-3-methylbenzoate
-
-
0.000034
methyl 4-[(3-chlorobenzyl)oxy]-3-methylbenzoate
-
-
0.000097
methyl 4-[(3-chlorobenzyl)oxy]-3-methylbenzoate
-
-
0.0031
methyl 4-[(3-chlorobenzyl)oxy]benzoate
-
-
0.012
methyl 4-[(3-chlorobenzyl)oxy]benzoate
-
-
0.064
methyl 4-[(3-chlorophenyl)carbamoyl]benzoate
-
larger than 0.064
0.064
methyl 4-[(3-chlorophenyl)carbamoyl]benzoate
-
larger than 0.064
0.00013
methyl 4-[(E)-2-(3-chlorophenyl)ethenyl]-3-methylbenzoate
-
-
0.002
methyl 4-[(E)-2-(3-chlorophenyl)ethenyl]-3-methylbenzoate
-
-
0.064
methyl 4-[[(3-chlorophenyl)(methyl)amino]methyl]benzoate
-
larger than 0.064
0.064
methyl 4-[[(3-chlorophenyl)(methyl)amino]methyl]benzoate
-
larger than 0.064
0.057
methyl 4-[[(3-chlorophenyl)amino]methyl]benzoate
-
-
0.064
methyl 4-[[(3-chlorophenyl)amino]methyl]benzoate
-
larger than 0.064
0.00024
N-(1-[3-chloro-4-[(4-chlorobenzyl)oxy]benzyl]pyrrolidin-3-yl)acetamide
-
-
0.0022
N-(1-[3-chloro-4-[(4-chlorobenzyl)oxy]benzyl]pyrrolidin-3-yl)acetamide
-
-
0.0000013
N-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetamide
-
-
0.000028
N-(5-[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]-1,3,4-oxadiazol-2-yl)acetamide
-
-
0.00015
[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl](4-methylpiperazin-1-yl)methanone
-
-
0.0023
[3-chloro-4-[(3-chlorobenzyl)oxy]phenyl](4-methylpiperazin-1-yl)methanone
-
-
0.0000019
[4-([3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]sulfonyl)piperazin-1-yl](4-methylphenyl)methanone
-
-
0.000012
[4-([3-chloro-4-[(3-chlorobenzyl)oxy]phenyl]sulfonyl)piperazin-1-yl](4-methylphenyl)methanone
-
-
0.0064
[4-[1-(3-chlorophenyl)-2-hydroxyethyl]-3-methylphenyl](4-methylpiperazin-1-yl)methanone
-
larger than 0.064
0.064
[4-[1-(3-chlorophenyl)-2-hydroxyethyl]-3-methylphenyl](4-methylpiperazin-1-yl)methanone
-
larger than 0.064
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0026 - 0.0031
(2R,3R,3aS,5aS,10aR)-N-(3,4-dichlorophenyl)-4,10-dioxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
0.00047 - 0.00051
(2R,3R,3aS,5aS,10R,10aS)-N-(3,4-dichlorophenyl)-10-hydroxy-4-oxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
0.00017 - 0.00026
(2R,3R,3aS,5aS,10S,10aS)-N-(3,4-dichlorophenyl)-10-hydroxy-4-oxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
0.00017 - 0.002
(2Z)-2-(cyclopropylimino)-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
0.00001 - 0.0006
(2Z)-2-[(3-chlorophenyl)imino]-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
0.00004
(3a'R,6a'S)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
0.00073 - 0.00099
(3a'R,6a'S)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
0.003 - 0.004
(3a'S,6a'R)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
0.0061 - 0.0087
(3a'S,6a'R)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
0.00056 - 0.00085
(3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
0.00007 - 0.00022
(3aR,6aS)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
0.000002 - 0.000005
(3aS,6aR)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
0.0083 - 0.0137
(3aS,6aR)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
0.032 - 0.045
(3aS,6aR)-5-[4-chloro-3-(trifluoromethyl)phenyl]-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
0.000004 - 0.00013
(3R,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
0.011 - 0.033
(3R,4S,5R)-4-[(3,4-dichlorophenyl)carbamoyl]-1',3'-dioxo-5-phenyl-1',3',4,5-tetrahydro-3H-spiro[furan-2,2'-indene]-3-carboxylic acid
0.00082 - 0.0032
(3S,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
0.0023 - 0.0049
1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)[2,2'-binaphthalene]-8,8'-dicarbaldehyde
0.00011
1-(3-bromophenyl)-2-[(2-methoxybenzyl)amino]ethanol
Staphylococcus aureus
-
IC50: 110 nM
0.000031
1-(3-chlorophenyl)-2-[(2-phenoxybenzyl)amino]ethanol
Staphylococcus aureus
-
IC50: 31 nM
0.000032
1-(3-iodophenyl)-2-[(2-phenoxybenzyl)amino]ethanol
Staphylococcus aureus
-
IC50: 32 nM
0.000083
1-(3-methoxyphenyl)-2-[(2-phenoxybenzyl)amino]ethanol
Staphylococcus aureus
-
IC50: 83 nM
0.000015 - 0.00005
1-(3-[[4-(3,5-dichlorophenyl)piperazin-1-yl]sulfonyl]phenyl)-3-(1,3-thiazol-2-yl)urea
0.00005
1-(4-bromothiophen-2-yl)-2-[(2-methoxybenzyl)amino]ethanol
Staphylococcus aureus
-
IC50: 50 nM
0.00012
1-(4-bromothiophen-2-yl)-2-[(2-phenoxybenzyl)amino]ethanol
Staphylococcus aureus
-
IC50: 120 nM
0.000026
1-(4-bromothiophen-2-yl)-2-[(2-[[4-(methylsulfonyl)benzyl]oxy]benzyl)amino]ethanol
Staphylococcus aureus
-
IC50: 26 nM
0.000008
1-(4-bromothiophen-2-yl)-2-[[2-(2-hydroxyethoxy)benzyl]amino]ethanol
Staphylococcus aureus
-
IC50: 8 nM
0.000018
1-(4-bromothiophen-2-yl)-2-[[2-(but-3-en-1-yloxy)benzyl]amino]ethanol
Staphylococcus aureus
-
IC50: 18 nM
0.000035
1-(4-bromothiophen-2-yl)-2-[[2-(methoxymethoxy)benzyl]amino]ethanol
Staphylococcus aureus
-
IC50: 35 nM
0.000043
1-(4-bromothiophen-2-yl)-2-[[2-(pyridin-2-ylmethoxy)benzyl]amino]ethanol
Staphylococcus aureus
-
IC50: 43 nM
0.000018
1-(4-bromothiophen-2-yl)-2-[[2-(pyridin-3-ylmethoxy)benzyl]amino]ethanol
Staphylococcus aureus
-
IC50: 18 nM
0.000016
1-(4-bromothiophen-2-yl)-2-[[2-(pyridin-4-ylmethoxy)benzyl]amino]ethanol
Staphylococcus aureus
-
IC50: 16 nM
0.00057
1-[3-(hydroxymethyl)phenyl]-2-[(2-phenoxybenzyl)amino]ethanol
Staphylococcus aureus
-
IC50: 570 nM
0.016 - 0.2
2-(3-methoxyphenyl)-5-(trifluoromethyl)-1H-imidazole
0.00011
2-[(2-methoxybenzyl)amino]-1-(3-methylphenyl)ethanol
Staphylococcus aureus
-
IC50: 110 nM
0.00019
2-[(2-methoxybenzyl)amino]-1-[3-(trifluoromethoxy)phenyl]ethanol
Staphylococcus aureus
-
IC50: 190 nM
0.00016
2-[(2-methoxybenzyl)amino]-1-[3-(trifluoromethyl)phenyl]ethanol
Staphylococcus aureus
-
IC50: 160 nM
0.00079
2-[(2-methylbenzyl)amino]-1-[3-(trifluoromethyl)phenyl]ethanol
Staphylococcus aureus
-
IC50: 790 nM
0.00019 - 0.026
2-[(4-chlorophenoxy)methyl]-N-(2-sulfamoylethyl)-1,3-thiazole-4-carboxamide
0.0001 - 0.013
2-[(4-chlorophenoxy)methyl]-N-(cyanomethyl)-1,3-thiazole-4-carboxamide
0.0025
2-[([2-hydroxy-2-[3-(trifluoromethyl)phenyl]ethyl]amino)methyl]benzoic acid
Staphylococcus aureus
-
IC50: 2500 nM
0.0001
2-[([2-hydroxy-2-[3-(trifluoromethyl)phenyl]ethyl]amino)methyl]phenol
Staphylococcus aureus
-
IC50: 100 nM
0.00011
2-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-(3-hydroxypropyl)acetamide
Staphylococcus aureus
-
IC50: 110 nM
0.000032
2-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-ethylacetamide
Staphylococcus aureus
-
IC50: 32 nM
0.000042
2-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]acetamide
Staphylococcus aureus
-
IC50: 42 nM
0.0001 - 0.034
2-[3-[(4-chloropyridin-2-yl)amino]phenoxy]-N-(1,1-dioxo-1l6-thiolan-3-yl)acetamide
0.0014 - 0.082
2-[3-[(4-chloropyridin-2-yl)amino]phenoxy]-N-methylacetamide
0.00056 - 0.041
2-[3-[(4-cyanopyridin-2-yl)amino]phenoxy]-N-methylacetamide
0.000022
2-[4-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]butyl]-1H-isoindole-1,3(2H)-dione
Staphylococcus aureus
-
IC50: 22 nM
0.000026
2-[[2-(1H-benzimidazol-2-ylmethoxy)benzyl]amino]-1-(4-bromothiophen-2-yl)ethanol
Staphylococcus aureus
-
IC50: 26 nM
0.00022
2-[[2-(2-aminoethoxy)benzyl]amino]-1-(4-bromothiophen-2-yl)ethanol
Staphylococcus aureus
-
IC50: 220 nM
0.000022
2-[[2-(4-aminobutoxy)benzyl]amino]-1-(4-bromothiophen-2-yl)ethanol
Staphylococcus aureus
-
IC50: 22 nM
0.00001
2-[[2-(benzyloxy)benzyl]amino]-1-(4-bromothiophen-2-yl)ethanol
Staphylococcus aureus
-
IC50: 10 nM
0.00005
2-[[2-(benzyloxy)benzyl]amino]-1-[3-(trifluoromethyl)phenyl]ethanol
Staphylococcus aureus
-
IC50: 50 nM
0.00026
2-[[2-(difluoromethoxy)benzyl]amino]-1-[3-(trifluoromethyl)phenyl]ethanol
Staphylococcus aureus
-
IC50: 260 nM
0.000058
2-[[2-(prop-2-en-1-yloxy)benzyl]amino]-1-[3-(trifluoromethyl)phenyl]ethanol
Staphylococcus aureus
-
IC50: 58 nM
0.000025
3-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-(3-hydroxypropyl)propanamide
Staphylococcus aureus
-
IC50: 25 nM
0.000036
3-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-[2-(methylamino)-2-oxoethyl]propanamide
Staphylococcus aureus
-
IC50: 36 nM
0.000058
3-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]propanoic acid
Staphylococcus aureus
-
IC50: 58 nM
0.000026
4-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-(3-hydroxypropyl)butanamide
Staphylococcus aureus
-
IC50: 26 nM
0.00003
4-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]-N-[2-(methylamino)-2-oxoethyl]butanamide
Staphylococcus aureus
-
IC50: 30 nM
0.000043
4-[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]butanoic acid
