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

for references in articles please use BRENDA:EC6.3.2.43
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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota

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 metabolism
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Lysine biosynthesis
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Metabolic pathways
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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
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Manually annotated by BRENDA team
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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 + [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
ATP + [lysine-biosynthesis-protein LysW]-C-terminal-L-glutamate + L-glutamate
ADP + phosphate + [lysine-biosynthesis-protein LysW]-C-terminal-gamma-(L-glutam-2-yl)-L-glutamate
show the reaction diagram
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
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pH 8.0, 60°C
0.85
L-2-aminoadipate
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pH 8.0, 60°C
2
[LysW]-C-terminal-L-glutamate54
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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
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pH 8.0, 60°C
0.4
L-2-aminoadipate
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pH 8.0, 60°C
26
[LysW]-C-terminal-L-glutamate54
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pH 8.0, 60°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.016
substrate L-glutamate, pH not specified in the publication, temperature not specified in the publication
0.021
substrate L-2-aminoadipate, pH not specified in the publication, temperature not specified in the publication
PDB
SCOP
CATH
UNIPROT
ORGANISM
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579);
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in presence of carrier protein LysW and AMP-PNP, MgSO4, and L-2-aminoadipate or glutamate, to 2.18 A resolution
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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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in the presence of antimicrobial peptides, lysX expression increases significantly
in the presence of antimicrobial peptides, lysX expression increases significantly; in the presence of antimicrobial peptides, lysX expression increases significantly; in the presence of antimicrobial peptides, lysX expression increases significantly
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N264G/T265T
Y175I/I185Y/N250G/S251F
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine