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Information on EC 6.1.1.22 - asparagine-tRNA ligase and Organism(s) Pyrococcus horikoshii and UniProt Accession O57980

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Pyrococcus horikoshii
UNIPROT: O57980 not found.
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Word Map
The taxonomic range for the selected organisms is: Pyrococcus horikoshii
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
Asparaginyl-tRNA synthetase
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AsnRS
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Asparagine translase
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Asparagine--tRNA ligase
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Asparaginyl transfer ribonucleic acid synthetase
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Asparaginyl transfer RNA synthetase
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Asparaginyl-transfer ribonucleate synthetase
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Asparaginyl-tRNA synthetase
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Asparagyl-transfer RNA synthetase
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Potentially protective 63 kDa antigen
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Synthetase, asparaginyl-transfer ribonucleate
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additional information
the enzyme belongs to the class-II aminoacyl-tRNA synthetase family
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-asparagine + tRNAAsn = AMP + diphosphate + L-asparaginyl-tRNAAsn
show the reaction diagram
substrate binding structure, active site structure, tRNAAsn and amino acid recognition, binding of Asn-AMP induces a conformational change in AsnRS
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-asparagine:tRNAAsn ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
37211-76-0
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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
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5'-O-[N-(L-asparaginyl)sulfamoyl]adenosine
a non-hydrolysable analogue of asparaginyl adenylate, i.e. Asn-SA
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
AsnRS complexed with asparaginyl-adenylate Asn-AMP, or free AsnRS and AsnRS complexed with an Asn-AMP analog Asn-SA, sitting-drop vapor diffusion method at 20°C, 0.001 ml protein solution is mixed with an equal volume of reservoir solution containing 25 mM sodium cacodylate buffer, pH 6.5, 50 mM sodium acetate trihydrate, and 7.5% w/v PEG 8000, equilibration against 0.5 ml reservoir solution, for ligand complex formation the crystals are soaked in a reservoir solution, containing 1.5 mM AMP-PNP, 1.5 mM asparagine, and 2 mM MgCl2, for approximately 10 h, followed by a reservoir solution containing 25% 2-methyl-2,4-pentanediol for a few seconds, X-ray diffraction strucure determination and analysis at 1.45 A, and 1.98 A and 1.8 A resolution, respectively
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R83A
site-directed mutagenesis, active site amino acid binding mutant, structure analysis in comparison to the wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by anion exchange and hydroxyapatite chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Iwasaki, W.; Sekine, S.; Kuroishi, C.; Kuramitsu, S.; Shirouzu, M.; Yokoyama, S.
Structural basis of the water-assisted asparagine recognition by asparaginyl-tRNA synthetase
J. Mol. Biol.
360
329-342
2006
Pyrococcus horikoshii (O57980), Pyrococcus horikoshii
Manually annotated by BRENDA team