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cytosolic phenylalanyl-tRNA synthetase
-
L-Phenylalanyl-tRNA synthetase
-
Phenylalanine translase
-
Phenylalanine--tRNA ligase
-
Phenylalanine-tRNA synthetase
-
Phenylalanyl transfer ribonucleic acid synthetase
-
Phenylalanyl-transfer ribonucleate synthetase
-
Phenylalanyl-transfer RNA ligase
-
Phenylalanyl-transfer RNA synthetase
-
Phenylalanyl-tRNA ligase
-
Phenylalanyl-tRNA synthetase
-
Synthetase, phenylalanyl-transfer ribonucleate
-
cytoplasmic phenylalanyl-tRNA synthetase
cytosolic phenylalanyl-tRNA synthetase
L-Phenylalanyl-tRNA synthetase
mitochondrial phenylalanyl-tRNA synthetase
Phenylalanine--tRNA ligase
Phenylalanine-tRNA synthetase
Phenylalanyl transfer ribonucleic acid synthetase
Phenylalanyl-transfer ribonucleate synthetase
Phenylalanyl-transfer RNA ligase
Phenylalanyl-transfer RNA synthetase
Phenylalanyl-tRNA synthetase
Synthetase, phenylalanyl-transfer ribonucleate
CML33
-
-
-
-
cytoplasmic phenylalanyl-tRNA synthetase
-
-
cytoplasmic phenylalanyl-tRNA synthetase
-
cytosolic phenylalanyl-tRNA synthetase
-
cytosolic phenylalanyl-tRNA synthetase
-
FARS2
-
-
FRS
-
-
-
-
hcPheRS
-
HSPC173
-
-
-
-
L-Phenylalanyl-tRNA synthetase
-
-
-
-
L-Phenylalanyl-tRNA synthetase
-
-
L-Phenylalanyl-tRNA synthetase
-
mitochondrial phenylalanyl-tRNA synthetase
-
-
mitochondrial phenylalanyl-tRNA synthetase
-
mtPheRS
-
-
mtPheRS
-
mitochondrial type
Phenylalanine translase
-
-
-
-
Phenylalanine translase
-
-
Phenylalanine translase
-
Phenylalanine--tRNA ligase
-
-
-
-
Phenylalanine--tRNA ligase
-
-
Phenylalanine--tRNA ligase
-
Phenylalanine-tRNA synthetase
-
-
-
-
Phenylalanine-tRNA synthetase
-
-
Phenylalanine-tRNA synthetase
-
Phenylalanyl transfer ribonucleic acid synthetase
-
-
-
-
Phenylalanyl transfer ribonucleic acid synthetase
-
-
Phenylalanyl transfer ribonucleic acid synthetase
-
Phenylalanyl-transfer ribonucleate synthetase
-
-
-
-
Phenylalanyl-transfer ribonucleate synthetase
-
-
Phenylalanyl-transfer ribonucleate synthetase
-
Phenylalanyl-transfer RNA ligase
-
-
-
-
Phenylalanyl-transfer RNA ligase
-
-
Phenylalanyl-transfer RNA ligase
-
Phenylalanyl-transfer RNA synthetase
-
-
-
-
Phenylalanyl-transfer RNA synthetase
-
-
Phenylalanyl-transfer RNA synthetase
-
Phenylalanyl-tRNA ligase
-
-
-
-
Phenylalanyl-tRNA ligase
-
-
Phenylalanyl-tRNA ligase
-
Phenylalanyl-tRNA synthetase
-
-
-
-
Phenylalanyl-tRNA synthetase
-
-
Phenylalanyl-tRNA synthetase
-
PheRS
-
-
-
-
Synthetase, phenylalanyl-transfer ribonucleate
-
-
-
-
Synthetase, phenylalanyl-transfer ribonucleate
-
-
Synthetase, phenylalanyl-transfer ribonucleate
-
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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
?
ATP + 3,4-dihydroxy-L-phenylalanine + tRNAPhe
AMP + diphosphate + 3,4-dihydroxy-L-phenylalanyl-tRNAPhe
ATP + DL-m-tyrosine + tRNAPhe
AMP + diphosphate + DL-m-tyrosyl-tRNAPhe
ATP + L-phenylalanine + (s-pA)tRNAPhe
AMP + diphosphate + L-phenylalanyl-(s-pA)tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + (s-pC)tRNAPhe
AMP + diphosphate + L-phenylalanyl-(s-pC)tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + (s-pG)tRNAPhe
AMP + diphosphate + L-phenylalanyl-(s-pG)tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + (s-pU)tRNAPhe
AMP + diphosphate + L-phenylalanyl-(s-pU)tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
ATP + L-tyrosine + tRNAPhe
AMP + diphosphate + L-tyrosyl-tRNAPhe
additional information
?
