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Information on EC 6.1.1.12 - aspartate-tRNA ligase and Organism(s) Thermus thermophilus and UniProt Accession Q5SIC2
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EC Tree
6.1.1.12 aspartate-tRNA ligaseSpecify your search results
Word Map
- 6.1.1.12
- synthetases
- aminoacyl-trna
- aminoacylation
-
aspartylation
-
asparaginyl-trna
-
anticodon
- leukoencephalopathy
- trnaasn
-
aarss
-
amidotransferase
-
aspartyl-adenylate
-
microcin
-
asparaginylation
- asp-trnaasn
- glnrs
- gatcabs
-
anticodon-binding
- glutaminyl-trna
-
misacylated
-
mischarged
-
transamidation
-
nondiscriminating
- lysyl-trna
- argrs
- trnaphe
- leurs
- medicine
-
glutaminylation
- pharmacology
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
aspartyl-trna synthetase, asprs, dars2, asnrs, mitochondrial aspartyl-trna synthetase, non-discriminating aspartyl-trna synthetase, cytoplasmic aspartyl-trna synthetase, mt-asprs, discriminating asprs, d-asprs, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Antigen T5
-
-
-
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Aspartate--tRNA ligase
-
-
-
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Aspartic acid translase
Aspartyl ribonucleate synthetase
Aspartyl ribonucleic synthetase
-
-
-
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aspartyl ribonuleic synthetase
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-
Aspartyl-transfer ribonucleic acid synthetase
Aspartyl-transfer RNA synthetase
Aspartyl-tRNA synthetase
AspRS
Synthetase, aspartyl-transfer ribonucleate
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-
-
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Aspartic acid translase
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-
-
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Aspartic acid translase
-
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Aspartyl ribonucleate synthetase
-
-
-
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Aspartyl ribonucleate synthetase
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-
Aspartyl-transfer ribonucleic acid synthetase
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-
-
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Aspartyl-transfer ribonucleic acid synthetase
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Aspartyl-transfer RNA synthetase
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-
-
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Aspartyl-transfer RNA synthetase
-
-
Aspartyl-tRNA synthetase
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-
-
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Aspartyl-tRNA synthetase
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-
AspRS
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp
active site residues
-
ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp
conserved amino acid residues of functional importance in consensus motifs: Pro227 in motif 1, Arg332 and Glu334 in motif 2, Gly675, Gly679, Asp681, Arg682, and Pro700 in motif 3
ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp
conserved amino acid residues of functional importance in consensus motifs: Pro227 in motif 1, Arg332 and Glu334 in motif 2, Gly675, Gly679, Glu681, Arg682, and Pro700 in motif 3
ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp
determination of structural features for discriminating or nondiscriminating aminoacylation activity
-
ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp
mechanism, active site structure, substrate binding, simulations of binding and free energy
-
ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp
pathway for tRNA binding and recognition is proposed
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
esterification
Aminoacylation
aminoacyl group transfer
esterification
-
-
-
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Aminoacylation
-
-
-
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PATHWAY SOURCE
PATHWAYS
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-
SYSTEMATIC NAME
IUBMB Comments
L-aspartate:tRNAAsp ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY
9027-32-1
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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 + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsp
about half as effective as tRNAAsp
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsp
about have as effective as tRNAAsp
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
Thermus thermophilus or Escherichia coli tRNA
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?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
Thermus thermophilus or Eschrichia coli tRNA
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
the archaeal AspRS2 enzyme is nondiscriminating, which means that it forms Asp-tRNAAsp and Asp-tRNAAsn
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
non-discriminating AspRS2
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
non-discriminating AspRS2, recombinantly produced tRNAAsn
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
specific amino acid binding by the enzyme is required for correct translation of the genetic code
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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discriminating AspRS1 and non-discriminating AspRS2
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-
?
additional information
?
-
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aspartate-dependent ATP-diphosphate exchange
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-
?
additional information
?
-
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erroneous binding of Asn by the enzyme is highly improbable, determination of binding energy
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?
additional information
?
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aspartyl- and asparaginyl-tRNA synthetases have evolved relatively recently from a comon ancestor
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?
additional information
?
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-
in Thermus thermophilus Asn-tRNAAsn is formed indirectly via a two-step pathway whereby tRNAAsn is mischarged with Asp that will subsequently be amidated into Asn by an amidotransferase.The non-discriminating aspartyl-tRNA synthetase, the trimeric GatCAB tRNA-dependent amidotransferase and the tRNAAsn promoting this pathway assemble into a ribonucleoprotein particle termed transamidosome, analysis of the mechanism of Asn-tRNAAsn formation by the transamidosome, overview
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-
?
additional information
?
