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IUBMB Comments The enzyme catalyses the first step of an L -lysine degradation pathway found in many fungal species. The enzyme is specific for acetyl-CoA as the acetyl donor. cf . EC 2.3.1.32 , lysine N -acetyltransferase.
Synonyms
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lysine N6-acetyltransferase
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ambiguous
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acetyl-CoA + L-lysine = CoA + N6-acetyl-L-lysine
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MetaCyc
L-lysine degradation III
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acetyl-CoA:L-lysine N6-acetyltransferase
The enzyme catalyses the first step of an L-lysine degradation pathway found in many fungal species. The enzyme is specific for acetyl-CoA as the acetyl donor. cf. EC 2.3.1.32, lysine N-acetyltransferase.
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acetyl-CoA + 5-hydroxy-DL-lysine
CoA + N6-acetyl-5-hydroxy-DL-lysine
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Substrates: -
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acetyl-CoA + 5-hydroxy-L-lysine
CoA + N6-acetyl-5-hydroxy-L-lysine
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Substrates: -
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acetyl-CoA + L-arginine
CoA + ?
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Substrates: 16% of the activity with L-lysine
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acetyl-CoA + L-lysine
CoA + N6-acetyl-L-lysine
acetyl-CoA + L-thialysine
CoA + N6-acetyl-L-thialysine
acetyl-CoA + spermidine
CoA + ?
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Substrates: 15% of the activity with L-lysine
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acetyl-CoA + L-lysine
CoA + N6-acetyl-L-lysine
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Substrates: -
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acetyl-CoA + L-lysine
CoA + N6-acetyl-L-lysine
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Substrates: -
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acetyl-CoA + L-lysine
CoA + N6-acetyl-L-lysine
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Substrates: -
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acetyl-CoA + L-thialysine
CoA + N6-acetyl-L-thialysine
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Substrates: 69% of the activity with L-lysine
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acetyl-CoA + L-thialysine
CoA + N6-acetyl-L-thialysine
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Substrates: -
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acetyl-CoA + L-lysine
CoA + N6-acetyl-L-lysine
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Substrates: -
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2.8
5-hydroxy-L-lysine
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pH 8.5, 30°C
100
L-thialysine
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pH 8.5, 30°C
0.33
acetyl-CoA
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pH 8.1, 37°C
0.8
acetyl-CoA
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pH 8.5, 30°C
5.8
L-lysine
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pH 8.5, 30°C
10
L-lysine
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pH 8.1, 37°C
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8.5
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assay at
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UniProt
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UniProt
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Highest Expressing Human Cell Lines
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Gene Links
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metabolism
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the enzyme is specific for both acetyl-CoA and L-lysine
physiological function
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L-lysine is degraded in Candida tropicalis via N6-acetyllysine, 5-acetamidovalerate and 5-aminovalerate, both nitrogen atoms being removed by transamination
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LYC1_YARLI
Yarrowia lipolytica (strain CLIB 122 / E 150)
392
0
43935
Swiss-Prot
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monomer
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1 * 52000, SDS-PAGE
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x * 43526, calculated from sequence
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x * 43526, calculated from sequence
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-20°C, crude dialysed extract, stable for months
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expression in Saccharomyces cerevisiae
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expression is induced after growth in defined medium on L-lysine as sole nitrogen source
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expression is strongly induced in cells grown on L-lysine as sole carbon source
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highest expression levels are observed when 5-aminovalerate and lysine are used as a nitrogen source
strongly induced in cells grown on L-lysine as sole carbon source
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highest expression levels are observed when 5-aminovalerate and lysine are used as a nitrogen source
highest expression levels are observed when 5-aminovalerate and lysine are used as a nitrogen source
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Schmidt, H.; Bode, R.; Birnbaum, D.
Lysine degradation in Candida maltosa occurrence of a novel enzyme, acetyl-CoA L-lysine N-acetyltransferase
Arch. Microbiol.
150
215-218
1988
Candida maltosa
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Bode, R.; Thurau, A.M.; Schmidt, H.
Characterization of acetyl-CoA L-lysine N6-acetyltransferase, which catalyses the first step of carbon catabolism from lysine in Saccharomyces cerevisiae
Arch. Microbiol.
160
397-400
1993
Saccharomyces cerevisiae
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Beckerich, J.; Lambert, M.; Gaillardin, C.
LYC1 is the structural gene for lysine N-6-acetyl transferase in yeast
Curr. Genet.
25
24-29
1994
Yarrowia lipolytica (P41929), Yarrowia lipolytica CLIB 122 (P41929)
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Large, P.J.; Robertson, A.
The route of lysine breakdown in Candida tropicalis
FEMS Microbiol. Lett.
66
209-213
1991
Candida tropicalis
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