-
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 + 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-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-tyrosine + tRNAPhe
AMP + diphosphate + L-tyrosyl-tRNAPhe
-
-
-
-
?
ATP + L-tyrosine + tRNAPhe
AMP + diphosphate + L-tyrosyl-tRNAPhe
0.089% activity compared to L-phenylalanine
-
-
?
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 enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
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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ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
additional information
?
-
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
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 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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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
-
-
-
0.6 - 0.65
3,4-dihydroxy-L-phenylalanine
0.012 - 0.13
DL-m-tyrosine
0.00057 - 0.033
L-phenylalanine
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
additional information
additional information
-
Km-values for mutant yeast tRNAPhe transcripts
-
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
-
-
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
0.00057
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
0.0015
L-phenylalanine
-
25°C
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
0.0032
L-phenylalanine
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.0056
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
0.033
L-phenylalanine
ATP-diphosphate exchange reaction, recombinant mitochondrial isozyme, pH 7.3, 37°C
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
0.00036
tRNAPhe
mutant enzyme T210M, at pH 8.5 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
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
0.018
tRNAPhe
aminoacylation reaction, recombinant mitochondrial isozyme, pH 7.5, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.057 - 0.23
3,4-dihydroxy-L-phenylalanine
2.9
ATP
ATP-diphosphate exchange reaction, mitochondrial isozyme, pH 7.3, 37°C
0.052 - 0.65
DL-m-tyrosine
0.005 - 1.1
L-phenylalanine
0.033
L-tyrosine
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
additional information
additional information
-
turnover numbers for mutant yeast tRNAPhe transcripts
-
0.057
3,4-dihydroxy-L-phenylalanine
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.23
3,4-dihydroxy-L-phenylalanine
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.052
DL-m-tyrosine
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.65
DL-m-tyrosine
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.005
L-phenylalanine
mitochondrial chimeric enzyme with implanted editing module from Escherichia coli phenylalanine-tRNA synthetase, at pH 8.5 and 37°C
0.012
L-phenylalanine
mutant enzyme H99D, at pH 8.5 and 37°C
0.02
L-phenylalanine
mutant enzyme R117G, at pH 8.5 and 37°C
0.06
L-phenylalanine
wild type mitochondrial enzyme, at pH 8.5 and 37°C
0.075
L-phenylalanine
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.19
L-phenylalanine
wild type enzyme, at pH 8.5 and 37°C
0.87
L-phenylalanine
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
1.1
L-phenylalanine
ATP-diphosphate exchange reaction, recombinant mitochondrial isozyme, pH 7.3, 37°C
0.07
tRNAPhe
mutant enzyme R383C, at pH 8.5 and 37°C
0.08
tRNAPhe
mutant enzyme D289Y, at pH 8.5 and 37°C
0.11
tRNAPhe
aminoacylation reaction, recombinant mitochondrial isozyme, pH 7.5, 37°C
0.14
tRNAPhe
mutant enzyme P49A, at pH 8.5 and 37°C
0.14
tRNAPhe
mutant enzyme R387Q, at pH 8.5 and 37°C
0.19
tRNAPhe
wild type enzyme, at pH 8.5 and 37°C
0.22
tRNAPhe
mutant enzyme T210M, at pH 8.5 and 37°C
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0.095 - 0.37
3,4-dihydroxy-L-phenylalanine
1.7 - 270
L-phenylalanine
0.017
L-tyrosine
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.095
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
0.37
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
4.3
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
5
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
1.7
L-phenylalanine
mutant enzyme R117G, at pH 8.5 and 37°C
2.2
L-phenylalanine
mutant enzyme H99D, at pH 8.5 and 37°C
8.8
L-phenylalanine
mitochondrial chimeric enzyme with implanted editing module from Escherichia coli phenylalanine-tRNA synthetase, at pH 8.5 and 37°C
28.3
L-phenylalanine
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
71.4
L-phenylalanine
wild type mitochondrial enzyme, at pH 8.5 and 37°C
80
L-phenylalanine
wild type enzyme, at pH 8.5 and 37°C
270
L-phenylalanine
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
7.2
tRNAPhe
