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Literature summary for 2.3.1.306 extracted from

  • Schmidt, H.; Bode, R.; Birnbaum, D.
    Lysine degradation in Candida maltosa occurrence of a novel enzyme, acetyl-CoA L-lysine N-acetyltransferase (1988), Arch. Microbiol., 150, 215-218 .
No PubMed abstract available
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.33
-
 acetyl-CoA pH 8.1, 37°C Candida maltosa
10
-
 L-lysine pH 8.1, 37°C Candida maltosa

Organism

Organism UniProt Comment Textmining
Candida maltosa
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + 5-hydroxy-DL-lysine
-
 Candida maltosa CoA + N6-acetyl-5-hydroxy-DL-lysine
-
 ?
acetyl-CoA + L-arginine 16% of the activity with L-lysine Candida maltosa CoA + ?
-
 ?
acetyl-CoA + L-lysine
-
 Candida maltosa CoA + N6-acetyl-L-lysine
-
 ?
acetyl-CoA + L-thialysine 69% of the activity with L-lysine Candida maltosa CoA + N6-acetyl-L-thialysine
-
 ?
acetyl-CoA + spermidine 15% of the activity with L-lysine Candida maltosa CoA + ?
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.1
-
-
 Candida maltosa

Expression

Organism Comment Expression
Candida maltosa expression is strongly induced in cells grown on L-lysine as sole carbon source up

General Information

General Information Comment Organism
metabolism the enzyme is specific for both acetyl-CoA and L-lysine Candida maltosa