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Information on EC 6.1.1.20 - phenylalanine-tRNA ligase and Organism(s) Homo sapiens
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6.1.1.20 phenylalanine-tRNA ligaseSpecify your search results
Word Map
- 6.1.1.20
- aminoacylation
- synthetases
- aminoacyl-trna
-
phenylalanylation
- thermophilus
- thermus
-
anticodon
-
aarss
-
proofreading
- phe-trnaphe
-
noncognate
- tyrosyl-trna
-
misacylated
- seryl-trna
- threonyl-trna
-
misaminoacylated
-
mischarging
- trna-phe
-
aminoacyladenylate
- valyl-trna
-
alphabeta2
- biotechnology
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
phenylalanyl-trna synthetase, phers, fars2, mitochondrial phenylalanyl-trna synthetase, mtphers, phenylalanine trna synthetase, phenylalanine-trna synthetase, mitochondrial phers, ecphers, hcphers, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CML33
cytoplasmic phenylalanyl-tRNA synthetase
cytosolic phenylalanyl-tRNA synthetase
FARS2
FRS
hcPheRS
HSPC173
L-Phenylalanyl-tRNA synthetase
mitochondrial phenylalanyl-tRNA synthetase
mtPheRS
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
PheRS
Synthetase, phenylalanyl-transfer ribonucleate
CML33
-
-
-
-
FRS
-
-
-
-
HSPC173
-
-
-
-
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
-
-
-
-
Phenylalanyl-tRNA synthetase
-
-
PheRS
-
-
-
-
Synthetase, phenylalanyl-transfer ribonucleate
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
tRNA recognition and binding mode
ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
tRNAPhe substrate binding mechanism, base-specific interactions between the 3'-end of the tRNA and the enzymes alpha- and beta-subunit
-
ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
two-step reaction, the second reaction step is the ester bond formation between the 2'-hydroxyl group of the 3'-terminal adenosine base of the tRNA and the carboxylic acid function of phenylalanine
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Aminoacylation
esterification
Aminoacylation
-
-
-
-
esterification
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-phenylalanine:tRNAPhe ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY
9055-66-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 3,4-dihydroxy-L-phenylalanine + tRNAPhe
AMP + diphosphate + 3,4-dihydroxy-L-phenylalanyl-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 + 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
0.089% activity compared to L-phenylalanine
-
-
?
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 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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
mitochondrial isozyme, high concentration is required for maximal activity
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
spermine
optimal at 1 mM, stimulates 2-4fold the second reaction step, the ester bond formation between the 2'-hydroxyl group of the 3'-terminal adenosine base of the tRNA and the carboxylic acid function of phenylalanine
Mg2+
optimal at 5-10 mM, required, stimulates 2-4fold the second reaction step, the ester bond formation between the 2'-hydroxyl group of the 3'-terminal adenosine base of the tRNA and the carboxylic acid function of phenylalanine
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
0.0026
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
0.033
L-phenylalanine
ATP-diphosphate exchange reaction, recombinant mitochondrial isozyme, pH 7.3, 37°C
0.018
tRNAPhe
aminoacylation reaction, recombinant mitochondrial isozyme, pH 7.5, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.9
ATP
ATP-diphosphate exchange reaction, mitochondrial isozyme, pH 7.3, 37°C
0.033
L-tyrosine
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
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
0.075
L-phenylalanine
mitochondrial enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
0.87
L-phenylalanine
cytoplasmic enzyme, in 50 mM Tris-HCl, pH 8.0, 30 mM MgCl2, 20 mM KCl, 5 mM dithiothreitol, at 30°C
1.1
L-phenylalanine
ATP-diphosphate exchange reaction, recombinant mitochondrial isozyme, pH 7.3, 37°C
0.11
tRNAPhe
aminoacylation reaction, recombinant mitochondrial isozyme, pH 7.5, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.0136
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
enzyme content is increased in cancer cell lines, with the beta-subunit showing higher expression levels than the alpha-subunit
additional information
