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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 enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
alpha-aminoadipate-lysW ligase lysX, LysX, Saci_0754, Tk0278, 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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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-(1,5-dicarboxypentan-1-yl)-L-glutamine
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
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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 + [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
-
-
?
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-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 + [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 + [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
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
-
?
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
-
?
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
-
?
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
-
?
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
-
?
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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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 + [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
-
-
?
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
-
-
?
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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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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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
-
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
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
-
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
-
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
-
lysine biosynthesis. Protection of the amino group of L-2-aminoadipate by conjugation to the carrier protein LysW
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
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
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
physiological function
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
the enzyme is involved in the biosynthesis of lysine through the L-2-aminoadipate pathway
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). LYSX_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
275
0
32028
Swiss-Prot
-
LYSX_SULAC
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
276
0
31712
Swiss-Prot
-
LYSX_SULTO
Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
285
0
33107
Swiss-Prot
-
LYSX_THET8
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
280
0
30718
Swiss-Prot
-
A0A399FBQ0_9DEIN
285
0
30942
TrEMBL
-
A0A2H9TAJ4_9ZZZZ
508
0
58868
TrEMBL
other Location (Reliability: 5)
A0A2K5AS27_9ARCH
320
0
35284
TrEMBL
-
A0A1D8S784_9EURY
291
0
32131
TrEMBL
-
A0A343TF29_9EURY
308
0
33408
TrEMBL
-
A0A2S6SBF0_9PROT
301
0
34822
TrEMBL
-
A0A1S9D0K8_9GAMM
302
0
33357
TrEMBL
-
A0A2G9L7T3_PSESF
528
0
60060
TrEMBL
-
A0A644X8B3_9ZZZZ
286
0
30502
TrEMBL
Mitochondrion (Reliability: 5)
A0A645AG49_9ZZZZ
211
0
22400
TrEMBL
other Location (Reliability: 2)
A0A645CL22_9ZZZZ
213
0
22832
TrEMBL
other Location (Reliability: 2)
A0A5J4QEB8_9ZZZZ
293
0
34523
TrEMBL
other Location (Reliability: 2)
LYSX_MYCTA
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
1172
7
128240
Swiss-Prot
-
LYSX_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
1172
7
128240
Swiss-Prot
-
Q5JFW0_THEKO
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
273
0
30488
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
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
-
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
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
-
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
-
mutant exhibits an apparent substrate preference for glutamate
Y175I/I185Y/N250G/S251F
-
mutant exhibits an apparent substrate preference for glutamate
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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
Mycobacterium tuberculosis LAM09005186
-
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
-
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
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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 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 H37Rv (P9WFU7), Mycobacterium tuberculosis LAM09005186
brenda
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