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Information on EC 6.1.1.20 - phenylalanine-tRNA ligase and Organism(s) Thermus thermophilus and UniProt Accession Q5SGX2
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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: Thermus thermophilus
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, mitochondrial phers, phenylalanine trna synthetase, ecphers, hcphers, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
PheRS
Synthetase, phenylalanyl-transfer ribonucleate
CML33
-
-
-
-
FRS
-
-
-
-
HSPC173
-
-
-
-
L-Phenylalanyl-tRNA synthetase
-
-
-
-
L-Phenylalanyl-tRNA synthetase
-
-
Phenylalanine translase
-
-
-
-
Phenylalanine--tRNA ligase
-
-
-
-
Phenylalanine-tRNA synthetase
-
-
-
-
Phenylalanine-tRNA synthetase
-
-
Phenylalanyl transfer ribonucleic acid synthetase
-
-
-
-
Phenylalanyl transfer ribonucleic acid synthetase
-
-
Phenylalanyl-transfer ribonucleate synthetase
-
-
-
-
Phenylalanyl-transfer ribonucleate synthetase
-
-
Phenylalanyl-transfer RNA ligase
-
-
-
-
Phenylalanyl-transfer RNA ligase
-
-
Phenylalanyl-transfer RNA synthetase
-
-
-
-
Phenylalanyl-transfer RNA synthetase
-
-
Phenylalanyl-tRNA ligase
-
-
-
-
Phenylalanyl-tRNA synthetase
-
-
-
-
Phenylalanyl-tRNA synthetase
-
-
PheRS
-
-
-
-
PheRS
-
-
Synthetase, phenylalanyl-transfer ribonucleate
-
-
-
-
Synthetase, phenylalanyl-transfer ribonucleate
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
reaction mechanism
-
ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
mechanism, the reaction intermediate is bound to the active site cleft in the catalytic alpha-subunit
-
ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
substrate binding mechanism, residues S180, Q218, E220, W149, H178, R204, and Q218 are involved in binding of phenylalanine via hydrogen bonds
-
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 + 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 + 3,4-dihydroxy-L-phenylalanine + tRNAPhe
AMP + diphosphate + 3,4-dihydroxy-L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-Phe + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
-
?
ATP + L-phenylalanine + tRNAPhe-s6 G76
AMP + diphosphate + L-phenylalanyl-tRNAPhe-s6 G76
-
tRNAPhe variant, 370fold reduced activity compared to wild-type 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
-
-
?
additional information
?
-
-
no activity with tRNAPhe-s4 U76, a tRNA variant harboring a 4-thiouridine residue in the 3'-end
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
the enzyme probably interacts with DNA
-
?
additional information
?
-
the enzyme specifically binds certain Thermus thermophilus DNA sequences, accession number Y15464, of the genomic DNA
-
?
additional information
?
-
-
the enzyme specifically binds certain Thermus thermophilus DNA sequences, accession number Y15464, of the genomic DNA
-
?
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
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
editing activity of the isolated recombinant B3/4 editing domain from PheRS, 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
-
-
-
ir
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
-
r
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
-
?