Staphylococcus aureus
-
IC50: 43 nM
0.00006 - 0.01
5-(3-methoxyphenyl)-3-(trifluoromethyl)-1H-pyrazole
0.0023 - 0.0049
BPP_03B04
0.001 - 0.059
ethyl [3-[3-(difluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetate
0.00008 - 0.011
ethyl [3-[3-(trifluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetate
0.0014 - 0.08
N-(1,1-dioxo-1l6-thiolan-3-yl)-2-[(4-methylphenoxy)methyl]-1,3-thiazole-4-carboxamide
0.000008 - 0.00005
N-[2-(1H-indol-3-yl)ethyl]-3-[(1,3-thiazol-2-ylcarbamoyl)amino]benzenesulfonamide
0.0000022 - 0.000013
N-[2-(1H-indol-3-yl)ethyl]-3-[[(1,3-thiazol-2-yl)carbamoyl]amino]benzene-1-sulfonamide
0.00007 - 0.0042
N-[2-[1-(methanesulfonyl)cyclopropyl]ethyl]-2-[3-[3-(trifluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetamide
0.0000027 - 0.000022
N-[3-[4-(pyridin-2-yl)piperazine-1-sulfonyl]phenyl]-N'-1,3-thiazol-2-ylurea
0.00012
N2-[[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]acetyl]-N-methylglycinamide
Staphylococcus aureus
-
IC50: 120 nM
0.000049
[2-([[2-(4-bromothiophen-2-yl)-2-hydroxyethyl]amino]methyl)phenoxy]acetonitrile
Staphylococcus aureus
-
IC50: 49 nM
0.0026
(2R,3R,3aS,5aS,10aR)-N-(3,4-dichlorophenyl)-4,10-dioxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
Enterococcus faecalis
-
IC50: 0.0026 mM
0.0031
(2R,3R,3aS,5aS,10aR)-N-(3,4-dichlorophenyl)-4,10-dioxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
Enterococcus faecalis
-
IC50: 0.0031 mM
0.00047
(2R,3R,3aS,5aS,10R,10aS)-N-(3,4-dichlorophenyl)-10-hydroxy-4-oxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
Enterococcus faecalis
-
IC50: 0.00047 mM
0.00051
(2R,3R,3aS,5aS,10R,10aS)-N-(3,4-dichlorophenyl)-10-hydroxy-4-oxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
Enterococcus faecalis
-
IC50: 0.00051 mM
0.00017
(2R,3R,3aS,5aS,10S,10aS)-N-(3,4-dichlorophenyl)-10-hydroxy-4-oxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
Enterococcus faecalis
-
IC50: 0.00017 mM
0.00026
(2R,3R,3aS,5aS,10S,10aS)-N-(3,4-dichlorophenyl)-10-hydroxy-4-oxo-2-phenyl-2,3,3a,4,5a,10-hexahydrofuro[2,3-c]indeno[1,2-b]furan-3-carboxamide
Enterococcus faecalis
-
IC50: 0.00026 mM
0.00017
(2Z)-2-(cyclopropylimino)-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
Escherichia coli
-
competitive with respect to Phe, selective for bacterial Phe-RS versus human Phe-RS, IC50: 0.00017 mM
0.0016
(2Z)-2-(cyclopropylimino)-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
Staphylococcus aureus
-
competitive with respect to Phe, selective for bacterial Phe-RS versus human Phe-RS, IC50: 0.0016 mM
0.002
(2Z)-2-(cyclopropylimino)-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
Enterococcus faecalis
-
competitive with respect to Phe, selective for bacterial Phe-RS versus human Phe-RS, IC50: 0.002 mM
0.00001
(2Z)-2-[(3-chlorophenyl)imino]-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
Escherichia coli
-
IC50: 10 nM
0.00007
(2Z)-2-[(3-chlorophenyl)imino]-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
Staphylococcus aureus
-
IC50: 70 nM
0.0006
(2Z)-2-[(3-chlorophenyl)imino]-3-(2-thienylmethyl)-1,3-thiazolidin-4-one
Enterococcus faecalis
-
IC50: 600 nM
0.00004
(3a'R,6a'S)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
Staphylococcus aureus
-
IC50: 40 nM, high selectivity over the human enzyme
0.00004
(3a'R,6a'S)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
Enterococcus faecalis
-
IC50: 40 nM, high selectivity over the human enzyme
0.00073
(3a'R,6a'S)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
Staphylococcus aureus
-
IC50: 0.00073 mM, high selectivity over the human enzyme
0.00099
(3a'R,6a'S)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
Enterococcus faecalis
-
IC50: 0.00099 mM, high selectivity over the human enzyme
0.003
(3a'S,6a'R)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
Staphylococcus aureus
-
IC50: 0.003 mM, high selectivity over the human enzyme
0.004
(3a'S,6a'R)-5'-(3,4-dichlorophenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
Enterococcus faecalis
-
IC50: 0.004 mM, high selectivity over the human enzyme
0.0061
(3a'S,6a'R)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
Staphylococcus aureus
-
IC50: 0.0061 mM, high selectivity over the human enzyme
0.0087
(3a'S,6a'R)-5'-(3-chloro-4-methylphenyl)-3'-phenyl-3a',6a'-dihydro-2'H-spiro[indene-2,1'-pyrrolo[3,4-c]pyrrole]-1,3,4',6'(3'H,5'H)-tetrone
Enterococcus faecalis
-
IC50: 0.0087 mM, high selectivity over the human enzyme
0.00056
(3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Staphylococcus aureus
-
IC50: 0.00056 mM, high selectivity over the human enzyme
0.00085
(3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Enterococcus faecalis
-
IC50: 0.00085 mM, high selectivity over the human enzyme
0.00007
(3aR,6aS)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Staphylococcus aureus
-
IC50: 0.00007 mM, high selectivity over the human enzyme
0.00022
(3aR,6aS)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Enterococcus faecalis
-
IC50: 0.00022 mM, high selectivity over the human enzyme
0.000002
(3aS,6aR)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Staphylococcus aureus
-
IC50: 2 nM, high selectivity over the human enzyme
0.000005
(3aS,6aR)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Enterococcus faecalis
-
IC50: 5 nM, high selectivity over the human enzyme
0.0083
(3aS,6aR)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Enterococcus faecalis
-
IC50: 0.0083 mM, high selectivity over the human enzyme
0.0137
(3aS,6aR)-5-(3-chloro-4-methylphenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Staphylococcus aureus
-
IC50: 0.0137 mM, high selectivity over the human enzyme
0.032
(3aS,6aR)-5-[4-chloro-3-(trifluoromethyl)phenyl]-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Enterococcus faecalis
-
IC50: 0.032 mM, high selectivity over the human enzyme
0.045
(3aS,6aR)-5-[4-chloro-3-(trifluoromethyl)phenyl]-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Staphylococcus aureus
-
IC50: 0.045 mM, high selectivity over the human enzyme
0.000004
(3R,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Staphylococcus aureus
-
IC50: 4 nM
0.000005
(3R,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Enterococcus faecalis
-
IC50: 5 nM
0.00013
(3R,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Escherichia coli
-
IC50: 130 nM
0.011
(3R,4S,5R)-4-[(3,4-dichlorophenyl)carbamoyl]-1',3'-dioxo-5-phenyl-1',3',4,5-tetrahydro-3H-spiro[furan-2,2'-indene]-3-carboxylic acid
Enterococcus faecalis
-
IC50: 0.011 mM
0.033
(3R,4S,5R)-4-[(3,4-dichlorophenyl)carbamoyl]-1',3'-dioxo-5-phenyl-1',3',4,5-tetrahydro-3H-spiro[furan-2,2'-indene]-3-carboxylic acid
Enterococcus faecalis
-
IC50: 0.033 mM
0.00082
(3S,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Enterococcus faecalis
-
IC50: 820 nM
0.0032
(3S,3aR,6aS)-5-(3,4-dichlorophenyl)-3-phenyl-3a,6a-dihydrospiro[furo[3,4-c]pyrrole-1,2'-indene]-1',3',4,6(3H,5H)-tetrone
Escherichia coli
-
IC50: 3200 nM
0.0023
1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)[2,2'-binaphthalene]-8,8'-dicarbaldehyde
Pseudomonas aeruginosa
-
at pH 7.5 and 37°
0.0049
1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)[2,2'-binaphthalene]-8,8'-dicarbaldehyde
Streptococcus pneumoniae
-
at pH 7.5 and 37°
0.000015
1-(3-[[4-(3,5-dichlorophenyl)piperazin-1-yl]sulfonyl]phenyl)-3-(1,3-thiazol-2-yl)urea
Haemophilus influenzae
-
IC50: 15 nM
0.000015
1-(3-[[4-(3,5-dichlorophenyl)piperazin-1-yl]sulfonyl]phenyl)-3-(1,3-thiazol-2-yl)urea
Escherichia coli
-
IC50: 15 nM
0.00005
1-(3-[[4-(3,5-dichlorophenyl)piperazin-1-yl]sulfonyl]phenyl)-3-(1,3-thiazol-2-yl)urea
Streptococcus pneumoniae
-
IC50: 50 nM
0.016
2-(3-methoxyphenyl)-5-(trifluoromethyl)-1H-imidazole
Escherichia coli
-
pH and temperature not specified in the publication
0.2
2-(3-methoxyphenyl)-5-(trifluoromethyl)-1H-imidazole
Pseudomonas aeruginosa
-
IC50 above 0.2 mM, pH and temperature not specified in the publication
0.00019
2-[(4-chlorophenoxy)methyl]-N-(2-sulfamoylethyl)-1,3-thiazole-4-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.026
2-[(4-chlorophenoxy)methyl]-N-(2-sulfamoylethyl)-1,3-thiazole-4-carboxamide
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0001
2-[(4-chlorophenoxy)methyl]-N-(cyanomethyl)-1,3-thiazole-4-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.013
2-[(4-chlorophenoxy)methyl]-N-(cyanomethyl)-1,3-thiazole-4-carboxamide
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0001
