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IUBMB Comments The enzyme participates in an L -lysine biosynthesis pathway in certain species of archaea and bacteria.
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms lysJ , [LysW]-aminoadipate semialdehyde transaminase, more
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[LysW]-aminoadipate semialdehyde transaminase
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lysJ
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an [amino group carrier protein]-C-terminal-gamma-(L-lysyl)-L-glutamate + 2-oxoglutarate = an [amino group carrier protein]-C-terminal-N-(1-carboxy-5-oxopentan-1-yl)-L-glutamine + L-glutamate
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MetaCyc
L-lysine biosynthesis V
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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.
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N2-acetyl-L-lysine + 2-oxoglutarate
N2-acetyl-L-aminoadipate semialdehyde + L-glutamate
Substrates: ping-pong bi-bi mechanism Products: -
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N2-acetyl-L-ornithine + 2-oxoglutarate
(2R)-2-acetamido-5-oxopentanoic acid + L-glutamate
Substrates: - Products: -
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[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
Substrates: - Products: -
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[LysW]-aminoadipate 6-semialdehyde + L-glutamate
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Substrates: - Products: -
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10
N2-acetyl-L-lysine
pH 8.9, 45°C
0.8
N2-Acetyl-L-ornithine
pH 8.9, 45°C
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0.8
N2-acetyl-L-lysine
pH 8.9, 45°C
1
N2-Acetyl-L-ornithine
pH 8.9, 45°C
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0.0786
N2-acetyl-L-lysine
pH 8.9, 45°C
1.266
N2-Acetyl-L-ornithine
pH 8.9, 45°C
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UniProt
brenda
Highest Expressing Human Cell Lines
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Cell Line Links
Gene Links
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physiological function
for the conversion of alpha-aminoadipate to lysine, the amino group of alpha-aminoadipate is modified by attachment to the gamma-carboxyl group of the C-terminal Glu54 of a small protein, LysW. The side chain of alpha-aminoadipate is converted to the lysyl side chain while still attached to LysW, and lysine is subsequently liberated from the LysW-lysine fusion
physiological function
gene product is essential for lysine biosynthesis in Thermus thermophilus
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dimer
2 * 43000, SDS-PAGE, 2 * 43503, calculated from sequence
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expression in Escherichia coli
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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)
brenda
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)
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