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Information on EC 2.6.1.118 - [amino group carrier protein]-gamma-(L-lysyl)-L-glutamate aminotransferase and Organism(s) Thermus thermophilus and UniProt Accession Q93R93

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IUBMB Comments
The enzyme participates in an L-lysine biosynthesis pathway in certain species of archaea and bacteria.
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This record set is specific for:
Thermus thermophilus
UNIPROT: Q93R93
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The taxonomic range for the selected organisms is: Thermus thermophilus
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
lysJ, [LysW]-aminoadipate semialdehyde transaminase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
[LysW]-aminoadipate semialdehyde transaminase
-
lysJ
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
2-oxoglutarate:[amino group carrier protein]-C-terminal-gamma-(L-lysyl)-L-glutamate aminotransferase
The enzyme participates in an L-lysine biosynthesis pathway in certain species of archaea and bacteria.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N2-acetyl-L-lysine + 2-oxoglutarate
N2-acetyl-L-aminoadipate semialdehyde + L-glutamate
show the reaction diagram
ping-pong bi-bi mechanism
-
-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
(2R)-2-acetamido-5-oxopentanoic acid + L-glutamate
show the reaction diagram
-
-
-
?
[carrier protein LysW]-C-terminal-N-(1-carboxy-5-oxopentan-1-yl)-L-glutamine + L-glutamate
[carrier protein LysW]-C-terminal-gamma-(L-lysyl)-L-glutamate + 2-oxoglutarate
show the reaction diagram
-
-
-
?
[LysW]-aminoadipate 6-semialdehyde + L-glutamate
?
show the reaction diagram
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10
N2-acetyl-L-lysine
pH 8.9, 45°C
0.8
N2-Acetyl-L-ornithine
pH 8.9, 45°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8
N2-acetyl-L-lysine
pH 8.9, 45°C
1
N2-Acetyl-L-ornithine
pH 8.9, 45°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0786
N2-acetyl-L-lysine
pH 8.9, 45°C
1.266
N2-Acetyl-L-ornithine
pH 8.9, 45°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 43000, SDS-PAGE, 2 * 43503, calculated from sequence
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (Q93R93)
Manually annotated by BRENDA team
Miyazaki, J.; Kobashi, N.; Nishiyama, M.; Yamane, H.
Functional and evolutionary relationship between arginine biosynthesis and prokaryotic lysine biosynthesis through alpha-aminoadipate
J. Bacteriol.
183
5067-5073
2001
Thermus thermophilus (Q93R93)
Manually annotated by BRENDA team