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Enzyme Nomenclature
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: Bacteria, Archaea, Eukaryota
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EC NUMBER 
COMMENTARY 
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
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
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
no growth of deletion mutant without L-lysine. Growth is possible with lysine supplementation. A 0.05-mM concentration of lysine is most effective to support the growth of the deletion mutant, but a higher concentration of lysine decreases the growth rate
malfunction
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no growth of deletion mutant without L-lysine. Growth is possible with lysine supplementation. A 0.05-mM concentration of lysine is most effective to support the growth of the deletion mutant, but a higher concentration of lysine decreases the growth rate
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physiological function
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the enzyme is involved in the biosynthesis of lysine through the L-2-aminoadipate pathway
physiological function
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the enzyme is involved in biosynthesis of lysine in Thermus thermophilus
physiological function
lysine biosynthesis. Protection of the amino group of L-2-aminoadipate by conjugation to the carrier protein LysW
physiological function
Thermococcus kodakarensis has the potential to biosynthesize lysine and ornithine using the carrier protein LysW-mediated system with a single set of bifunctional enzymes
physiological function
in the presence of antimicrobial peptides produced by epithelial cells and macrophages, lysX expression increases significantly. Strains with higher lysX expression show increased levels of intracellular survival in vivo and in vitro and induce more severe lesion related with pneumonia. The ability of Mycobacterium tuberculosis to replicate intracellularly is directly correlated to the level of lysX expression; in the presence of antimicrobial peptides produced by epithelial cells and macrophages, lysX expression increases significantly. Strains with higher lysX expression show increased levels of intracellular survival in vivo and in vitro and induce more severe lesion related with pneumonia. The ability of Mycobacterium tuberculosis to replicate intracellularly is directly correlated to the level of lysX expression; in the presence of antimicrobial peptides produced by epithelial cells and macrophages, lysX expression increases significantly. Strains with higher lysX expression show increased levels of intracellular survival in vivo and in vitro and induce more severe lesion related with pneumonia. The ability of Mycobacterium tuberculosis to replicate intracellularly is directly correlated to the level of lysX expression
physiological function
-
in the presence of antimicrobial peptides produced by epithelial cells and macrophages, lysX expression increases significantly. Strains with higher lysX expression show increased levels of intracellular survival in vivo and in vitro and induce more severe lesion related with pneumonia. The ability of Mycobacterium tuberculosis to replicate intracellularly is directly correlated to the level of lysX expression
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physiological function
Mycobacterium tuberculosis LAM09005186
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in the presence of antimicrobial peptides produced by epithelial cells and macrophages, lysX expression increases significantly. Strains with higher lysX expression show increased levels of intracellular survival in vivo and in vitro and induce more severe lesion related with pneumonia. The ability of Mycobacterium tuberculosis to replicate intracellularly is directly correlated to the level of lysX expression
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physiological function
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lysine biosynthesis. Protection of the amino group of L-2-aminoadipate by conjugation to the carrier protein LysW
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physiological function
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Thermococcus kodakarensis has the potential to biosynthesize lysine and ornithine using the carrier protein LysW-mediated system with a single set of bifunctional enzymes
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physiological function
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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the enzyme is involved in the biosynthesis of lysine through the L-2-aminoadipate pathway
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
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
ATP + [LysW]-C-terminal-L-glutamate + L-2-aminoadipate
ADP + phosphate + [LysW]-C-terminal-gamma-(L-2-aminoadip-2-yl)-L-glutamate
ATP + [LysW]-C-terminal-L-glutamate + L-2-aminoadipate
ADP + phosphate + [LysW]-gamma-(L-2-aminoadip-2-yl)-L-glutamate
ATP + [LysW]-C-terminal-L-glutamate54 + L-2-aminoadipate
ADP + phosphate + [LysW]-C-terminal-gamma-(L-2-aminoadip-2-yl)-L-glutamate54
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
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-
-
?
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
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-
-
?
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
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-
-
?
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
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-
-
?
ATP + [LysW]-C-terminal-L-glutamate + L-2-aminoadipate
ADP + phosphate + [LysW]-C-terminal-gamma-(L-2-aminoadip-2-yl)-L-glutamate
mutant enzyme N264G/T265T shows a substrate preference for glutamate over L-2-aminoadipate contrasting distinctly with the substrate specificity of wild-type enzyme, which shows a distinct preference for L-2-aminoadipate over glutamate
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-
?
ATP + [LysW]-C-terminal-L-glutamate + L-2-aminoadipate
ADP + phosphate + [LysW]-C-terminal-gamma-(L-2-aminoadip-2-yl)-L-glutamate
mutant enzyme N264G/T265T shows a substrate preference for glutamate over L-2-aminoadipate contrasting distinctly with the substrate specificity of wild-type enzyme, which shows a distinct preference for L-2-aminoadipate over glutamate
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-
?
