Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Chang, J.H.; Kim, H.C.; Hwang, K.Y.; Lee, J.W.; Jackson, S.P.; Bell, S.D.; Cho, Y.
    Structural basis for the NAD-dependent deacetylase mechanism of Sir2 (2002), J. Biol. Chem., 277, 34489-34498.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.B43 hanging drop vapor diffusion method at 4°C, crystal structure of wild-type enzyme, mutant enzyme S24A, mutant enzyme H80N, mutant enzyme F159A, and triple Sir2 mutant (D102G/F159A/R170A) Archaeoglobus fulgidus

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.B43 D101N the decreased NAD-dependent deacetylase activity for the mutant proteins is at least partly due to reduced binding affinities for NAD+ Archaeoglobus fulgidus
2.3.1.B43 F159A the Km value of the mutant enzyme is twice that of wild type enzyme, whereas the kcat is 5fold less. In the F159A mutant, two water molecules occupy the position of the Phe159 ring Archaeoglobus fulgidus
2.3.1.B43 H80N mutant retains about 60% of the NAD binding ability of wild type Sir2 Archaeoglobus fulgidus
2.3.1.B43 S24A the decreased NAD-dependent deacetylase activity for the mutant proteins is at least partly due to reduced binding affinities for NAD+ Archaeoglobus fulgidus

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.B43 Archaeoglobus fulgidus O28597
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.B43
-
 Archaeoglobus fulgidus

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.B43 NAD+ + [protein]-N6-acetyl-L-lysine = nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose crystallographic evidence is provided that 2'-O-acetyl ADP-ribose is a final product in the Sir2 reaction. A revised mechanism for catalysis based on the structural and functional characterization of Sir2 mutants is proposed. In this mechanism, the activation of the 2'-OH of nicotinamide ribose by His-116 is essential for the hydrolysis of the acetyl groups from N-acetyl lysine. The conserved Ser-24 and Asp-101 participate in the stabilization of local structure for NAD binding rather than direct involvement in catalysis Archaeoglobus fulgidus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.B43 NAD+ + [bovine serum albumin]-N6-acetyl-L-lysine crystallographic evidence is provided that 2'-O-acetyl ADP-ribose is a final product in the Sir2 reaction. A revised mechanism for catalysis based on the structural and functional characterization of Sir2 mutants is proposed. In this mechanism, the activation of the 2'-OH of nicotinamide ribose by His-116 is essential for the hydrolysis of the acetyl groups from N-acetyl lysine. The conserved Ser-24 and Asp-101 participate in the stabilization of local structure for NAD binding rather than direct involvement in catalysis Archaeoglobus fulgidus nicotinamide + [bovine serum albumin]-L-lysine + 2'-O-acetyl-ADP-ribose
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.B43 50
-
 assay at Archaeoglobus fulgidus