2-[3-[(4-chloropyridin-2-yl)amino]phenoxy]-N-(1,1-dioxo-1l6-thiolan-3-yl)acetamide
Escherichia coli
-
pH and temperature not specified in the publication
0.034
2-[3-[(4-chloropyridin-2-yl)amino]phenoxy]-N-(1,1-dioxo-1l6-thiolan-3-yl)acetamide
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0014
2-[3-[(4-chloropyridin-2-yl)amino]phenoxy]-N-methylacetamide
Escherichia coli
-
pH and temperature not specified in the publication
0.082
2-[3-[(4-chloropyridin-2-yl)amino]phenoxy]-N-methylacetamide
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.00056
2-[3-[(4-cyanopyridin-2-yl)amino]phenoxy]-N-methylacetamide
Escherichia coli
-
pH and temperature not specified in the publication
0.041
2-[3-[(4-cyanopyridin-2-yl)amino]phenoxy]-N-methylacetamide
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.00006
5-(3-methoxyphenyl)-3-(trifluoromethyl)-1H-pyrazole
Escherichia coli
-
pH and temperature not specified in the publication
0.01
5-(3-methoxyphenyl)-3-(trifluoromethyl)-1H-pyrazole
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0023
BPP_03B04
Pseudomonas aeruginosa
-
at pH 7.5 and 37°C
0.0049
BPP_03B04
Streptococcus pneumoniae
-
at pH 7.5 and 37°C
0.001
ethyl [3-[3-(difluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetate
Escherichia coli
-
pH and temperature not specified in the publication
0.059
ethyl [3-[3-(difluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetate
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.00008
ethyl [3-[3-(trifluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetate
Escherichia coli
-
pH and temperature not specified in the publication
0.011
ethyl [3-[3-(trifluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetate
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0014
N-(1,1-dioxo-1l6-thiolan-3-yl)-2-[(4-methylphenoxy)methyl]-1,3-thiazole-4-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.08
N-(1,1-dioxo-1l6-thiolan-3-yl)-2-[(4-methylphenoxy)methyl]-1,3-thiazole-4-carboxamide
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.000008
N-[2-(1H-indol-3-yl)ethyl]-3-[(1,3-thiazol-2-ylcarbamoyl)amino]benzenesulfonamide
Haemophilus influenzae
-
IC50: 8 nM
0.000008
N-[2-(1H-indol-3-yl)ethyl]-3-[(1,3-thiazol-2-ylcarbamoyl)amino]benzenesulfonamide
Escherichia coli
-
IC50: 8 nM
0.00005
N-[2-(1H-indol-3-yl)ethyl]-3-[(1,3-thiazol-2-ylcarbamoyl)amino]benzenesulfonamide
Staphylococcus aureus
-
IC50: 50 nM
0.0000022
N-[2-(1H-indol-3-yl)ethyl]-3-[[(1,3-thiazol-2-yl)carbamoyl]amino]benzene-1-sulfonamide
Escherichia coli
-
pH and temperature not specified in the publication
0.000013
N-[2-(1H-indol-3-yl)ethyl]-3-[[(1,3-thiazol-2-yl)carbamoyl]amino]benzene-1-sulfonamide
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.00007
N-[2-[1-(methanesulfonyl)cyclopropyl]ethyl]-2-[3-[3-(trifluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetamide
Escherichia coli
-
pH and temperature not specified in the publication
0.0042
N-[2-[1-(methanesulfonyl)cyclopropyl]ethyl]-2-[3-[3-(trifluoromethyl)-1H-pyrazol-5-yl]phenoxy]acetamide
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0000027
N-[3-[4-(pyridin-2-yl)piperazine-1-sulfonyl]phenyl]-N'-1,3-thiazol-2-ylurea
Escherichia coli
-
pH and temperature not specified in the publication
0.000022
N-[3-[4-(pyridin-2-yl)piperazine-1-sulfonyl]phenyl]-N'-1,3-thiazol-2-ylurea
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
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?
-
x * 59000 (alpha) + x * 72000 (beta)
?
-
x * 74000 (alpha) + x * 63000 (beta), SDS-PAGE
?
-
x * 60000, alpha-subunit, + x * 70000, beta-subunit, SDS-PAGE
?
x * 57600, alpha-subunit, + x * 66200, beta-subunit, amino acid sequence determination
dimer
-
dimer
1 * 55000, alpha-subunit, + 1 * 57000, beta-subunit, alphabeta, amino acid determination
dimer
1 * 55000, alpha-subunit, + 1 * 57000, beta-subunit, alphabeta2, amino acid determination
dimer
-
1 * 33000 (alpha) + 1 * 42000 (beta), SDS-PAGE
heterodimer
-
1 * 54000, alpha-subunit, + 1 * 62000, beta-subunit, SDS-PAGE
heterodimer
-
1 * 80000 + 1 * 41000, SDS-PAGE
heterodimer
-
1 * 85000 + 1 * 42000, SDS-PAGE
heterotetramer
-
EcPheRS, alpha and beta-subunits, the alpha-subunits contain the actice site, the beta-subunits harbor the editing site