ATP + [LysW]-C-terminal-L-glutamate + L-2-aminoadipate
ADP + phosphate + [LysW]-gamma-(L-2-aminoadip-2-yl)-L-glutamate
lysine biosynthesis. Protection of the amino group of L-2-aminoadipate by conjugation to the carrier protein LysW
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-
?
ATP + [LysW]-C-terminal-L-glutamate + L-2-aminoadipate
ADP + phosphate + [LysW]-gamma-(L-2-aminoadip-2-yl)-L-glutamate
lysine biosynthesis. Protection of the amino group of L-2-aminoadipate by conjugation to the carrier protein LysW
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-
?
ATP + [LysW]-C-terminal-L-glutamate54 + L-2-aminoadipate
ADP + phosphate + [LysW]-C-terminal-gamma-(L-2-aminoadip-2-yl)-L-glutamate54
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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-
?
ATP + [LysW]-C-terminal-L-glutamate54 + L-2-aminoadipate
ADP + phosphate + [LysW]-C-terminal-gamma-(L-2-aminoadip-2-yl)-L-glutamate54
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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?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
ATP + [LysW]-C-terminal-L-glutamate54 + L-2-aminoadipate
ADP + phosphate + [LysW]-C-terminal-gamma-(L-2-aminoadip-2-yl)-L-glutamate54
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
-
-
?
ATP + [LysW]-C-terminal-L-glutamate + L-2-aminoadipate
ADP + phosphate + [LysW]-gamma-(L-2-aminoadip-2-yl)-L-glutamate
Q4JAP9
lysine biosynthesis. Protection of the amino group of L-2-aminoadipate by conjugation to the carrier protein LysW
-
-
?
ATP + [LysW]-C-terminal-L-glutamate + L-2-aminoadipate
ADP + phosphate + [LysW]-gamma-(L-2-aminoadip-2-yl)-L-glutamate
Q4JAP9
lysine biosynthesis. Protection of the amino group of L-2-aminoadipate by conjugation to the carrier protein LysW
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-
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
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
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579);
Q5SH23
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579);
Q5SH23
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579);
Q5SH23
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579);
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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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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
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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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
in the presence of antimicrobial peptides, lysX expression increases significantly
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in the presence of antimicrobial peptides, lysX expression increases significantly
Mycobacterium tuberculosis LAM09005186
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N264G/T265T
Y175I/I185Y/N250G/S251F
N264G/T265T
the mutant shows a substrate preference for glutamate over L-2-aminoadipate contrasting distinctly with the substrate specificity of wild-type enzyme, which shows a distinct preference for L-2-aminoadipate over glutamate
N264G/T265T
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the mutant shows a substrate preference for glutamate over L-2-aminoadipate contrasting distinctly with the substrate specificity of wild-type enzyme, which shows a distinct preference for L-2-aminoadipate over glutamate
-
Y175I/I185Y/N250G/S251F
mutant exhibits an apparent substrate preference for glutamate
Y175I/I185Y/N250G/S251F
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mutant exhibits an apparent substrate preference for glutamate
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
in the presence of antimicrobial peptides produced by epithelial cells and macrophages, lysX expression increases significantly. Strains with higher lysX expression show increased levels of intracellular survival in vivo and in vitro and induce more severe lesion related with pneumonia. The ability of Mycobacterium tuberculosis to replicate intracellularly is directly correlated to the level of lysX expression; in the presence of antimicrobial peptides produced by epithelial cells and macrophages, lysX expression increases significantly. Strains with higher lysX expression show increased levels of intracellular survival in vivo and in vitro and induce more severe lesion related with pneumonia. The ability of Mycobacterium tuberculosis to replicate intracellularly is directly correlated to the level of lysX expression; in the presence of antimicrobial peptides produced by epithelial cells and macrophages, lysX expression increases significantly. Strains with higher lysX expression show increased levels of intracellular survival in vivo and in vitro and induce more severe lesion related with pneumonia. The ability of Mycobacterium tuberculosis to replicate intracellularly is directly correlated to the level of lysX expression
medicine
-
in the presence of antimicrobial peptides produced by epithelial cells and macrophages, lysX expression increases significantly. Strains with higher lysX expression show increased levels of intracellular survival in vivo and in vitro and induce more severe lesion related with pneumonia. The ability of Mycobacterium tuberculosis to replicate intracellularly is directly correlated to the level of lysX expression
-
medicine
Mycobacterium tuberculosis LAM09005186
-
in the presence of antimicrobial peptides produced by epithelial cells and macrophages, lysX expression increases significantly. Strains with higher lysX expression show increased levels of intracellular survival in vivo and in vitro and induce more severe lesion related with pneumonia. The ability of Mycobacterium tuberculosis to replicate intracellularly is directly correlated to the level of lysX expression
-
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