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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 6.1.1.12 - aspartate-tRNA ligase and Organism(s) Helicobacter pylori and UniProt Accession P56459

for references in articles please use BRENDA:EC6.1.1.12
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:
Helicobacter pylori
UNIPROT: P56459 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: Helicobacter pylori
The enzyme appears in selected viruses and cellular organisms
Synonyms
aspartyl-trna synthetase, asprs, dars2, asnrs, mitochondrial aspartyl-trna synthetase, cytoplasmic aspartyl-trna synthetase, non-discriminating aspartyl-trna synthetase, mt-asprs, discriminating asprs, d-asprs, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Aspartyl-tRNA synthetase
-
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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
-
-
-
-
Aminoacylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-aspartate:tRNAAsp ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9027-32-1
-
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-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
show the reaction diagram
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
show the reaction diagram
-
-
-
?
ATP + L-aspartate + tRNAAsn
AMP + diphosphate + L-aspartyl-tRNAAsn
show the reaction diagram
-
-
-
-
?
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12870
-
1 * 12870, calculated from amino acid sequence
15500
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 12870, calculated from amino acid sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 7% (w/v) PEG 4000, 0.1 M ammonium sulfate, 0.1 M sodium citrate pH 5.6
hanging drop vapor diffusion method, in 30% (w/v) PEG 4000, 100 mM ammonium sulfate, 100 mM sodium citrate at pH 5.6
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 42
-
the enzyme is stable up to 42°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography, and Sephacryl S200 gel filtration
Ni-NTA column chromatography and Hiprep 16/60 Sephacryl S-200 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fuengfuloy, P.; Chuawong, P.; Suebka, S.; Wattana-Amorn, P.; Williams, C.; Crump, M.P.; Songsiriritthigul, C.
Overproduction of the N-terminal anticodon-binding domain of the non-discriminating aspartyl-tRNA synthetase from Helicobacter pylori for crystallization and NMR measurements
Protein Expr. Purif.
89
25-32
2013
Helicobacter pylori
Manually annotated by BRENDA team
Songsiriritthigul, C.; Suebka, S.; Chen, C.J.; Fuengfuloy, P.; Chuawong, P.
Crystal structure of the N-terminal anticodon-binding domain of the nondiscriminating aspartyl-tRNA synthetase from Helicobacter pylori
Acta Crystallogr. Sect. F
73
62-69
2017
Helicobacter pylori (P56459), Helicobacter pylori ATCC 700392 (P56459)
Manually annotated by BRENDA team