heterotetramer
EcPheRS is a (alphabeta)2 heterotetramer, built of two alphabeta heterodimers
heterotetramer
build of two alphabeta heterodimers
heterotetramer
two alpha and two beta subunits
heterotetramer
-
ctPheRS, alpha and beta-subunits, the alpha-subunits contain the actice site, the beta-subunits harbor the editing site
monomer
-
-
monomer
1 * 48000, recombinant mitochondrial isozyme, analytical sedimentation centrifugation
monomer
-
1 * 48000, recombinant enzyme, SDS-PAGE
monomer
-
1 * 49600, sequence calculation
monomer
-
mtPheRS, alpha-subunit monomer, catalytic domain
oligomer
-
PheRs is a multidomain (alphabeta)2 heterotetrameric protein, the alpha subunit forms the catalytic core of the enzyme, while the beta subunit contains a number of autonomous structural modules with a wide range of functions including tRNA anticodon binding and editing of the misaminoacylated species Tyr-tRNAPhe
oligomer
-
PheRs is a multidomain (alphabeta)2 heterotetrameric protein, the alpha subunit forms the catalytic core of the enzyme, while the beta subunit contains a number of autonomous structural modules with a wide range of functions including tRNA anticodon binding and editing of the misaminoacylated species Tyr-tRNAPhe
-
tetramer
2 * alpha + 2 * beta
tetramer
-
2 * alpha + 2 * beta
-
tetramer
-
2 * 39000 (alpha) + 2 * 94000 (beta), SDS-PAGE
tetramer
-
2 * 98000 (alpha) + 2 * 38000 (beta), SDS-PAGE
tetramer
-
2 * 39000 (alpha) + 2 * 94000 (beta), SDS-PAGE
-
tetramer
-
2 * 57000 (alpha) + 2 * 66000 (beta), SDS-PAGE
tetramer
-
2 * 57000, alpha-subunit, + 2 * 66000, beta-subunit, (alphabeta)2, SDS-PAGE
tetramer
Methanobacterium thermoautotrophicus
-
2 * 60000, alpha, + 2 * 70000, beta, alphabeta2, SDS-PAGE
tetramer
-
2 * 63000 (alpha) + 2 * 70000 (beta), SDS-PAGE
tetramer
-
2 * 59000 (alpha) + 2 * 70000 (beta), PAGE under denaturing conditions
tetramer
-
PheRS belongs to class IIc and is a tetrameric enzyme consisting of two alphabeta heterodimers. The B3/4 domain of the beta-subunit catalyzes the editing, domain architecture, overview
tetramer
-
2 * 56000, alpha-subunit, + 2 * 64000, beta-subunit, (alphabeta)2, SDS-PAGE
tetramer
-
2 * 57000 (alpha) + 2 * 72000 (beta), urea-SDS PAGE
tetramer
-
2 * 40000, alpha subunit, + 2 * 90000, beta-subunit, (alphabeta)2, recombinant enzyme, SDS-PAGE
tetramer
-
2 * 40000 (alpha) + 2 * 92000 (beta), SDS-PAGE
tetramer
-
(alphabeta)2 heterotetramer
additional information
-
the separated subunits do not possess any detectable tRNA-amino-acylation activity
additional information
-
the separated subunits do not possess any detectable tRNA-amino-acylation activity
additional information
-
all forms of homologous subunits have no catalytic activity
additional information
-
beta-subunits exist in solution mainly in the monomeric form with negligible formation of beta2-dimers. The alpha-subunits predominantly form alpha2-dimers
additional information
-
beta-subunits exist in solution mainly in the monomeric form with negligible formation of beta2-dimers. The alpha-subunits predominantly form alpha2-dimers
additional information
-
the tRNA-binding sites are formed on heavy beta-subunits of the enzyme. The catalytic center of tRNA aminoacylation is formed in the contact region of subunits
additional information
EcPheRS consists of 11 structural domains. Three of them: the N-terminus, A1 and A2 belong to the alpha-subunit and B1-B8 domains to the beta subunit. The N-terminal domain of the alpha-subunit in EcPheRS forms compact triple helix domain, structure comparisons, overview
additional information
-
EcPheRS consists of 11 structural domains. Three of them: the N-terminus, A1 and A2 belong to the alpha-subunit and B1-B8 domains to the beta subunit. The N-terminal domain of the alpha-subunit in EcPheRS forms compact triple helix domain, structure comparisons, overview
additional information
-
the separated subunits do not possess any detectable tRNA-amino-acylation activity
-
additional information
-
beta-subunits exist in solution mainly in the monomeric form with negligible formation of beta2-dimers. The alpha-subunits predominantly form alpha2-dimers
-
additional information
