Information on EC 6.3.2.43 - [lysine-biosynthesis-protein LysW]-L-2-aminoadipate ligase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria

EC NUMBER
COMMENTARY hide
6.3.2.43
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RECOMMENDED NAME
GeneOntology No.
[lysine-biosynthesis-protein LysW]-L-2-aminoadipate ligase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + [lysine-biosynthesis-protein LysW]-C-terminal-L-glutamate + L-2-aminoadipate = ADP + phosphate + [lysine-biosynthesis-protein LysW]-C-terminal-gamma-(L-2-aminoadip-2-yl)-L-glutamate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-lysine biosynthesis V
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Lysine biosynthesis
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Metabolic pathways
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lysine metabolism
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SYSTEMATIC NAME
IUBMB Comments
[lysine-biosynthesis-protein LysW]-C-terminal-L-glutamate:L-2-aminoadipate ligase (ADP-forming)
The enzymes from the thermophilic bacterium Thermus thermophilus and the thermophilic archaea Sulfolobus acidocaldarius and Sulfolobus tokodaii protect the amino group of L-2-aminoadipate by conjugation to the carrier protein LysW. This reaction is part of the lysine biosynthesis pathway in these organisms.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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 + [LysW]-C-terminal-L-glutamate + L-2-aminoadipate
ADP + phosphate + [LysW]-C-terminal-gamma-(L-2-aminoadip-2-yl)-L-glutamate
show the reaction diagram
ATP + [LysW]-C-terminal-L-glutamate + L-2-aminoadipate
ADP + phosphate + [LysW]-gamma-(L-2-aminoadip-2-yl)-L-glutamate
show the reaction diagram
ATP + [LysW]-C-terminal-L-glutamate54 + L-2-aminoadipate
ADP + phosphate + [LysW]-C-terminal-gamma-(L-2-aminoadip-2-yl)-L-glutamate54
show the reaction diagram
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 + [LysW]-C-terminal-L-glutamate + L-2-aminoadipate
ADP + phosphate + [LysW]-gamma-(L-2-aminoadip-2-yl)-L-glutamate
show the reaction diagram
ATP + [LysW]-C-terminal-L-glutamate54 + L-2-aminoadipate
ADP + phosphate + [LysW]-C-terminal-gamma-(L-2-aminoadip-2-yl)-L-glutamate54
show the reaction diagram
Q5SH23
the enzyme is involved in biosynthesis of lysine. LysX activates the gamma-carboxyl group of the C-terminal Glu54 of the 2-L-aminoaadipate carrier-protein LysW by phosphorylation, with concomitant conversion of ATP to ADP. LysX recognizes not only the C-terminal glutamate residue of LysW but also other portions, possibly the globular domain of LysW specifically
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.6
ATP
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pH 8.0, 60°C
2.1
L-2-aminoadipate
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pH 8.0, 60°C
0.078
[LysW]-C-terminal-L-glutamate54
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pH 8.0, 60°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.2
ATP
Thermus thermophilus
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pH 8.0, 60°C
0.85
L-2-aminoadipate
Thermus thermophilus
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pH 8.0, 60°C
2
[LysW]-C-terminal-L-glutamate54
Thermus thermophilus
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pH 8.0, 60°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.7
ATP
Thermus thermophilus
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pH 8.0, 60°C
4
0.4
L-2-aminoadipate
Thermus thermophilus
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pH 8.0, 60°C
1790
26
[LysW]-C-terminal-L-glutamate54
Thermus thermophilus
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pH 8.0, 60°C
42692
PDB
SCOP
CATH
ORGANISM
UNIPROT
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structures of LysX and its complex with ADP at 2.0 A and 2.38 A resolutions
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crystal structures of the AMP-PNP–bound complex of LysX
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hanging-drop vapour-diffusion technique in two different space groups, C2 (unit-cell parameters a = 124.7, b = 51.4, c = 103.6 A, beta = 122.8) and R3 (a = b = 122.6, c = 97.6 A)
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli BL21
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N264G/T265T