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Information on EC 6.1.1.12 - aspartate-tRNA ligase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P04802
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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: Saccharomyces cerevisiae
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
-
-
-
-
Aspartate--tRNA ligase
-
-
-
-
Aspartic acid translase
Aspartyl ribonucleate synthetase
Aspartyl ribonucleic synthetase
-
-
-
-
Aspartyl-transfer ribonucleic acid synthetase
Aspartyl-transfer RNA synthetase
Aspartyl-tRNA synthetase
AspRS
Synthetase, aspartyl-transfer ribonucleate
-
-
-
-
Aspartic acid translase
-
-
-
-
Aspartyl ribonucleate synthetase
-
-
-
-
Aspartyl ribonucleate synthetase
-
-
Aspartyl-transfer ribonucleic acid synthetase
-
-
-
-
Aspartyl-transfer ribonucleic acid synthetase
-
-
Aspartyl-transfer RNA synthetase
-
-
-
-
Aspartyl-transfer RNA synthetase
-
-
Aspartyl-tRNA synthetase
-
-
-
-
Aspartyl-tRNA synthetase
-
-
AspRS
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp
mechanism
-
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
RNA-binding motif XSKXXLKKXK
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
esterification
Aminoacylation
esterification
-
-
-
-
Aminoacylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-aspartate:tRNAAsp ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY
9027-32-1
-
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 + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
tRNA undergoes large conformational changes upon binding to the enzyme, specific charging of amino acid resdiue on tRNA, accurate recognition by the enzyme is achieved through sequence and structural signalling
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
the N-terminal extension of each AspRS subunit plays a crucial role in anchoring the tRNA-like motifs of the mRNA on the synthetase
-
-
?
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
-
-
-
?
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
-
specificty of tRNA recognition by the enzyme is primarily ensured by the tRNA identity determinants, the discriminator base G37, four bases in the anticodon loop G34, U35, C36, and C38, and G10-U25 base pair in the core region of the tRNA, substrate specificity of wild-type and truncated mutant enzymes, overview
-
?
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
-
the yeast AspRS not only binds and aminoacylates tRNAAsp but also binds its yeast mRNA and initiates retro-inhibition of its expression, overview
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
-
the yeast enzyme also binds its own mRNA and autoinhibits itself
-
-
?
additional information
?
-
-
erroneous binding of Asn by the enzyme is highly improbable, determination of binding energy
-
?
additional information
?
-
-
the enzyme also binds to its mRNA via its N-terminal extension of 70 amino acid residues and the anticodon-binding module, which has a regulatory function on the expression of the enzyme
-
?
additional information
?
-
-
misaspartylation of tRNAAsn and tRNAGlu does not exist in vivo
-
-
?
additional information
?
-
-
increased concentrations of AspRS lead to the accumulation of significant amounts of Asp-tRNAAsn and Asp-tRNAGlu in vitro, but not in vivo. The enzyme does not perform autoaspartylation
-
-
?
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 + 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
-
the yeast AspRS not only binds and aminoacylates tRNAAsp but also binds its yeast mRNA and initiates retro-inhibition of its expression, overview
-
-
?
additional information
?
-
-
the enzyme also binds to its mRNA via its N-terminal extension of 70 amino acid residues and the anticodon-binding module, which has a regulatory function on the expression of the enzyme
-
?
additional information
?
