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Information on EC 6.1.1.12 - aspartate-tRNA ligase and Organism(s) Pseudomonas aeruginosa

for references in articles please use BRENDA:EC6.1.1.12

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The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms

Synonyms
aspartyl-trna synthetase, asprs, dars2, asnrs, mitochondrial aspartyl-trna synthetase, non-discriminating aspartyl-trna synthetase, cytoplasmic aspartyl-trna synthetase, mt-asprs, discriminating asprs, d-asprs, more

SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
Aminoacylation
esterification
PATHWAY SOURCE
PATHWAYS
MetaCyc
tRNA charging
SYSTEMATIC NAME
IUBMB Comments
L-aspartate:tRNAAsp ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9027-32-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY hide
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
show the reaction diagram
-
Substrates: -
Products: -
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY hide
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-aspartate + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
show the reaction diagram
-
Substrates: -
Products: -
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5'-O-[N-(L-aspartyl)sulfamoyl]adenosine
-
ASP-AMS
L-aspartol-adenylate
-
aspartol-AMP
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
L-aspartate
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.041
L-aspartol-adenylate
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
aspartylation and inhibition assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
aspartylation and inhibition assay
top print hide Go to Organism Search
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line Links Gene Links
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A485IPZ1_PSEAI
174
0
18557
TrEMBL
-
A0A485IPM3_PSEAI
418
0
48618
TrEMBL
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
the adaption of pathogens to antibiotics calls for new target macromolecules and new types of inhibitors
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Messmer, M.; Blais, S.P.; Balg, C.; Chenevert, R.; Grenier, L.; Laguee, P.; Sauter, C.; Sissler, M.; Giege, R.; Lapointe, J.; Florentz, C.
Peculiar inhibition of human mitochondrial aspartyl-tRNA synthetase by adenylate analogs
Biochimie
91
596-603
2009
Bos taurus, Escherichia coli, Homo sapiens, Pseudomonas aeruginosa
Manually annotated by BRENDA team