mutant enzyme R383C, at pH 8.5 and 37°C
8.7
tRNAPhe
mutant enzyme D289Y, at pH 8.5 and 37°C
14.3
tRNAPhe
mutant enzyme R387Q, at pH 8.5 and 37°C
23.3
tRNAPhe
mutant enzyme T210M, at pH 8.5 and 37°C
125
tRNAPhe
mutant enzyme P49A, at pH 8.5 and 37°C
160
tRNAPhe
wild type enzyme, at pH 8.5 and 37°C
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38200
alpha-subunit, mutant DELTA1-175, determined by SDS-PAGE
45000
alpha-subunit, mutant DELTA60-170, determined by SDS-PAGE
57500
alpha-subunit, wild-type, determined by SDS-PAGE
297000
-
recombinant enzyme, dynamic light scattering at 20°
57000
-
2 * 57000, alpha-subunit, + 2 * 66000, beta-subunit, (alphabeta)2, SDS-PAGE
60000
-
x * 60000, alpha-subunit, + x * 70000, beta-subunit, SDS-PAGE
63000
-
x * 74000 (alpha) + x * 63000 (beta), SDS-PAGE
66000
-
2 * 57000, alpha-subunit, + 2 * 66000, beta-subunit, (alphabeta)2, SDS-PAGE
67000
beta-subunit, wild-type, determined by SDS-PAGE
70000
-
x * 60000, alpha-subunit, + x * 70000, beta-subunit, SDS-PAGE
71000
-
binary mitPheRS-tRNAPhe complex, gel filtration
74000
-
x * 74000 (alpha) + x * 63000 (beta), SDS-PAGE
96000
dimer, mutant, crosslinked subunits
55000
1 * 55000, alpha-subunit, + 1 * 57000, beta-subunit, alphabeta, amino acid determination
55000
1 * 55000, alpha-subunit, + 1 * 57000, beta-subunit, alphabeta2, amino acid determination
57000
1 * 55000, alpha-subunit, + 1 * 57000, beta-subunit, alphabeta, amino acid determination
57000
1 * 55000, alpha-subunit, + 1 * 57000, beta-subunit, alphabeta2, amino acid determination
45000
recombinant mitochondrial isozyme, gel filtration
45000
-
mitPheRS, gel filtration
48000
-
recombinant enzyme, gel filtration
48000
recombinant mitochondrial isozyme, analytical velocity sedimentation centrifugation
48000
monomer, determined by SDS-PAGE
49600
recombinant mitochondrial isozyme, amino acid sequence determination
49600
-
1 * 49600, sequence calculation
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heterotetramer
build of two alphabeta heterodimers
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
?
-
x * 74000 (alpha) + x * 63000 (beta), SDS-PAGE
?
-
x * 60000, alpha-subunit, + x * 70000, beta-subunit, SDS-PAGE
heterotetramer
build of two alphabeta heterodimers
heterotetramer
two alpha and two beta subunits
monomer
-
-
monomer
1 * 48000, recombinant mitochondrial isozyme, analytical sedimentation centrifugation
monomer
-
1 * 48000, recombinant enzyme, SDS-PAGE
monomer
-
1 * 49600, sequence calculation
tetramer
-
-
tetramer
-
2 * 57000, alpha-subunit, + 2 * 66000, beta-subunit, (alphabeta)2, SDS-PAGE
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
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alphaDELTA1-175
truncated N-terminal domain of the alpha subunit of hcPheRS
alphaDELTA60-170
truncated N-terminal domain of the alpha subunit of hcPheRS
D289Y
the mutant shows 52% of wild type activity
D325Y
-
the mutation is associated with early-onset epilepsy and isolated complex IV deficiency in muscle. The mutant is unable to bind ATP and shows consequently undetectable aminoacylation activity
H99D
the mutant shows 2.7% of wild type activity
K33C/T351C
mutant, crosslinked catalytic and RNA-binding domains, results in a closed form of mtPheRS that still catalyses ATP-dependent Phe activation, but is no longer able to transfer Phe to tRNA and complete the aminoacylation reaction
N280S
-
the mutant displays wild-type aminoacylation activity and stability with respect to their free energies of unfolding, but are less stable at low pH. It shows no significant loss in secondary structure. The mutant retains less activity than wild-type enzyme after refolding for mitochondrial import
P49A
the mutant shows 78% of wild type activity
R117G
the mutant shows 2.1% of wild type activity
R383C
the mutant shows 43% of wild type activity
R387Q
the mutant shows 86% of wild type activity
S57C
-
the mutant displays wild-type aminoacylation activity and stability with respect to their free energies of unfolding, but are less stable at low pH. It shows no significant loss in secondary structure. The mutant retains less activity than wild-type enzyme after refolding for mitochondrial import
S57C/N280S
-
Ser57 and Asn280 map to positions away from the catalytic center and the anticodon binding domain of hmtPheRS, the mutant does not show significant loss in secondary structure or aminoacylation activity in vitro compared to wild-type enzyme. The S57C/N280S double mutant had remarkable stability even at low pH
T210M
the mutant shows 140% of wild type activity
additional information
-
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
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Zakharova, O.D.; Kotenko, I.; Lavrik, O.I.