enzyme content is increased in cancer cell lines, with the beta-subunit showing higher expression levels than the alpha-subunit
additional information
-
enzyme content is increased in cancer cell lines, with the beta-subunit showing higher expression levels than the alpha-subunit
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
cytosolic phenylalanyl-tRNA synthetase exerts control over the translation accuracy, hydrolyzing misacylated products, while the monomeric mitochondrial enzyme lacks the editing activity
malfunction
-
mutation of the human mitochondrial phenylalanine-tRNA synthetase causes infantile-onset epilepsy and cytochrome c oxidase deficiency
malfunction
pathogenic variants of the FARS2 gene, encoding the human mitochondrial phenylalanine-tRNA synthetase lead to spastic paraplegia or fatal infantile Alpers encephalopathy
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SYFM_HUMAN
451
0
52357
Swiss-Prot
Mitochondrion (Reliability: 2)
SYFA_HUMAN
508
0
57564
Swiss-Prot
other Location (Reliability: 1)
SYFB_HUMAN
589
0
66116
Swiss-Prot
other Location (Reliability: 2)
Q9BR63_HUMAN
585
0
65701
TrEMBL
other Location (Reliability: 1)
A8K666_HUMAN
589
0
66044
TrEMBL
other Location (Reliability: 2)
K7EPH2_HUMAN
378
0
43042
TrEMBL
other Location (Reliability: 2)
K7ER00_HUMAN
548
0
62395
TrEMBL
other Location (Reliability: 5)
A0A3B3ITR6_HUMAN
433
0
50076
TrEMBL
Mitochondrion (Reliability: 2)
Q6IBR2_HUMAN
508
0
57564
TrEMBL
other Location (Reliability: 1)
B7ZB32_HUMAN
490
0
54815
TrEMBL
other Location (Reliability: 1)
Q5JRF7_HUMAN
101
0
11563
TrEMBL
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45000
48000
49600
55000
57000
66000
-
2 * 57000, alpha-subunit, + 2 * 66000, beta-subunit, (alphabeta)2, SDS-PAGE
48000
recombinant mitochondrial isozyme, analytical velocity sedimentation centrifugation
49600
recombinant mitochondrial isozyme, amino acid sequence determination
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
57000
-
2 * 57000, alpha-subunit, + 2 * 66000, beta-subunit, (alphabeta)2, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterotetramer
monomer
tetramer
additional information
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
monomer
1 * 48000, recombinant mitochondrial isozyme, analytical sedimentation centrifugation
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified mitochondrial PheRS complexed with Phe-AMP, cryoprotection by mother liquor solution containing 25% glycerol, X-ray diffraction structure determination and analysis at 2.2 A resolution
-
purified recombinant mitPheRS in complex with L-phenylalanine and ATP, hanging or sitting drop vapour diffusion method, 0.001-0.003 ml of protein solution containing 6 mg/ml protein in 20 mM Tris-HCl pH 8.0, 100 mM NaCl, 7 mM MgCl2, 5 mM 2-mercaptoethanol, 1 mM EDTA and 0.0065% NaN3, is mixed with an equal volume of reservoir solution containing 25 mM Tris-HCl pH 8.5, 10 mM MgCl2, 5 mM ATP, 2 mM L-phenylalanine, equilibration against reservoir solution, at 4°C or 19°C, X-ray diffraction structure determination and analysis at 2.2 A resolution
-
the structure of cytosolic phenylalanyl-tRNA synthetase in complex with phenylalanine is solved to 3.3 A resolution
the structure of human cytoplasmic phenylalanyl-tRNA synthetase is determined to a resolution of 3.3 A
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
alphaDELTA1-175
truncated N-terminal domain of the alpha subunit of hcPheRS
alphaDELTA60-170
truncated N-terminal domain of the alpha subunit of hcPheRS
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
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
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
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.5 - 8
-
high stability of wild-type and mutant mtPheRSs in the pH range, unfolding parameters, overview
715937
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, purified recombinant His-tagged mitochondrial isozyme, 50 mM Tris-HCl, pH 7.6, 50 mM KCl, 10 mM MgCl2, 7 mM 2-mercaptoethanol, 10% v/v glycerol, small aliquots, stable for at least 6 months
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate fractionation is followed by four chromatography columns, anion exchange on a DEAE-Sepharose column, a heparin-Sepharose column, concentrating the protein on a TSK hydrophobic interaction column and finally gel filtration on a column of superfine Sephadex G-200