-
-
misaspartylation of tRNAAsn and tRNAGlu does not exist in vivo
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the yeast AspRS initiates retro-inhibition of its expression, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Km values of ATP-diphosphate exchange reaction and acylation of homodimers and heterodimers of AspRS molecules
-
additional information
additional information
-
kinetics of several tRNAAsp variants
-
additional information
additional information
-
kinetics, tRNAAsp mimics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
activity of tRNAAsp mimics
-
additional information
additional information
-
catalytic efficiency of several tRNAAsp variants
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
additional information
-
the N-terminal 70 amino acid residues extension protrudes from the anticodon-binding module, it is not essential for acylation activity but contains the RNA-binding motif that promotes non-specific interactions with the tRNAs, it can also interact with the 5'-end of the enzyme's mRNA
additional information
-
the N-terminal appendix of 70 amino acid residues adopts a helical structure and encompasses the RNA binding motif XSKXXLKKXK
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the enzyme does not perform autoaspartylation in vivo
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant truncated enzyme, tri- and tetragonal crystals, X-ry structure determination at 3 and 2.3 A resolution, respectively, molecular replacement, structure analysis and modeling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D210A
-
central core binding mutant, increased acylation activity, increased dissociation constant
E188A
-
anticodon loop binding mutant, slightly reduced acylation activity, increased dissociation constant
E188A/S239A
-
anticodon-G73 binding mutant, reduced acylation activity, highly increased dissociation constant
E188A/T331A
-
anticodon-G73 binding mutant, highly reduced acylation activity, highly increased dissociation constant
E202A
-
central core binding mutant, slightly increased acylation activity, increased dissociation constant
F127A
-
anticodon loop binding mutant, increased acylation activity, increased dissociation constant
F127A/D210A
-
anticodon binding mutant, reduced acylation activity, highly increased dissociation constant
F127A/E188A
-
anticodon binding mutant, reduced acylation activity, highly increased dissociation constant
F127A/S239A
-
anticodon-G73 binding mutant, reduced acylation activity, highly increased dissociation constant
F127A/T331A
-
anticodon-G73 binding mutant, highly reduced acylation activity, highly increased dissociation constant
H116G
-
mutants with substituted His residues, His116Gly mutant with a slightly reduced rate of amino acid activation without affecting the other kinetic parameters, His271Gly mutant with completely destroyed activity, His332Gly mutant with 60% decrease in rate of tRNA aminoacylation and no significant changes in the other parameters, His334Gly mutant with 70% decrease in amino acid activation, complete loss of tRNA aspartylation and slightly increased Km for ATP, His271Ala mutant with 25% decrease in the rate of tRNA charging. His334 seems do be part of the active site, while His271 and His332 play an important structural role
H334A
-
acceptor arm binding mutant, highly reduced acylation activity, increased dissociation constant
K142A
-
anticodon loop binding mutant, increased acylation activity, increased dissociation constant
K142A/E188A
-
anticodon binding mutant, reduced acylation activity, highly increased dissociation constant
K155A
-
central core binding mutant, increased acylation activity, increased dissociation constant
K180A
-
anticodon loop binding mutant, slightly increased acylation activity, increased dissociation constant
K293A
-
acceptor arm binding mutant, highly increased acylation activity, increased dissociation constant
K428A
-
acceptor arm binding mutant, increased acylation activity, increased dissociation constant
K553A
-
acceptor arm binding mutant, acylation activity similar to wild-type, increased dissociation constant
N117A
-
anticodon loop binding mutant, increased acylation activity, increased dissociation constant
N227A
-
central core binding mutant, slightly increased acylation activity, increased dissociation constant
N328A
-
acceptor arm binding mutant, reduced acylation activity, increased dissociation constant
N328A/S329A/T331A
-
G73 binding mutant, highly reduced acylation activity, increased dissociation constant
P273G
-
Pro273Gly mutant. Catalytic properties of native and Pro273Gly homodimers or heterodimers of AspRS molecules, confirm the participation of Pro273 in subunit association
Q121A
-
anticodon loop binding mutant, increased acylation activity, increased dissociation constant
Q138A
-
anticodon loop binding mutant, slightly increased acylation activity, increased dissociation constant