Phenylalanyl-tRNA-synthetase from human placenta: isolation and characteristics
Biokhimiia
55
1025-1031
1990
Homo sapiens
brenda
Nazarenko, I.A.; Peterson, E.T.; Zakharova, O.D.; Lavrik, O.I.; Uhlenbeck, O.C.
Recognition nucleotides for human phenylalanyl-tRNA synthetase
Nucleic Acids Res.
20
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1992
Homo sapiens
brenda
Rodova, M.; Ankilova, V.; Safro, M.G.
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
Biochem. Biophys. Res. Commun.
255
765-773
1999
Homo sapiens (Q9NSD9), Homo sapiens (Q9Y285), Homo sapiens
brenda
Moor, N.; Lavrik, O.; Favre, A.; Safro, M.
Prokaryotic and eukaryotic tetrameric phenylalanyl-tRNA synthetases display conservation of the binding mode of the tRNAPhe CCA end
Biochemistry
42
10697-10708
2003
Homo sapiens
brenda
Bullard, J.M.; Cai, Y.C.; Demeler, B.; Spremulli, L.L.
Expression and characterization of a human mitochondrial phenylalanyl-tRNA synthetase
J. Mol. Biol.
288
567-577
1999
Homo sapiens (O95363), Homo sapiens
brenda
Moor, N.; Linshiz, G.; Safro, M.
Cloning and expression of human phenylalanyl-tRNA synthetase in Escherichia coli: comparative study of purified recombinant enzymes
Protein Expr. Purif.
24
260-267
2002
Homo sapiens
brenda
Levin, I.; Kessler, N.; Moor, N.; Klipcan, L.; Koc, E.; Templeton, P.; Spremulli, L.; Safro, M.
Purification, crystallization and preliminary X-ray characterization of a human mitochondrial phenylalanyl-tRNA synthetase
Acta Crystallogr. Sect. F
63
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Homo sapiens
brenda
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Autoantibodies and their significance in myositis
Curr. Rheumatol. Rep.
10
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2008
Homo sapiens
brenda
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The tRNA-induced conformational activation of human mitochondrial phenylalanyl-tRNA synthetase
Structure
16
1095-1104
2008
Homo sapiens
brenda
Finarov, I.; Moor, N.; Kessler, N.; Safro, M.
Crystallization and X-ray analysis of human cytoplasmic phenylalanyl-tRNA synthetase
Acta Crystallogr. Sect. F
65
93-97
2009
Homo sapiens (O95363), Homo sapiens
brenda
Vasileva, I.A.; Semenova, E.A.; Moor, N.A.
Interaction of human phenylalanyl-tRNA synthetase with specific tRNA according to thiophosphate footprinting
Biochemistry (Moscow)
74
175-185
2009
Homo sapiens
brenda
Yadavalli, S.S.; Klipcan, L.; Zozulya, A.; Banerjee, R.; Svergun, D.; Safro, M.; Ibba, M.
Large-scale movement of functional domains facilitates aminoacylation by human mitochondrial phenylalanyl-tRNA synthetase
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583
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2009
Homo sapiens (O95363), Homo sapiens
brenda
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Cell-specific differences in the requirements for translation quality control
Proc. Natl. Acad. Sci. USA
107
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2010
Saccharomyces cerevisiae, Escherichia coli, Homo sapiens
brenda
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Structure of human cytosolic phenylalanyl-tRNA synthetase: evidence for kingdom-specific design of the active sites and tRNA binding patterns
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18
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2010
Homo sapiens (Q9NSD9), Homo sapiens (Q9Y285), Homo sapiens
brenda
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2011
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Mutation of the human mitochondrial phenylalanine-tRNA synthetase causes infantile-onset epilepsy and cytochrome c oxidase deficiency
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1842
56-64
2014
Homo sapiens
brenda
Moor, N.; Klipcan, L.; Safro, M.G.
Bacterial and eukaryotic phenylalanyl-tRNA synthetases catalyze misaminoacylation of tRNAPhe with 3,4-dihydroxy-L-phenylalanine
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18
1221-1229
2011
Thermus thermophilus, Homo sapiens, Homo sapiens (O95363)
brenda
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Chimeric human mitochondrial PheRS exhibits editing activity to discriminate nonprotein amino acids
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25
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2016
Homo sapiens (O95363), Homo sapiens
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26
1505-1516
2017
Homo sapiens (O95363), Homo sapiens
brenda