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Information on EC 6.3.2.43 - [amino group carrier protein]-L-2-aminoadipate ligase
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6.3.2.43 [amino group carrier protein]-L-2-aminoadipate ligaseIUBMB Comments
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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The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
Synonyms
alpha-aminoadipate-lysW ligase lysX, LysX, More, RimK-related lysine biosynthesis protein, Saci_0754, Tk0278, TkLysX/ArgX, TtLysX, [lysine-biosynthesis-protein LysW]-C-terminal-L-glutamate:L-2-aminoadipate ligase (ADP-forming), [lysine-biosynthesis-protein LysW]-L-2-aminoadipate ligase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
LysX
Saci_0754
TtLysX
[lysine-biosynthesis-protein LysW]-C-terminal-L-glutamate:L-2-aminoadipate ligase (ADP-forming)
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-
-
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[lysine-biosynthesis-protein LysW]-L-2-aminoadipate ligase
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additional information
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + an [amino group carrier protein]-C-terminal-L-glutamate + L-2-aminoadipate = ADP + phosphate + an [amino group carrier protein]-C-terminal-N-(1,4-dicarboxybutyl)-L-glutamine
ATP + an [amino group carrier protein]-C-terminal-L-glutamate + L-2-aminoadipate = ADP + phosphate + an [amino group carrier protein]-C-terminal-N-(1,4-dicarboxybutyl)-L-glutamine
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ATP + an [amino group carrier protein]-C-terminal-L-glutamate + L-2-aminoadipate = ADP + phosphate + an [amino group carrier protein]-C-terminal-N-(1,4-dicarboxybutyl)-L-glutamine
substrate-recognition mechanism of bifunctional TkLysX/ArgX
ATP + an [amino group carrier protein]-C-terminal-L-glutamate + L-2-aminoadipate = ADP + phosphate + an [amino group carrier protein]-C-terminal-N-(1,4-dicarboxybutyl)-L-glutamine
substrate-recognition mechanism of bifunctional TkLysX/ArgX
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ATP + an [amino group carrier protein]-C-terminal-L-glutamate + L-2-aminoadipate = ADP + phosphate + an [amino group carrier protein]-C-terminal-N-(1,4-dicarboxybutyl)-L-glutamine
substrate-recognition mechanism of bifunctional TkLysX/ArgX
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SYSTEMATIC NAME
IUBMB Comments
[amino group carrier protein]-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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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 + an [amino group carrier protein]-C-terminal-L-glutamate + L-2-aminoadipate
ADP + phosphate + an [amino group carrier protein]-C-terminal-N-(1,5-dicarboxypentan-1-yl)-L-glutamine
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
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-
-
?
ATP + [LysW mutant E42R]-C-terminal-L-glutamate + L-2-aminoadipate
ADP + phosphate + [LysW mutant E42R]-C-terminal-N-(1,5-dicarboxypentan-1-yl)-L-glutamine
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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
ATP + [LysW]-C-terminal-L-glutamate + L-2-aminoadipate
ADP + phosphate + [LysW]-C-terminal-N-(1,4-dicarboxybutan-1-yl)-L-glutamine
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-
-
?
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 + an [amino group carrier protein]-C-terminal-L-glutamate + L-2-aminoadipate
ADP + phosphate + an [amino group carrier protein]-C-terminal-N-(1,5-dicarboxypentan-1-yl)-L-glutamine
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-
-
?
ATP + an [amino group carrier protein]-C-terminal-L-glutamate + L-2-aminoadipate
ADP + phosphate + an [amino group carrier protein]-C-terminal-N-(1,5-dicarboxypentan-1-yl)-L-glutamine
the amino-group carrier protein is LysW. Determination of the crystal structure of the LysX family protein from Thermococcus kodakarensis, which catalyzes the conjugation of LysW with either alpha-aminoadipate (AAA) or glutamate, in a complex with LysW-gamma-AAA. Substrate binding structure, overview. Residues Thr196, Asn250, and Ala251 are involved in the recognition of the delta-carboxyl group of AAA
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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-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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-
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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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?
additional information
?