-
-
Thermus thermophilus contains two AspRSs: the discriminating AspRS1 which aspartylates only tRNAAsp and the non-discriminating AspRS2 which aspartylates tRNAAsn as efficiently as tRNAAsp
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-
?
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-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
the archaeal AspRS2 enzyme is nondiscriminating, which means that it forms Asp-tRNAAsp and Asp-tRNAAsn
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
-
non-discriminating AspRS2
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
specific amino acid binding by the enzyme is required for correct translation of the genetic code
-
?
additional information
?
-
-
aspartyl- and asparaginyl-tRNA synthetases have evolved relatively recently from a comon ancestor
-
?
additional information
?
-
-
in Thermus thermophilus Asn-tRNAAsn is formed indirectly via a two-step pathway whereby tRNAAsn is mischarged with Asp that will subsequently be amidated into Asn by an amidotransferase.The non-discriminating aspartyl-tRNA synthetase, the trimeric GatCAB tRNA-dependent amidotransferase and the tRNAAsn promoting this pathway assemble into a ribonucleoprotein particle termed transamidosome, analysis of the mechanism of Asn-tRNAAsn formation by the transamidosome, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03
Asp
-
37°C, ATP-diphosphate exchange, and 70°C, tRNAaminoacylation, enzyme form AspRS1
0.1
Asp
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70°C, ATP-diphosphate exchange by enzyme form AspRS1, and tRNA aminoacylation by enzyme form AspRS2
additional information
additional information
-
Km value of pure tRNA, transcript tRNA and unfractionated tRNAs of various origins with enzyme form AspRS1 and enzyme form AspRS2
-
additional information
additional information
-
very low kinetic effiency at 17°C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.043
recombinant enzyme, Escherichia coli DH5alpha cell extract, 37°C
0.055
recombinant enzyme, Escherichia coli BL21 cell extract, 37°C
0.124
recombinant enzyme, Escherichia coli BL21 cell extract, 37°C
0.155
recombinant enzyme, Escherichia coli DH5alpha cell extract, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
7 different mutants, modification of crystal surfaces, investigation of crystallizability to determine the influence of surface residues and protein structure on crystal growth, packing arrangement, and quality
-
enzyme complexed with a non-hydrolysable analogue of asparaginyl-adenylate and with ATP, X-ray diffraction structure determination at 2.6 A resolution
-
isozyme AspRS2, hanging-drop vapour diffusion method, pH 9.5, in presence of PEG 8000 and NaCl, structure determination
-
purified enzyme complexed with tRNAAsp from Thermus thermophilus or Escherichia coli, potential intermediate of the recognition process, protein solution: 15 mg/ml of enzyme, 7.35 mg/ml of tRNA, plus equal volume of reservoir solution: 10 mM MgCl2, 50 mM HEPES, pH 7.5, 0.7 M sodium citrate, 17°C, 2 weeks, X-ray diffraction structure determination at 3.5 A resolution, structure analysis
-
purified recombinant enzyme, hanging-drop vapour diffusion method, in presence of PEG 8000, at 293K, growth kinetics and solubility measurements, X-ray diffraction structure determination at 3.1 A resolution
-
purified wild-type and seleno-Met isozymes AspRS2, vapour phase diffusion from mother liquid: 100 mM CHES buffer, pH 9.5, 200 mM NaCl, 10% w/v PEG 8000, X-ray diffraction structure determination at 2.3 A resolution, structure analysis
-
AspRS2, hanging drop vapour diffusion method, 0.002 ml of 14 mg/ml protein with 10% m/v PEG 8000, 200 mM NaCl, and 100 mM Na-CHES buffer, pH 9.5, X-ray diffraction structure determination and analysis at 2.3-3.2 A resolution
-
hanging-drop vapour-diffusion method, enzyme crystallizes either in a monoclinic or an orthorhombic habit. Minute amounts of protein impurities alter to a different extent the growth of each crystal form. The best synthetase crystals are obtained when the crystallizating solution is either enclosed in capillaries or immobilized in agarose gels
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant AspRS2 from Escherichia coli by two different steps of anion exchange chromatography and hydroxy apatite chromatography
-
recombinant from overexpressing Escherichia coli, 34.3fold
recombinant wild-type and seleno-Met isozyme 2 from overexpressing Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
aspS1 gene, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strains DH5alpha and BL21
aspS2 gene, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strains DH5alpha and BL21
overexpression in Escherichia coli
overexpression of wild-type isozyme AspRS2 and seleno-Met isozyme AspRS2 in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Poterszman, A.; Plateau, P.; Moras, D.; Blanquet, S.; Mazauric, M.H.; Kreutzer, R.; Kern, D.
