Information on EC 6.1.1.B3 - glutamyl-Q-tRNA(Asp) ligase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
6.1.1.B3
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
glutamyl-Q-tRNA(Asp) ligase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-glutamate + tRNAAsp = AMP + diphosphate + L-glutamyl-tRNAAsp
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
L-glutamate:tRNAAsp ligase (AMP-forming)
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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 + tRNA
AMP + diphosphate + L-glutamyl-tRNA
show the reaction diagram
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acceptor is unfractionated RNA
the activation step of L-glutamate is tRNA-independent
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?
ATP + L-glutamate + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-glutamate + tRNAAsp
AMP + diphosphate + L-glutamyl-tRNAAsp
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
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enzyme possesses a Zn2+ ion located in the putative tRNA acceptor stem-binding domain. The Zn2+ ion is coordinated by three cysteine and a tyrosine ligand
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glutamol-adenosine monophosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.17 - 0.5
ATP
0.5 - 6
L-glutamate
0.00015
tRNAAsp
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pH 7.2, 37C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.2 - 18
L-glutamate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.73
L-glutamate
Escherichia coli
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pH 7.2, 37C
41
14700
tRNAAsp
Escherichia coli
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pH 7.2, 37C
785
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0002 - 0.44
glutamol-adenosine monophosphate
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
determination of strucure by molecular replacement, to 1.5 A resolution. Enzyme possesses a Zn2+ located in the putative tRNA acceptor stem-binding domain. The Zn2+ ion is coordinated by three cysteine and a tyrosine ligand
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partially purified by affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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