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

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Pseudomonas aeruginosa
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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, cytoplasmic aspartyl-trna synthetase, non-discriminating 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
-
-
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
-
-
-
-
?
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
-
-
-
-
?
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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