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Literature summary extracted from

  • Zhu, A.Y.; Zhou, Y.; Khan, S.; Deitsch, K.W.; Hao, Q.; Lin, H.
    Plasmodium falciparum Sir2A preferentially hydrolyzes medium and long chain fatty acyl lysine (2012), ACS Chem. Biol., 7, 155-159 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.286 expressed in Escherichia coli BL21 cells Plasmodium falciparum

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.286 in complex with [histone H3]-N6-myristoyl-L-lysine9, hanging drop vapor diffusion method, using 16% (w/v) PEG 3350, 0.1 M NaF, 7% (v/v) formamide Plasmodium falciparum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.286 0.001
-
 [histone H3]-N6-myristoyl-L-lysine9 Km below 0.001 mM, at pH 8.0 and 37°C Plasmodium falciparum
2.3.1.286 0.0012
-
 [histone H3]-N6-octanoyl-L-lysine9 at pH 8.0 and 37°C Plasmodium falciparum
2.3.1.286 0.008
-
 [histone H3]-N6-butyryl-L-lysine9 at pH 8.0 and 37°C Plasmodium falciparum
2.3.1.286 0.039
-
 [histone H3]-N6-acetyl-L-lysine9 at pH 8.0 and 37°C Plasmodium falciparum

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.286 Plasmodium falciparum Q8IE47
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.286 Ni-affinity column chromatography and Superdex 75 gel filtration Plasmodium falciparum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.286 additional information the enzyme preferentially hydrolyzes medium and long chain fatty acyl lysine. The deacetylase activity of the enzyme is weak Plasmodium falciparum ?
-
 ?
2.3.1.286 [histone H3]-N6-acetyl-L-lysine9 + NAD+ + H2O least efficient substrate Plasmodium falciparum [histone H3]-L-lysine9 + 2''-O-acetyl-ADP-D-ribose + nicotinamide
-
 ?
2.3.1.286 [histone H3]-N6-butyryl-L-lysine9 + NAD+ + H2O
-
 Plasmodium falciparum [histone H3]-L-lysine9 + 2''-O-butyryl-ADP-D-ribose + nicotinamide
-
 ?
2.3.1.286 [histone H3]-N6-myristoyl-L-lysine9 + NAD+ + H2O best substrate Plasmodium falciparum [histone H3]-L-lysine9 + 2''-O-myristoyl-ADP-D-ribose + nicotinamide
-
 ?
2.3.1.286 [histone H3]-N6-octanoyl-L-lysine9 + NAD+ + H2O
-
 Plasmodium falciparum [histone H3]-L-lysine9 + 2''-O-octanoyl-ADP-D-ribose + nicotinamide
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.286 protein lysine deacetylase
-
 Plasmodium falciparum
2.3.1.286 Sir2A
-
 Plasmodium falciparum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.1.286 0.001
-
 [histone H3]-N6-acetyl-L-lysine9 at pH 8.0 and 37°C Plasmodium falciparum
2.3.1.286 0.001
-
 [histone H3]-N6-butyryl-L-lysine9 at pH 8.0 and 37°C Plasmodium falciparum
2.3.1.286 0.001
-
 [histone H3]-N6-octanoyl-L-lysine9 at pH 8.0 and 37°C Plasmodium falciparum
2.3.1.286 0.01
-
 [histone H3]-N6-myristoyl-L-lysine9 Km below 0.001 mM, at pH 8.0 and 37°C Plasmodium falciparum

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.286 NAD+
-
 Plasmodium falciparum

General Information

EC Number General Information Comment Organism
2.3.1.286 physiological function the enzyme regulates the expression of surface antigens to evade the detection by host immune surveillance by removing medium and long chain fatty acyl groups from protein lysine residues Plasmodium falciparum

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.3.1.286 0.026
-
 [histone H3]-N6-acetyl-L-lysine9 at pH 8.0 and 37°C Plasmodium falciparum
2.3.1.286 0.16
-
 [histone H3]-N6-butyryl-L-lysine9 at pH 8.0 and 37°C Plasmodium falciparum
2.3.1.286 0.92
-
 [histone H3]-N6-octanoyl-L-lysine9 at pH 8.0 and 37°C Plasmodium falciparum
2.3.1.286 10
-
 [histone H3]-N6-myristoyl-L-lysine9 Km above 10 1/sec*mM, at pH 8.0 and 37°C Plasmodium falciparum