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Information on EC 6.1.1.2 - tryptophan-tRNA ligase and Organism(s) Pyrococcus horikoshii and UniProt Accession O59584

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Pyrococcus horikoshii
UNIPROT: O59584 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
tryptophanyl-trna synthetase, trprs, wars2, mini-trprs, t2-trprs, tryptophanyl trna synthetase, htrprs, trprs1, trprs ii, trp-rs, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Tryptophanyl-tRNA synthetase
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(Mt)TrpRS
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hWRS
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IFP53
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Synthetase, tryptophanyl-transfer ribonucleate
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TrpRS
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Tryptophan translase
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Tryptophan--tRNA ligase
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Tryptophanyl ribonucleic synthetase
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Tryptophanyl-transfer ribonucleate synthetase
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Tryptophanyl-transfer ribonucleic acid synthetase
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Tryptophanyl-transfer ribonucleic synthetase
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Tryptophanyl-transfer RNA synthetase
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Tryptophanyl-tRNA synthase
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Tryptophanyl-tRNA synthetase
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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-tryptophan:tRNATrp ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9023-44-3
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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-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
show the reaction diagram
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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-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
show the reaction diagram
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-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystal structure of the enzyme in complex with tryptophanyl-5' AMP at 3.0 A resolution
the structure of tryptophanyl-tRNA synthetase in complex with tryptophanyl-5' AMP is solved at 3.0 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
on a Ni-affinity column
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
the trpS1 gene is inserted into the vector pET28a for expression in Escherichia coli BL21DE3 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dong, X.; Zhou, M.; Zhong, C.; Yang, B.; Shen, N.; Ding, J.
Crystal structure of Pyrococcus horikoshii tryptophanyl-tRNA synthetase and structure-based phylogenetic analysis suggest an archaeal origin of tryptophanyl-tRNA synthetase
Nucleic Acids Res.
38
1401-1412
2010
Pyrococcus horikoshii (O59584), Pyrococcus horikoshii
Manually annotated by BRENDA team
Dong, X.; Zhou, M.; Zhong, C.; Yang, B.; Shen, N.; Ding, J.
Crystal structure of Pyrococcus horikoshii tryptophanyl-tRNA synthetase and structure-based phylogenetic analysis suggest an archaeal origin of tryptophanyl-tRNA synthetase
Nucleic Acids Res.
38
1401-1412
2009
Pyrococcus horikoshii (O59584), Pyrococcus horikoshii
Manually annotated by BRENDA team