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Information on EC 6.1.1.22 - asparagine-tRNA ligase and Organism(s) Thermus thermophilus and UniProt Accession P54263

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Thermus thermophilus
UNIPROT: P54263 not found.
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The taxonomic range for the selected organisms is: Thermus thermophilus
The enzyme appears in selected viruses and cellular organisms
Synonyms
asparaginyl-trna synthetase, nars2, asparagine synthetase a, as-ar, asparagyl-transfer rna synthetase, asparaginyl trna synthetase, asparagine-trna ligase, asparaginyl-transfer rna synthetase, asparagine trna synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Asparagine translase
-
Asparagine--tRNA ligase
-
Asparaginyl transfer ribonucleic acid synthetase
-
Asparaginyl transfer RNA synthetase
-
Asparaginyl-transfer ribonucleate synthetase
-
Asparaginyl-tRNA synthetase
-
Asparagyl-transfer RNA synthetase
-
Potentially protective 63 kDa antigen
-
Synthetase, asparaginyl-transfer ribonucleate
-
AsnRS
Asparagine translase
-
-
-
-
Asparagine--tRNA ligase
-
-
-
-
Asparaginyl transfer ribonucleic acid synthetase
-
-
-
-
Asparaginyl transfer RNA synthetase
-
-
-
-
Asparaginyl-transfer ribonucleate synthetase
-
-
-
-
Asparaginyl-tRNA synthetase
Asparagyl-transfer RNA synthetase
-
-
-
-
Potentially protective 63 kDa antigen
-
-
-
-
Synthetase, asparaginyl-transfer ribonucleate
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-asparagine + tRNAAsn = AMP + diphosphate + L-asparaginyl-tRNAAsn
show the reaction diagram
mechanism of substrate specificity, structure of substrate binding sites
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
-
-
-
-
Aminoacylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-asparagine:tRNAAsn ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
37211-76-0
-
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-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
show the reaction diagram
ATP + L-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
show the reaction diagram
additional information
?
-
-
analysis of the molecular mechanism by molecular dynamics simulations and computational calculations using wild-type andmutant enzymes, overview
-
-
?
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-asparagine + tRNAAsn
AMP + diphosphate + L-asparaginyl-tRNAAsn
show the reaction diagram
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
a single Mg2+ bound to the ligand's alpha-phosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
a single Mg2+ bound to ATP alpha-phosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
binding kinetics, affinities, and thermidynamics, molecular dynamics simulations, overview
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
purified recombinant enzyme expressed in Escherichia coli
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
-
x * 50875, calculation from nucleotide sequence, x * 50000, SDS-PAGE
50875
-
x * 50875, calculation from nucleotide sequence, x * 50000, SDS-PAGE
additional information
-
high similarity with other bacterial asparaginyl-tRNA synthetase sequences (30-55% identity)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
class II synthetase, crystal structure determination
?
-
x * 50875, calculation from nucleotide sequence, x * 50000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, native or complexed withATP and asparaginyl-adenylate, 3 different crystal forms, X-ray diffraction structure determination at 2.6 A resolution and analysis
AsnRS with bound asparaginyladenylate, AsnAMP, X-ray diffraction structure anaylsis at 2.6 A resolution
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85
-
21 h, retains 50% of its activity
90
-
1 h, retains 50% of its activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overproduced in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
engineering of aspartyladenylate, AspAMP, specificity into asparaginyl-tRNA synthetase, AsnRS, whose substrate is asparaginyl-adenylate by CPD method, that uses a polar-hydrogen energy function for protein interactions and a coulomb/accessible surface area model for solvent effects, method development, overview. Application of an all-atom energy for protein interactions and a residue-pairwise generalized Born model for solvent effects, overview. The conformations and interactions are well maintained in molecular dynamics simulations and the sequences have an inverted specificity, favoring AspAMP over AsnAMP
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Seignovert, L.; Hrtlein, M.; Leberman, R.
Asparaginyl-tRNA synthetase from Thermus thermophilus HB8. Sequence of the gene and crystallization of the enzyme expressed in Escherichia coli
Eur. J. Biochem.
239
501-508
1996
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Manually annotated by BRENDA team
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 (P54263), Thermus thermophilus
Manually annotated by BRENDA team
Lopes, A.; Schmidt Am Busch, M.; Simonson, T.
Computational design of protein-ligand binding: modifying the specificity of asparaginyl-tRNA synthetase
J. Comput. Chem.
31
1273-1286
2010
Thermus thermophilus
Manually annotated by BRENDA team
Polydorides, S.; Amara, N.; Aubard, C.; Plateau, P.; Simonson, T.; Archontis, G.
Computational protein design with a generalized born solvent model: application to asparaginyl-tRNA synthetase
Proteins
79
3448-3468
2011
Thermus thermophilus
Manually annotated by BRENDA team