mature mitPheRS in Escherichia coli by streptomycin precipitation, ultrafiltration, anion exchange chromatography and heparin affinity chromatography, followed by ammonium sulfate fractionation, hydrophobic interaction chromatography, and gel filtration, to homogeneity
-
recombinant His-tagged heterodimers and nontagged subunits from Escherichia coli, over 200fold
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination of the alpha- and beta-subunit and analysis, expression in COS-7 cells
DNA and amino acid sequence determination, individual cloning and coexpression of His-tagged alpha- and beta-subunits in Escherichia coli resulting in 3 different types of (alphabeta)2 heterodimers with the His-tag at the N-terminus, N-terminally His-tagged beta-subunit renders the enzyme inactive, overexpression of nontagged alpha- and beta-subunits in Escherichia coli
-
Escherichia coli pET21c+ encoding human mtPheRS, FARS2, produces mature His6-tagged wild-type PheRS
-
Escherichia coli strain BL21(pArgU218)/pET21c-PheRS expresses C-terminal His6-tagged mtPheRS, RosettaDE3 cells containing pRARE plasmids encoding tRNAs for rare codons are transformed with the mutant mtPheRS plasmid constructs
mature mitPheRS in Escherichia coli without His-tag, which causes oligomerization of the recombinant enzyme during purification
-
mitochondrial isozyme, DNA sequence determination and analysis, expression in Escherichia coli BL21(DE3) as His-tagged enzyme
the two subunits of hcPheRS are cloned into two different plasmids, the alpha subunit, residues 1-508, into the vector pET21b+, the beta-subunit, residues 1-589, into pET28b+, for expression in Escherichia coli BLRDE3 cells, no affinity tag is used
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zakharova, O.D.; Kotenko, I.; Lavrik, O.I.
Phenylalanyl-tRNA-synthetase from human placenta: isolation and characteristics
Biokhimiia
55
1025-1031
1990
Homo sapiens
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
475-478
1992
Homo sapiens
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
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
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
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
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
761-764
2007
Homo sapiens
Targoff, I.N.
Autoantibodies and their significance in myositis
Curr. Rheumatol. Rep.
10
333-340
2008
Homo sapiens
Klipcan, L.; Levin, I.; Kessler, N.; Moor, N.; Finarov, I.; Safro, M.
The tRNA-induced conformational activation of human mitochondrial phenylalanyl-tRNA synthetase
Structure
16
1095-1104
2008
Homo sapiens
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
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
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
FEBS Lett.
583
3204-3208
2009
Homo sapiens (O95363), Homo sapiens
Reynolds, N.M.; Ling, J.; Roy, H.; Banerjee, R.; Repasky, S.E.; Hamel, P.; Ibba, M.
Cell-specific differences in the requirements for translation quality control
Proc. Natl. Acad. Sci. USA
107
4063-4068
2010
Saccharomyces cerevisiae, Escherichia coli, Homo sapiens
Finarov, I.; Moor, N.; Kessler, N.; Klipcan, L.; Safro, M.G.
Structure of human cytosolic phenylalanyl-tRNA synthetase: evidence for kingdom-specific design of the active sites and tRNA binding patterns
Structure
18
343-353
2010
Homo sapiens (Q9NSD9), Homo sapiens (Q9Y285), Homo sapiens
Banerjee, R.; Reynolds, N.M.; Yadavalli, S.S.; Rice, C.; Roy, H.; Banerjee, P.; Alexander, R.W.; Ibba, M.
Mitochondrial aminoacyl-tRNA synthetase single-nucleotide polymorphisms that lead to defects in refolding but not aminoacylation
J. Mol. Biol.
410
280-293
2011
Homo sapiens
Almalki, A.; Alston, C.L.; Parker, A.; Simonic, I.; Mehta, S.G.; He, L.; Reza, M.; Oliveira, J.M.; Lightowlers, R.N.; McFarland, R.; Taylor, R.W.; Chrzanowska-Lightowlers, Z.M.
Mutation of the human mitochondrial phenylalanine-tRNA synthetase causes infantile-onset epilepsy and cytochrome c oxidase deficiency
Biochim. Biophys. Acta
1842
56-64
2014
Homo sapiens
Moor, N.; Klipcan, L.; Safro, M.G.
Bacterial and eukaryotic phenylalanyl-tRNA synthetases catalyze misaminoacylation of tRNAPhe with 3,4-dihydroxy-L-phenylalanine
Chem. Biol.
18
1221-1229
2011
Thermus thermophilus, Homo sapiens, Homo sapiens (O95363)
Kartvelishvili, E.; Peretz, M.; Tworowski, D.; Moor, N.; Safro, M.
Chimeric human mitochondrial PheRS exhibits editing activity to discriminate nonprotein amino acids
Protein Sci.
25
618-626
2016
Homo sapiens (O95363), Homo sapiens
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