Q138A/E188A
-
anticodon binding mutant, reduced acylation activity, highly increased dissociation constant
Q138A/R119A
-
anticodon binding mutant, reduced acylation activity, highly increased dissociation constant
R119A
-
anticodon loop binding mutant, increased acylation activity, increased dissociation constant
R119A/E188A
-
anticodon binding mutant, highly reduced acylation activity, highly increased dissociation constant
R485K
-
site-directed mutagenesis, the substitution in the catalytic site completely inhibits aspartylation by impairing ATP binding, this mutant still retains the capacity to be modified and shows the same pattern as wild-type AspRS on the two-dimensional gel, thus the modifications are not the result of autoaspartylation
S181A
-
anticodon loop binding mutant, increased acylation activity, increased dissociation constant
S301A
-
terminal A binding mutant, reduced acylation activity, slightly increased dissociation constant
S329A
-
acceptor arm binding mutant, increased acylation activity, increased dissociation constant
T124A
-
anticodon loop binding mutant, slightly reduced acylation activity, increased dissociation constant
T230A
-
central core binding mutant, increased acylation activity, increased dissociation constant
T331A
-
acceptor arm binding mutant, reduced acylation activity, increased dissociation constant
T424A
-
acceptor arm binding mutant, acylation activity similar to the wild-type, increased dissociation constant
additional information
additional information
-
C-terminal and N-terminal truncated forms. On the C-terminal side, very limited modifications readily affect the enzyme properties. The N-terminal sequence up to amino acid 70 is dispensable for activity, domains beyond amino acid 70 have increasing catalytic importance
additional information
-
truncated form that has lost the first 50-64 residues, with full retention of both the activity and the dimeric structure
additional information
-
construction of several N-terminal deletion mutants with altered mRNA binding properties, overview
additional information
-
cooperativity analysis of the G73 and anticodon binding interactions, overview, effect of mutations on cell growth
additional information
-
proteomic analysis of mutant cells in comparison to wild-type cells
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged enzyme from Escherichia coli strain Top10 by glutathione affinity chromatography, the tag is then cleaved of by thrombin, and the enzyme is further purified by adsorption chromatography yielding an AspRS with a short additional amino acid stretch at its N-terminus
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
truncated enzyme lacking 70 amino acid residues in the N-terminus, overexpression in Escherichia coli
expression in Saccharomyces cerevisiae, and expression as His-tagged protein
-
expression of wild-type and mutant enzymes in yeast YBC-603 cells, functional overexpression of GST- and His6-tagged enzyme in Escherichia coli strain Top10. Expression in yeast cells at low copy number, since overexpression is cytotoxic, while moderate AspRS accumulation in the cell is not deleterious
-
expression of wild-type enzyme, amino acid residues 1-557, and a truncated mutant enzyme, amino acid resdiues 71-557, as His-tagged proteins in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Escalante, C.; Yang, D.C.
Expression of human aspartyl-tRNA synthetase in Escherichia coli. Functional analysis of the N-terminal putative amphiphilic helix
J. Biol. Chem.
268
6014-6023
1993
Bacteria, Saccharomyces cerevisiae, Homo sapiens, Mammalia
Cavarelli, J.; Rees, B.; Thierry, J.C.; Moras, D.
Yeast aspartyl-tRNA synthetase: a structural view of the aminoacylation reaction
Biochimie
75
1117-1123
1993
Saccharomyces cerevisiae
Eriani, G.; Prevost, G.; Kern, D.; Vincendon, P.; Dirheimer, G.; Gangloff, J.
Cytoplasmic aspartyl-tRNA synthetase from Saccharomyces cerevisiae. Study of its functional organisation by deletion analysis
Eur. J. Biochem.
200
337-343
1991
Saccharomyces cerevisiae
Gasparini, S.; Vincendon, P.; Eriani, G.; Gangloff, J.; Boulanger, Y.; Reinbolt, J.; Kern, D.
Identification of structurally and functionally important histidine residues in cytoplasmic aspartyl-tRNA synthetase from Saccharomyces cerevisiae
Biochemistry
30
4284-4289
1991
Saccharomyces cerevisiae
Eriani, G.; Caravelli.J.; Martin, F.; Dirheimer, G.; Moras, D.
Role of dimerization in yeast aspartyl-tRNA synthetase and importance of the class II invariant proline
Proc. Natl. Acad. Sci. USA
90
10816-10820
1993
Saccharomyces cerevisiae
Gangloff, J; Dirheimer, G.
Studies on aspartyl-tRNA synthetase from baker's yeast. I. Purification and properties of the enzyme
Biochim. Biophys. Acta
294
263-272
1973
Saccharomyces cerevisiae, Saccharomyces cerevisiae C836
Dietrich, A.; Giege, R.; Comarmond, M.B.; Thierry, J.C.; Moras, D.