-
the tRNA-binding sites are formed on heavy beta-subunits of the enzyme. The catalytic center of tRNA aminoacylation is formed in the contact region of subunits
-
additional information
-
enzyme is part of an aminoacyl-tRNA synthetase complex which is resistant to dissociation when subjected to gel filtration
additional information
the catalytic function resides in the alpha-subunit, while the beta-subunit provides several binding-like domains for OB, RNP, SH3, and DNA
additional information
the catalytic function resides in the alpha-subunit, while the beta-subunit provides several binding-like domains for OB, RNP, SH3, and DNA
additional information
-
the catalytic function resides in the alpha-subunit, while the beta-subunit provides several binding-like domains for OB, RNP, SH3, and DNA
additional information
the mitochondrial isozyme is a single polypeptide chain, which bears similarities in structure to the alpha/beta subunit organization of bacterial enzymes
additional information
-
the mitochondrial isozyme is a single polypeptide chain, which bears similarities in structure to the alpha/beta subunit organization of bacterial enzymes
additional information
-
human mitPheRS is a chimera of the bacterial beta-subunit of PheRS and the B8 domain of its beta-subunit, together, the beta-subunit and the RNP-domain, i.e. B8 domain, at the C-terminus form the minimal structural set to construct an enzyme with phenylalanylation activity, overview
additional information
-
human mitPheRS consists of four major parts: the N-terminal region, residues 1-47, the catalytic domain, residues 48-289, the linker region, residues 290-322, and the C-terminal domain, residues 323-415. Multimeric organization is not a prerequisite for phenylalanylation activity, as monomeric mitochondrial phenylalanyl-tRNA synthetase is also active. The anticodon binding domain of the beta subunit of alphabeta2 PheRS is located at the C-terminus of mitPheRS overlapping with the acceptor stem of phenylalanine transfer RNA, structure, overview
additional information
-
structure molecular dynamics simulations of hmtPheRS, wild-type and mutant enzymes, overview
additional information
the N-terminal fragment of the PheRS beta-subunit includes the editing domain B3/4, which has archaea/eukarya-specific insertions/deletions and adopts a different orientation relative to other domains, as compared with that of bacterial PheRS, structure, overview
additional information
-
the N-terminal fragment of the PheRS beta-subunit includes the editing domain B3/4, which has archaea/eukarya-specific insertions/deletions and adopts a different orientation relative to other domains, as compared with that of bacterial PheRS, structure, overview
additional information
-
the amino terminal part of each beta-subunit represents the main tRNA binding domain and is not involved in either catalysis or subunit interactions. The trypsin resistant alpha2beta2 core contains the catalytic site as well as contact areas between subunits
additional information
-
structure analysis and structure-activity relationship, overview
additional information
-
the separated subunits do not possess any detectable tRNA-amino-acylation activity
additional information
-
the separated subunits do not possess any detectable tRNA-amino-acylation activity
additional information
-
all forms of homologous subunits have no catalytic activity
additional information
-
both alpha- and beta-subunits mainly exist in the dimeric form
additional information
-
alphabeta organization, the alpha-subunit is the catalytically active one
additional information
the enzyme is modularly composed of several different domains
additional information
-
the enzyme is modularly composed of several different domains
additional information
-
the separated subunits do not possess any detectable tRNA-amino-acylation activity
-
additional information
-
both alpha- and beta-subunits mainly exist in the dimeric form
-
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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
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
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
