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Information on EC 6.1.1.17 - glutamate-tRNA ligase and Organism(s) Pseudomonas aeruginosa

for references in articles please use BRENDA:EC6.1.1.17
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This record set is specific for:
Pseudomonas aeruginosa
Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
Synonyms
glurs, glutaminyl-trna synthetase, glutamyl-trna synthetase, glurs2, trna modifying enzyme, glurs1, glutamyl trna synthetase, discriminating glurs, glursat, tm1351, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
discriminating GluRS
-
GluRS
Glutamate--tRNA ligase
-
-
-
0
Glutamate-tRNA synthetase
-
-
-
0
Glutamic acid translase
-
-
-
0
Glutamic acid tRNA ligase
-
-
-
0
Glutamyl tRNA synthetase
-
-
-
0
Glutamyl-transfer ribonucleate synthetase
-
-
-
0
Glutamyl-transfer ribonucleic acid synthetase
-
-
-
0
Glutamyl-transfer RNA synthetase
-
-
-
0
Glutamyl-tRNA synthetase
P85
-
-
-
0
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu
show the reaction diagram
a two-step reaction , in the first step, the enzyme condenses the cognate amino acid and ATP, forming an aminoacyl-adenylate intermediate with a diphosphate as the leaving group. This reaction is reversible in the absence of the tRNA. In the absence of tRNAGlu, ATP binding by GluRS is nonproductive because the alpha-phosphate of ATP and the alpha-carboxyl groups of Glu are positioned too far apart for a reaction to occur. The presence of tRNAGlu causes conformational changes surrounding the ATP binding site, allowing ATP to bind in the productive state, which moves the alpha-phosphate of the ATP closer to the alpha-carboxyl groups of Glu, allowing the reaction for the formation of the glutamyl-AMP intermediate to occur
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Aminoacylation
-
-
-
0
esterification
-
-
-
0
SYSTEMATIC NAME
IUBMB Comments
L-glutamate:tRNAGlu ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9068-76-2
-
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-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
show the reaction diagram
-
-
0
?
additional information
?
-
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-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N'-(3-chlorophenyl)-N-(5,5-dimethyl-3-[(E)-[(2E)-3-(5-nitrofuran-2-yl)prop-2-en-1-ylidene]amino]-2-sulfanylidene-1,3-thiazolidin-4-yl)-N-hydroxyurea
competitive with glutamic acid but noncompetitive with ATP
N-(2,4-difluorophenyl)-N'-[4-[1-phenyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]phenyl]urea
noncompetitive with both ATP and glutamic acid
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00068
tRNAGlu
pH 7.5, 37°C
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8
tRNAGlu
pH 7.5, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1176.5
tRNAGlu
pH 7.5, 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0249
N'-(3-chlorophenyl)-N-(5,5-dimethyl-3-[(E)-[(2E)-3-(5-nitrofuran-2-yl)prop-2-en-1-ylidene]amino]-2-sulfanylidene-1,3-thiazolidin-4-yl)-N-hydroxyurea
Pseudomonas aeruginosa
pH 7.5, 37°C
0.0219
N-(2,4-difluorophenyl)-N'-[4-[1-phenyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]phenyl]urea
Pseudomonas aeruginosa
pH 7.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the tRNA binding site is less conserved than either the Glu or the ATP binding site. Certain amino acids, including Arg147, which interacts with the tRNAGlu C74 phosphate, and Asp44 and Arg47, which interact with the 2'-hydroxyl group of C75, as well as Tyr187 and Thr43, which interact with the adenosine base and the 5'-hydroxyl group of A76, are strictly conserved
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A485F3H9_PSEAI
494
0
56732
TrEMBL
-
A0A485E7P7_PSEAI
494
0
56691
TrEMBL
-
A0A6H1QJL7_PSEAI
494
0
56719
TrEMBL
-
A0A0F6RRG6_PSEAI
494
0
56807
TrEMBL
-
A0A643H6V7_PSEAI
494
0
56735
TrEMBL
-
A0A431XC45_PSEAI
494
0
56732
TrEMBL
-
A0A6B0QFF6_PSEAI
494
0
56739
TrEMBL
-
A0A2R3IXA4_PSEAI
494
0
56718
TrEMBL
-
A0A0A8RGV1_PSEAI
494
0
56680
TrEMBL
-
A0A6H3G423_PSEAI
494
0
56739
TrEMBL
-
A0A6A9JVL7_PSEAI
494
0
56741
TrEMBL
-
A0A509JME9_PSEAI
494
0
56793
TrEMBL
-
A0A485EQS8_PSEAI
312
0
35713
TrEMBL
-
A0A0C7CSP6_PSEAI
494
0
56749
TrEMBL
-
A0A3E1MYX9_PSEAI
494
0
56777
TrEMBL
-
A0A2S5IJ14_PSEAI
493
0
56450
TrEMBL
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme to over 98% homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene gltX, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant enzyme expression
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hu, Y.; Guerrero, E.; Keniry, M.; Manrrique, J.; Bullard, J.M.
Identification of chemical compounds that inhibit the function of glutamyl-tRNA synthetase from Pseudomonas aeruginosa
J. Biomol. Screen.
20
1160-1170
2015
Pseudomonas aeruginosa (Q9XCL6), Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1 (Q9XCL6)
Manually annotated by BRENDA team
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