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purified recombinant TK0278 recognizes alpha-aminoadipate (AAA) and glutamate as substrates and ligated both compounds with TK0279, an amino group carrier protein LysW in this microorganism, in an ATP-dependent manner
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additional information
?
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purified recombinant TK0278 recognizes alpha-aminoadipate (AAA) and glutamate as substrates and ligated both compounds with TK0279, an amino group carrier protein LysW in this microorganism, in an ATP-dependent manner
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-
additional information
?
-
purified recombinant TK0278 recognizes alpha-aminoadipate (AAA) and glutamate as substrates and ligated both compounds with TK0279, an amino group carrier protein LysW in this microorganism, in an ATP-dependent manner
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NATURAL SUBSTRATE
NATURAL 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 + an [amino group carrier protein]-C-terminal-L-glutamate + L-2-aminoadipate
ADP + phosphate + an [amino group carrier protein]-C-terminal-N-(1,5-dicarboxypentan-1-yl)-L-glutamine
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-
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?
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
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-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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-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
0.021
substrate L-2-aminoadipate, pH not specified in the publication, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Pyrococcus kodakaraensis strain KOD1
UniProt
brenda
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Pyrococcus kodakaraensis strain KOD1
UniProt
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
proposal of a mechanism for substrate recognition and its relationship with molecular evolution among LysX family proteins, which have different substrate specificities
malfunction
metabolism
the enzyme is part of the lysine biosynthetic pathway in Thermococcus kodakarensis, overview. The gene cluster for lysine biosynthetic genes through AAA produces lysine with a LysW-mediated system. In this cluster, TK0279, TK0278, TK0276, TK0277, TK0275, and TK0274 are expected to be responsible for the conversion process from AAA to lysine through the LysW system as LysW-gamma-AAA synthetase, LysW-gamma-AAA kinase, LysW-gamma-AAA semialdehyde dehydrogenase, LysW-gamma-lysine aminotransferase, and LysW-gamma-lysine carboxypeptidase, respectively. LysW-gamma-AAA thus synthesized is transferred to subsequent biosynthetic enzymes to be converted to LysW-gamma-lysine by phosphorylation, reduction, and amination steps. In the final step, LysW-gamma-lysine is recognized by LysK, a carboxypeptidase, resulting in the release of lysine. The lysine biosynthetic enzymes of Thermococcus kodakarensis convert AAA/Glu to lysine/ornithine
physiological function
additional information
the modification by TK0278 and successive phosphorylation by TK0276 occurr at the C-terminus of TkLysW. Residue Tyr175 in TkLysX/ArgX plays a critical role in the recognition of glutamate. Residues Thr196, Asn250, and Ala251 are involved in the recognition of the delta-carboxyl group of AAA. The Tyr residue at strand beta10, the Tyr residue at strand beta11, and the Thr residue at the large loop as the additional key residues that define substrate specificity in LysX family proteins
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
lysine biosynthesis. Protection of the amino group of L-2-aminoadipate by conjugation to the carrier protein LysW
physiological function
the enzyme is involved in biosynthesis of lysine in Thermus thermophilus
physiological function
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the enzyme is involved in the biosynthesis of lysine through the L-2-aminoadipate pathway
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
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
enzyme LysX recognizes alpha-aminoadipate (AAA) as a substrate, structural basis for the bifunctionality of the LysX family protein from Thermococcus kodakarensis. Purified recombinant TK0278 recognizes alpha-aminoadipate (AAA) and glutamate as substrates and ligated both compounds with TK0279, an amino group carrier protein LysW in this microorganism, in an ATP-dependent manner. Proposal of a mechanism for substrate recognition
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
-
physiological function
-
enzyme LysX recognizes alpha-aminoadipate (AAA) as a substrate, structural basis for the bifunctionality of the LysX family protein from Thermococcus kodakarensis. Purified recombinant TK0278 recognizes alpha-aminoadipate (AAA) and glutamate as substrates and ligated both compounds with TK0279, an amino group carrier protein LysW in this microorganism, in an ATP-dependent manner. Proposal of a mechanism for substrate recognition
-
physiological function
-
lysine biosynthesis. Protection of the amino group of L-2-aminoadipate by conjugation to the carrier protein LysW
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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
-
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
-
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
-
enzyme LysX recognizes alpha-aminoadipate (AAA) as a substrate, structural basis for the bifunctionality of the LysX family protein from Thermococcus kodakarensis. Purified recombinant TK0278 recognizes alpha-aminoadipate (AAA) and glutamate as substrates and ligated both compounds with TK0279, an amino group carrier protein LysW in this microorganism, in an ATP-dependent manner. Proposal of a mechanism for substrate recognition
-
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
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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Show AA Sequence and Transmembrane Helices (118 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
tetramer
the crystal asymmetric unit contains two TkLysX/ArgX tetramers, two intact TkLysW monomers each with one zinc atom, four partial TkLysW, eight ADP molecules, five phosphate ions, two sulfate ions, nine magnesium atoms, one free AAA molecule, and 628 water molecules, binding structure, overview
tetramer
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the crystal asymmetric unit contains two TkLysX/ArgX tetramers, two intact TkLysW monomers each with one zinc atom, four partial TkLysW, eight ADP molecules, five phosphate ions, two sulfate ions, nine magnesium atoms, one free AAA molecule, and 628 water molecules, binding structure, overview
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tetramer
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the crystal asymmetric unit contains two TkLysX/ArgX tetramers, two intact TkLysW monomers each with one zinc atom, four partial TkLysW, eight ADP molecules, five phosphate ions, two sulfate ions, nine magnesium atoms, one free AAA molecule, and 628 water molecules, binding structure, overview
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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
purified recombinant nontagged enzyme TkLysX/ArgX in complex with [LysW]-C-terminal-N-(1,5-dicarboxypentan-1-yl)-L-glutamine ((TkLysX/ArgXx02LysW-gamma-AAA)), which corresponds to the structure of the post-reaction state of TkLysX/Arg, hanging drop vapor diffusion method, mixing of 7.5 mg/ml protein and 2.5 mg/ml TkLysW in 10 mM AMP-PNP, 10 mM AAA, or 50 mM glutamate and 10 mM MgSO4 with precipitation solution containing containing 20% v/v 2-methyl-2,4-pentanediol, 6.6% w/v PEG-3350, 0.066 M imidazole, pH 6.5, and 0.132 M ammonium sulfate, 20°C, X-ray diffraction structure determination and analysis at 2.18 A resolution. Molecular replacement. The asymmetric unit contains two TkLysX/ArgX tetramers, two intact TkLysW monomers each with one zinc atom, four partial TkLysW, eight ADP molecules, five phosphate ions, two sulfate ions, nine magnesium atoms, one free AAA molecule, and 628 water molecules. Good crystals containing TkLysW-gamma-Glu are not obtained
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N264G/T265T
I185Y
site-directed mutagenesis, the mutant exhibits an apparent substrate preference for glutamate
N250G
site-directed mutagenesis, the mutant exhibits an apparent substrate preference for glutamate
S251F
site-directed mutagenesis, the mutant exhibits an apparent substrate preference for glutamate
Y175I
site-directed mutagenesis, the mutant exhibits an apparent substrate preference for glutamate
Y175I/I185Y/N250G/S251F
mutant exhibits an apparent substrate preference for glutamate
I185Y
-
site-directed mutagenesis, the mutant exhibits an apparent substrate preference for glutamate
-
S251F
-
site-directed mutagenesis, the mutant exhibits an apparent substrate preference for glutamate
-
Y175I
-
site-directed mutagenesis, the mutant exhibits an apparent substrate preference for glutamate
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Y175I/I185Y/N250G/S251F
-
