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Information on EC 6.1.1.20 - phenylalanine-tRNA ligase and Organism(s) Pyrococcus horikoshii and UniProt Accession O73984

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Pyrococcus horikoshii
UNIPROT: O73984 not found.
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The taxonomic range for the selected organisms is: Pyrococcus horikoshii
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, cytoplasmic phenylalanyl-trna synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Phenylalanyl-tRNA synthetase
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CML33
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FRS
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HSPC173
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L-Phenylalanyl-tRNA synthetase
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Phenylalanine translase
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Phenylalanine--tRNA ligase
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Phenylalanine-tRNA synthetase
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Phenylalanyl transfer ribonucleic acid synthetase
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Phenylalanyl-transfer ribonucleate synthetase
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Phenylalanyl-transfer RNA ligase
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Phenylalanyl-transfer RNA synthetase
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Phenylalanyl-tRNA ligase
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Phenylalanyl-tRNA synthetase
PheRS
Synthetase, phenylalanyl-transfer ribonucleate
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
residue N217 is essential for catalysis
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
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Aminoacylation
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
L-phenylalanine:tRNAPhe ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9055-66-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
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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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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
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?
ATP + L-phenylalanine + tRNAPhe
AMP + diphosphate + L-phenylalanyl-tRNAPhe
show the reaction diagram
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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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
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant selenomethionine-labeled N-terminal fragment of the PheRS beta-subunit, 0.001 ml of protein solution containing 36 mg/ml protein in 20 mM Tris-HCl buffer, pH 8.0, containing 200 mM NaCl, mixed with 0.001 ml of precipitant solution, containing 100 mM sodium citrate, pH 5.6, and 16.5% PEG 20000, covarage with a 1:1 mixture of paraffin oil and silicone, 20°C, 1 week, soaking in a soaked in a cryoprotectant solution containing 100 mM sodium citrate, pH 5.6, 18.2% PEG 20000, and 20% glycerol, X-ray diffraction structure determination and analysis at 1.94 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminal fragment of the PheRS beta-subunit from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, recombinant selenomethionine-labeled N-terminal fragment of the PheRS beta-subunit from Escherichia coli strain B834(DE3) by anion exchange chromatography, adsorption chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of N-terminal fragment of the PheRS beta-subunit in Escherichia coli strain BL21(DE3), expression of selenomethionine-labeled N-terminal fragment of the PheRS beta-subunit in Escherichia coli strain B834(DE3)
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-Ped-IYRS, overview
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sasaki, H.M.; Sekine, S.; Sengoku, T.; Fukunaga, R.; Hattori, M.; Utsunomiya, Y.; Kuroishi, C.; Kuramitsu, S.; Shirouzu, M.; Yokoyama, S.
Structural and mutational studies of the amino acid-editing domain from archaeal/eukaryal phenylalanyl-tRNA synthetase
Proc. Natl. Acad. Sci. USA
103
14744-14749
2006
Pyrococcus horikoshii (O73984), Pyrococcus horikoshii
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team