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
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
-
not bound to the active site, located at the interface of alpha and beta subunits
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
additional information
-
the rate of overcharging of the tRNAPhe is dependenton the buffer system used
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the rate of overcharging of the tRNAPhe is dependenton the buffer system used
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.0017
L-phenylalanine
-
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-value for tRNA mutants
-
additional information
additional information
-
negative cooperativity exists in the binding of all substrates
-
additional information
additional information
-
kinetics, binding energies in the active conformation
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.16
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
1.12
L-phenylalanine
-
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 tRNA mutants
-
additional information
additional information
-
turnover-number of tRNAPheG34A is 10% of wild-type value, turnover-number of tRNAPheG34C/A35U is 31% of wild-type value, turnover-number of tRNAPheA36C is 4.2% of wild-type value, turnover-number of tRNAPheU20A is identical to wild-type value, turnover-number of tRNAPheG44C is 2.1% of wild-type value, turnover-number of tRNAPheG19U/C56G is 1.7% of wild-type value
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.43
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
650
L-phenylalanine
-
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
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). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
additional information
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of complexes of enzyme with L-Tyr, p-chlorophenylalanine, and L-tyrosyl-adenylate
-
enzyme complexed with phenylalanine or the phenylalanyl-adenylate analogue phenylalaninyl-adenylate, X-ray diffraction structure determination at 2.7 and 2.5 A resolution, respectively, and analysis
-
native enzyme complexed with phenylalanyl-adenylate in presence of manganese, X-ray diffraction structure determination at 2.6 A resolution and analysis
-
PheRS in complex with with cognate tRNAPhe and nonhydrolyzable phenylalanyladenylate analogue PheOH-AMP, hanging-drop vapor-diffusion method, 4°C, 3-5 mg/ml protein ina ratio of 1:2,5 with tRNAPhe in 20 mM imidazole-HCl, pH 7.8, 1 mM MgCl2, 5 mM 2-mercaptoethanol, 1 mM NaN3, 10% saturated ammonium sulfate, and 1 mM PheOH-AMP, slow equilibration against a reservoir solution containing the crystallization buffer and 27% saturated ammonium sulfate, cryoprotection by 30% v/v glycerol, X-ray diffraction structure determination and anaylsis at 3.1 A resolution, modeling
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type isolated B3/4 editing domain, and of the editing domain fused to the N-terminus of Escherichia coli iodoTyrRS to generate N-Ted-IYRS, overview
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bobkova, E.V.; Volfson, A.D.; Ankilova, V.N.; Lavrik, O.I.
Separation and comparative characteristics of subunits of phenylalanyl-tRNA synthetase from Escherichia coli MRE-600 and Thermus thermophilus HB8
Biokhimiia
55
525-533
1990
Escherichia coli, Escherichia coli MRE 600, Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Goldgur, Y.; Mosyak, L.; Reshetnikova, L.; Ankilova, V.; Lavrik, O.; Khodyreva, S.; Safro, M.
The crystal structure of phenylalanyl-tRNA synthetase from Thermus thermophilus complexed with tRNAPhe
Structure
5
59-68
1997
Thermus thermophilus
Ankilova, V.N.; Reshetnikova, L.S.; Chernaya, M.M.; Lavrik, O.I.
Phenylalanyl-tRNA synthetase from Thermus thermophilus HB8. Purification and properties of the crystallizing enzyme
FEBS Lett.
227
9-13
1988
Thermus thermophilus
-
Mosyak, L.; Reshetnikova, L.; Goldgur, Y.; Delarue, M.; Safro, M.G.
Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus
Nat. Struct. Biol.
2
537-547
1995
Thermus thermophilus
Chernaya, M.M.; Korolev, S.V.; Reshetnikova, L.S.; Safro, M.G.
Preliminary crystallographic study of the phenylalanyl-tRNA synthetase from Thermus thermophilus HB8
J. Mol. Biol.
198
555-556
1987
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Mosyak, L.; Safro, M.
Phenylalanyl-tRNA synthetase from Thermus thermophilus has four antiparallel folds of which only two are catalytically functional
Biochimie
75
1091-1098
1993
Thermus thermophilus
Stepanov, V.G.; Moor, N.A.; Ankilova, V.N.; Lavrik, O.I.
Phenylalanyl-tRNA synthetase from Thermus thermophilus can attach two molecules of phenylalanine to tRNAPhe
FEBS Lett.
311
192-194
1992
Thermus thermophilus
Moor, N.A.; Ankilova, V.N.; Lavrik, O.I.
Recognition of tRNAPhe by phenylalanyl-tRNA synthetase of Thermus thermophilus
Eur. J. Biochem.
234
897-902
1995
Thermus thermophilus
Bobkova, E.V.; Mashanov-Golikov, A.V.; Wolfson, A.; Ankilova, V.N.; Lavrik, O.I.
Comparative study of subunits of phenylalanyl-tRNA synthetase from Escherichia coli and Thermus thermophilus
FEBS Lett.
290
95-98
1991
Escherichia coli, Thermus thermophilus
Bobkova, E.V.; Stepanov, V.G.; Lavrik, O.I.