mutant exhibits an apparent substrate preference for glutamate
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I185Y
-
site-directed mutagenesis, the mutant exhibits an apparent substrate preference for glutamate
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S251F
-
site-directed mutagenesis, the mutant exhibits an apparent substrate preference for glutamate
-
Y175I
-
site-directed mutagenesis, the mutant exhibits an apparent substrate preference for glutamate
-
Y175I/I185Y/N250G/S251F
-
mutant exhibits an apparent substrate preference for glutamate
-
additional information
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
-
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
-
additional information
the N250G/A251F mutant is not produced as a soluble protein
additional information
-
the N250G/A251F mutant is not produced as a soluble protein
-
additional information
-
the N250G/A251F mutant is not produced as a soluble protein
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21-CodonPlus (DE3)-RIL by heat treatment at 80°C for 20 min and nickel affinity chromatography. Recombinant nontagged enzyme from Escherichia coli strain BL21(DE3) by heat treatment at 80°C for 20 min, ammonium sulfate fractionation, hydrophobic interaction chromatography, ultrafiltration, and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene TK0278, recombinant expression of C-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21-CodonPlus (DE3)-RIL, recombinant expression of nontagged enzyme in Escherichia coli strain BL21(DE3)
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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
Mycobacterium tuberculosis LAM09005186
-
-
in the presence of antimicrobial peptides, lysX expression increases significantly
-
-
in the presence of antimicrobial peptides, lysX expression increases significantly
-
-
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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
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
-
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
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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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vassylyeva, M.N.; Sakai, H.; Matsuura, T.; Sekine, S.; Nishiyama, M.; Terada, T.; Shirouzu, M.; Kuramitsu, S.; Vassylyev, D.G.; Yokoyama, S.
Cloning, expression, purification, crystallization and initial crystallographic analysis of the lysine-biosynthesis LysX protein from Thermus thermophilus HB8
Acta Crystallogr. Sect. D
59
1651-1652
2003
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
brenda
Sakai, H.; Vassylyeva, M.N.; Matsuura, T.; Sekine, S.; Gotoh, K.; Nishiyama, M.; Terada, T.; Shirouzu, M.; Kuramitsu, S.; Vassylyev, D.G.; Yokoyama, S.
Crystal structure of a lysine biosynthesis enzyme, LysX, from Thermus thermophilus HB8
J. Mol. Biol.
332
729-740
2003
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
brenda
Horie, A.; Tomita, T.; Saiki, A.; Kono, H.; Taka, H.; Mineki, R.; Fujimura, T.; Nishiyama, C.; Kuzuyama, T.; Nishiyama, M.
Discovery of proteinaceous N-modification in lysine biosynthesis of Thermus thermophilus
Nat. Chem. Biol.
5
673-679
2009
Thermus thermophilus (Q5SH23)
brenda
Ouchi, T.; Tomita, T.; Horie, A.; Yoshida, A.; Takahashi, K.; Nishida, H.; Lassak, K.; Taka, H.; Mineki, R.; Fujimura, T.; Kosono, S.; Nishiyama, C.; Masui, R.; Kuramitsu, S.; Albers, S.V.; Kuzuyama, T.; Nishiyama, M.
Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus
Nat. Chem. Biol.
9
277-283
2013
Sulfolobus acidocaldarius (Q4JAP9), Thermus thermophilus (Q5SH23), Sulfolobus acidocaldarius DSM 639 (Q4JAP9), Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q5SH23)
brenda
Yoshida, A.; Tomita, T.; Atomi, H.; Kuzuyama, T.; Nishiyama, M.
Lysine biosynthesis of Thermococcus kodakarensis with the capacity to function as an ornithine biosynthetic system
J. Biol. Chem.
291
21630-21643
2016
Thermococcus kodakarensis (Q5JFW0), Thermococcus kodakarensis JCM 12380 (Q5JFW0), Thermococcus kodakarensis ATCC BAA-918 (Q5JFW0)
brenda
Montoya-Rosales, A.; Provvedi, R.; Torres-Juarez, F.; Enciso-Moreno, J.; Hernandez-Pando, R.; Manganelli, R.; Rivas-Santiago, B.
lysX gene is differentially expressed among Mycobacterium tuberculosis strains with different levels of virulence
Tuberculosis
106
106-117
2017
Mycobacterium tuberculosis, Mycobacterium tuberculosis (A5U2Z7), Mycobacterium tuberculosis (P9WFU7), Mycobacterium tuberculosis LAM09005186, Mycobacterium tuberculosis H37Rv (P9WFU7)
brenda
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