Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 6.1.1.3 - threonine-tRNA ligase and Organism(s) Staphylococcus aureus and UniProt Accession Q8NW68

for references in articles please use BRENDA:EC6.1.1.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Staphylococcus aureus
UNIPROT: Q8NW68 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Staphylococcus aureus
The enzyme appears in selected viruses and cellular organisms
Synonyms
threonyl-trna synthetase, thrrs, thr-trna synthetase, mitochondrial threonyl-trna synthetase, threonyl trna synthetase, threonine-trna ligase, threonyl-transfer ribonucleic acid synthetase, bathrrs, apthrrs-1, apthrrs-2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Synthetase, threonyl-transfer ribonucleate
-
Threonine translase
-
Threonine--tRNA ligase
-
Threonine-transfer ribonucleate synthetase
-
Threonyl-ribonucleic synthetase
-
Threonyl-transfer ribonucleate synthetase
-
Threonyl-transfer ribonucleic acid synthetase
-
Threonyl-transfer RNA synthetase
-
Threonyl-tRNA synthetase
-
Synthetase, threonyl-transfer ribonucleate
-
-
-
-
Threonine translase
-
-
-
-
Threonine--tRNA ligase
-
-
-
-
Threonine-transfer ribonucleate synthetase
-
-
-
-
Threonyl-ribonucleic synthetase
-
-
-
-
Threonyl-transfer ribonucleate synthetase
-
-
-
-
Threonyl-transfer ribonucleic acid synthetase
-
-
-
-
Threonyl-transfer RNA synthetase
-
-
-
-
Threonyl-tRNA synthetase
-
-
-
-
ThrRS
-
-
-
-
TRS
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr
show the reaction diagram
substrate binding and mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
-
-
-
-
Aminoacylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-threonine:tRNAThr ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9023-46-5
-
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-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
show the reaction diagram
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-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
show the reaction diagram
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme complexed with ATP and threonine and complexed with substrate analogue 5'-O-(N-(L-threonyl)-sulfamoyl)adenosine, hanging drop method, 15 mg/ml protein in 20 mM HEPES, pH 7.2, 2 mM MgCl2, 100 mM KCl, in a 1:1:1 mixture with ligand solution containing 10 mM MgCl2, 10 mM ATP or 1 mM Thr-AMS, and well solution containing 50 mM Tris-HCl, pH 7.5-8.5, PEG 8000 12-14% w/v, and ammonium acetate or potassium chloride in the range 0.2-0.4 M, 2-3 days at 4°C, X-ray diffraction structure determination at resolution 2.8-3.2 A, structure analysis, modeling
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant from Escherichia coli
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Torres-Larios, A.; Sankaranarayanan, R.; Rees, B.; Dock-Bregeon, A.C.; Moras, D.
Conformational movements and cooperativity upon amino acid, ATP and tRNA binding in threonyl-tRNA synthetase
J. Mol. Biol.
331
201-211
2003
Staphylococcus aureus (Q8NW68), Staphylococcus aureus
Manually annotated by BRENDA team