Crystallographic studies on the aspartyl-tRNA synthetase-tRNAAsp system from yeast
J. Mol. Biol.
138
129-135
1980
Saccharomyces cerevisiae
Drocourt, J.L.; Gangloff, J.; Dirheimer, G.; Thang, M.N.
Interaction of yeast arginyl-tRNA synthetase and aspartyl-tRNA synthetase with blue-dextran Sepharose: assignement of the blue-dextran binding site on the synthetase
Biochem. Biophys. Res. Commun.
97
787-793
1980
Saccharomyces cerevisiae
Lorber, B.; Kern, D.; Dietrich, A.; Gangloff, J.; Ebel, J.P.; Giege, R.
Large scale purification and structural properties of yeast aspartyl-tRNA synthetase
Biochem. Biophys. Res. Commun.
117
259-267
1983
Saccharomyces cerevisiae
Lorber, B.; Mejdoub, H.; Reinbolt, J.; Boulanger, Y.; Giege, R.
Properties of N-terminal truncated yeast aspartyl synthetase and structural characteristics of the cleaved domain
Eur. J. Biochem.
174
155-161
1988
Saccharomyces cerevisiae
Ruff, M.; Cavarelli, J.; Mikol, V.; Lorber, B.; Mitschler, A.; Giege, R.; Thierry, J.C.; Moras, D.
A high resolution diffracting crystal form of the complex between yeast tRNAAsp and aspartyl-tRNA synthetase
J. Mol. Biol.
201
235-236
1988
Saccharomyces cerevisiae
Wolfson, A.D.; Khvorova, A.M.; Sauter, C.; Florentz, C.; Giege, R.
Mimics of yeast tRNAAsp and their recognition by aspartyl-tRNA synthetase
Biochemistry
38
11926-11932
1999
Saccharomyces cerevisiae
Ryckelynck, M.; Giege, R.; Frugier, M.
Yeast tRNA(Asp) charging accuracy is threatened by the N-terminal extension of aspartyl-tRNA synthetase
J. Biol. Chem.
278
9683-9690
2003
Saccharomyces cerevisiae
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
Eriani, G.; Gangloff, J.
Yeast aspartyl-tRNA synthetase residues interacting with tRNA(Asp) identity bases connectively contribute to tRNA(Asp) binding in the ground and transition-state complex and discriminate against non-cognate tRNAs
J. Mol. Biol.
291
761-773
1999
Saccharomyces cerevisiae
Sauter, C.; Lorber, B.; Cavarelli, J.; Moras, D.; Giege, R.
The free yeast aspartyl-tRNA synthetase differs from the tRNA(Asp)-complexed enzyme by structural changes in the catalytic site, hinge region, and anticodon-binding domain
J. Mol. Biol.
299
1313-1324
2000
Saccharomyces cerevisiae (P04802), Saccharomyces cerevisiae
Frugier, M.; Giege, R.
Yeast aspartyl-tRNA synthetase binds specifically its own mRNA
J. Mol. Biol.
331
375-383
2003
Saccharomyces cerevisiae
Ryckelynck, M.; Masquida, B.; Giege, R.; Frugier, M.
An intricate RNA structure with two tRNA-derived motifs directs complex formation between yeast aspartyl-tRNA synthetase and its mRNA
J. Mol. Biol.
354
614-629
2005
Saccharomyces cerevisiae (P04802), Saccharomyces cerevisiae
Ryckelynck, M.; A Paulus, C.; Frugier, M.
Post-translational modifications guard yeast from misaspartylation
Biochemistry
47
12476-12482
2008
Saccharomyces cerevisiae
Bour, T.; Akaddar, A.; Lorber, B.; Blais, S.; Balg, C.; Candolfi, E.; Frugier, M.
Plasmodial aspartyl-tRNA synthetases and peculiarities in Plasmodium falciparum
J. Biol. Chem.
284
18893-18903
2009
Saccharomyces cerevisiae, Homo sapiens, Plasmodium falciparum (Q8I2B1), Plasmodium falciparum
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