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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
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
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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
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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
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
A450G
-
mutation in subunit alpha, tRNAPhe substrate specificity and flexibilty in charging pPhe variants compared to the wild-type enzyme
A450G
-
the mutant shows normal cocoon production
A294G
-
mutation of the catalytical alpha-subunit, constructed mutant shows relaxed substrate specificity, efficient incorporation of p-iodo, p-ethynyl-, p-cyano-, and p-azidophenylalanines, but not p-acetylphenylalanine, into protein in the Escherichia coli host
A294G
-
mutant enzyme with A294G mutation in alpha-subunit, kcat/Km is 58% of wild-type value
A294G
-
thermosensitive active site mutant strain NP37 enzyme
A294G
-
thermosensitive active site mutant, the suppressor tRNAPhe CUA is misacylated with 4-iodo-L-phenylalanine by the mutant at a high magnesium-ion concentration of 70 mM
A294G
-
thermosensitive active site mutant strain NP37 enzyme
-
A294G
-
thermosensitive active site mutant, the suppressor tRNAPhe CUA is misacylated with 4-iodo-L-phenylalanine by the mutant at a high magnesium-ion concentration of 70 mM
-
additional information
-
engineering of a mutated counter-selectable marker based on the Burkholderia pseudomallei PheS, i.e. the alpha-subunit of PheRS protein, effectiveness in three different transformed Burkholderia species, the mutant PheS protein effectively killed 100% of the bacteria in the presence of 0.1% 4-chlorophenylalanine, overview. Assembling of mutant pheS on several allelic replacement vectors, in addition to construction of selectable markers based on tellurite and trimethoprim resistance that are excisable by flanking unique FLP recombination target sequences, overview
additional information
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construction of a truncated mutant PheRSDELTAB2A294G, lacking the B2 domain, which shows kinetics for in vitro aminoacylation comparable to the wild-type enzyme, a 2-fold drop compared to full-length PheRS in the catalytic efficiency of Tyr-tRNAPhe hydrolysis
additional information
-
editing-defective PheRS variants display significantly increased tyrosylation levels in the presence of EF-Tu, likely through elongation factor Tu, EF-Tu, protection of synthesized Tyr-tRNAPhe from hydrolysis, overview
additional information
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the editing domain of PheRS is transplanted at internal sites into Escherichia coli iodoTyrRS to edit tyrosyl-tRNATyr and thereby improve the overall specificity for 3-iodo-L-tyrosine, overview
additional information
-
construction of a truncated mutant PheRSDELTAB2A294G, lacking the B2 domain, which shows kinetics for in vitro aminoacylation comparable to the wild-type enzyme, a 2-fold drop compared to full-length PheRS in the catalytic efficiency of Tyr-tRNAPhe hydrolysis
-
additional information
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the N-terminal His-tag does not influence the kinetic parameters of tRNAPhe aminoacylation, cleavage of the His-tag by thrombin leads to nonspecific splitting of the enzyme that occurs in parallel to the main reaction
additional information
-
the editing domain of PheRS is transplanted at internal sites into Escherichia coli iodoTyrRS to edit tyrosyl-tRNATyr and thereby improve the overall specificity for 3-iodo-L-tyrosine, overview
additional information
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construction of enzyme mutants with better crystallization abilities, e.g. a PheRS variant which has both domains I and IV removed, or PheRS surface mutants, overview
additional information
-
the editing domain of PheRS is transplanted at internal sites into Escherichia coli iodoTyrRS to edit tyrosyl-tRNATyr and thereby improve the overall specificity for 3-iodo-L-tyrosine, overview
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