Sequence, overproduction and crystallization of aspartyl-tRNA synthetase from Thermus thermophilus
FEBS Lett.
325
183-186
1993
Thermus thermophilus (P36419), Thermus thermophilus, Thermus thermophilus VK-1 (P36419), Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (P36419)
Becker, H.D.; Reinbolt, J.; Kreutzer, R.; Giege, R.; Kern, D.
Existence of two distinct aspartyl-tRNA synthetases in Thermus thermophilus. Structural and biochemical properties of the two enzymes
Biochemistry
36
8785-8797
1997
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Delarue, M.; Poterszman, A.; Nikonov, S.; Garber, M.; Moras, D.; Thierry, J.C.
Crystal structure of a prokaryotic aspartyl tRNA-synthetase
EMBO J.
13
3219-3229
1994
Thermus thermophilus
Becker, H.D.; Roy, H.; Moulinier, L.; Mazauric, M.H.; Keith, G.; Kern, D.
Thermus thermophilus contains an eubacterial and an archaebacterial aspartyl-tRNA synthetase
Biochemistry
39
3216-3230
2000
Thermus thermophilus (P36419), Thermus thermophilus (Q5SIC2), Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (P36419), Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q5SIC2)
Charron, C.; Roy, H.; Lorber, B.; Kern, D.; Giege, R.
Crystallization and preliminary X-ray diffraction data of the second and archaebacterial-type aspartyl-tRNA synthetase from Thermus thermophilus
Acta Crystallogr. Sect. D
57
1177-1179
2001
Thermus thermophilus
Zhu, D.W.; Lorber, B.; Sauter, C.; Ng, J.D.; Benas, P.; Le Grimellec, C.; Giege, R.
Growth kinetics, diffraction properties and effect of agarose on the stability of a novel crystal form of Thermus thermophilus aspartyl-tRNA synthetase-1
Acta Crystallogr. Sect. D
57
552-558
2001
Thermus thermophilus
Charron, C.; Kern, D.; Giege, R.
Crystal contacts engineering of aspartyl-tRNA synthetase from Thermus thermophilus: effects on crystallizability
Acta Crystallogr. Sect. D
58
1729-1733
2002
Thermus thermophilus
Berthet-Colominas, C.; Seignovert, L.; Hartlein, M.; Grotli, M.; Cusack, S.; Leberman, R.
The crystal structure of asparaginyl-tRNA synthetase from Thermus thermophilus and its complexes with ATP and asparaginyl-adenylate: the mechanism of discrimination between asparagine and aspartic acid
EMBO J.
17
2947-2960
1998
Thermus thermophilus
Charron, C.; Roy, H.; Blaise, M.; Giege, R.; Kern, D.
Non-discriminating and discriminating aspartyl-tRNA synthetases differ in the anticodon-binding domain
EMBO J.
22
1632-1643
2003
Thermus thermophilus, Thermococcus kodakarensis
Archontis, G.; Simonson, T.; Moras, D.; Karplus, M.
Specific amino acid recognition by aspartyl-tRNA synthetase studied by free energy simulations
J. Mol. Biol.
275
823-846
1998
Saccharomyces cerevisiae, Escherichia coli, Thermus thermophilus
Briand, C.; Poterszman, A.; Eiler, S.; Webster, G.; Thierry, J.; Moras, D.
An intermediate step in the recognition of tRNA(Asp) by aspartyl-tRNA synthetase
J. Mol. Biol.
299
1051-1060
2000
Thermus thermophilus
Moreno, A.; Theobald-Dietrich, A.; Lorber, B.; Sauter, C.; Giege, R.
Effects of macromolecular impurities and of crystallization method on the quality of eubacterial aspartyl-tRNA synthetase crystals
Acta Crystallogr. Sect. D
61
789-792
2005
Thermus thermophilus
Bailly, M.; Blaise, M.; Roy, H.; Deniziak, M.; Lorber, B.; Birck, C.; Becker, H.D.; Kern, D.
tRNA-dependent asparagine formation in prokaryotes: Characterization, isolation and structural and functional analysis of a ribonucleoprotein particle generating Asn-tRNAAsn
Methods
44
146-163
2008
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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