A comparative study of the relationship between thermostability and function of phenylalanyl-tRNA synthetase from Escherichia coli and Thermus thermophilus
FEBS Lett.
302
54-56
1992
Escherichia coli, Thermus thermophilus
Reshetnikova, L.; Chernaya, M.; Ankilova, V.; Lavrik, O.; Delarue, M.; Thierry, J.C.; Moras, D.; Safro, M.
Glycyl-tRNA synthetase: Three-dimensional structure of phenylalanyl-transfer RNA synthetase from Thermus thermophilus HB8 at 0.6-nm resolution
Eur. J. Biochem.
208
411-417
1992
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Fishman, R.; Ankilova, V.; Moor, N.; Safro, M.
Structure at 2.6 A resolution of phenylalanyl-tRNA synthetase complexed with phenylalanyl-adenylate in the presence of manganese
Acta Crystallogr. Sect. D
57
1534-1544
2001
Thermus thermophilus
Vasil'eva, I.A.; Ankilova, V.N.; Lavrik, O.I.; Moor, N.A.
Interaction of T. thermophilus phenylalanyl-tRNA synthetase with the 3'-terminal nucleotide of tRNAPhe
Biochemistry
65
1157-1166
2000
Thermus thermophilus
Ivanov, K.A.; Moor, N.A.; Ankilova, V.N.; Lavrik, O.I.
Phenylalanyl-tRNA synthetase interacts with DNA: studies on activity using deoxyribooligonucleotides
Biochemistry (Moscow)
65
436-441
2000
Thermus thermophilus
Stepanov, V.G.; Moor, N.A.; Ankilova, V.N.; Vasil'eva, I.A.; Sukhanova, M.V.; Lavrik, O.I.
A peculiarity of the reaction of tRNA aminoacylation catalyzed by phenylalanyl-tRNA synthetase from the extreme thermophile Thermus thermophilus
Biochim. Biophys. Acta
1386
1-15
1998
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Lechler, A.; Kreutzer, R.
The phenylalanyl-tRNA synthetase specifically binds DNA
J. Mol. Biol.
278
897-901
1998
Thermus thermophilus (Q5SGX2 and Q5SGX1), Thermus thermophilus
Reshetnikova, L.; Moor, N.; Lavrik, O.; Vassylyev, D.G.
Crystal structures of phenylalanyl-tRNA synthetase complexed with phenylalanine and a phenylalanyl-adenylate analogue
J. Mol. Biol.
287
555-568
1999
Thermus thermophilus
Kekenes-Huskey, P.M.; Vaidehi, N.; Floriano, W.B.; Goddard, W.A.
Fidelity of Phenylalanyl-tRNA Synthetase in Binding the Natural Amino Acids
J. Phys. Chem. B
107
11549-11557
2003
Thermus thermophilus
-
Vasil'eva, I.A.; Favre, A.; Lavrik, O.I.; Moor, N.A.
Effect of nucleotide replacement in tRNAPhe on positioning of the acceptor end in the complex with phenylalanine-tRNA synthetase
Biochemistry
69
154-163
2004
Thermus thermophilus
Kotik-Kogan, O.; Moor, N.; Tworowski, D.; Safro, M.
Structural basis for discrimination of L-phenylalanine from L-tyrosine by phenylalanyl-tRNA synthetase
Structure
13
1799-1807
2005
Thermus thermophilus
Moor, N.; Kotik-Kogan, O.; Tworowski, D.; Sukhanova, M.; Safro, M.
The crystal structure of the ternary complex of phenylalanyl-tRNA synthetase with tRNAPhe and a phenylalanyl-adenylate analogue reveals a conformational switch of the CCA end
Biochemistry
45
10572-10583
2006
Thermus thermophilus
Oki, K.; Sakamoto, K.; Kobayashi, T.; Sasaki, H.M.; Yokoyama, S.
Transplantation of a tyrosine editing domain into a tyrosyl-tRNA synthetase variant enhances its specificity for a tyrosine analog
Proc. Natl. Acad. Sci. USA
105
13298-13303
2008
Escherichia coli, Thermus thermophilus, Pyrococcus horikoshii
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