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Information on EC 2.3.1.B43 - protein-lysine desuccinylase (NAD+) and Organism(s) Archaeoglobus fulgidus and UniProt Accession O28597

for references in articles please use BRENDA:EC2.3.1.B43
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Archaeoglobus fulgidus
UNIPROT: O28597
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The taxonomic range for the selected organisms is: Archaeoglobus fulgidus
The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria
Synonyms
sirt5, sirtuin 5, nad+-dependent protein deacetylase, nad+ dependent deacetylase, nicotinamide adenine dinucleotide-dependent protein deacetylase, sirtuin deacylase, histone desuccinylase, nad+-dependent protein deacylase, lysine desuccinylase, nad+-dependent sirtuin deacetylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NAD+ + [protein]-N6-acetyl-L-lysine = nicotinamide + [protein]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
NAD+ + KGLGKGGA(N6-acetyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-acetyl-ADP-ribose
show the reaction diagram
the rate of desuccinylation is about 5fold faster than the rate of deacetylation
-
-
?
NAD+ + KGLGKGGA(N6-butyryl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-butyryl-ADP-ribose
show the reaction diagram
the rate of desuccinylation is about 10fold faster than the rate of debutyrylation
-
-
?
NAD+ + KGLGKGGA(N6-propionyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-propionyl-ADP-ribose
show the reaction diagram
the rate of desuccinylation is about 5fold faster than the rate of depropionylation
-
-
?
NAD+ + KGLGKGGA(N6-succinyl)KRHRKW
nicotinamide + KGLGKGGAKRHRKW + 2'-O-succinyl-ADP-ribose
show the reaction diagram
the rate of desuccinylation is about 5fold faster than the rate of deacetylation
-
-
?
NAD+ + [bovine serum albumin]-N6-acetyl-L-lysine
nicotinamide + [bovine serum albumin]-L-lysine + 2'-O-acetyl-ADP-ribose
show the reaction diagram
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
-
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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)
vapor diffusion at 20°C, crystal structure of the enzyme bound to KGLGKGGA(N6-succinyl)KRHRKW
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D101N
the decreased NAD-dependent deacetylase activity for the mutant proteins is at least partly due to reduced binding affinities for NAD+
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
H80N
mutant retains about 60% of the NAD binding ability of wild type Sir2
S24A
the decreased NAD-dependent deacetylase activity for the mutant proteins is at least partly due to reduced binding affinities for NAD+
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
J. Biol. Chem.
277
34489-34498
2002
Archaeoglobus fulgidus (O28597)
Manually annotated by BRENDA team
Ringel, A.E.; Roman, C.; Wolberger, C.
Alternate deacylating specificities of the archaeal sirtuins Sir2Af1 and Sir2Af2
Protein Sci.
23
1686-1697
2014
Escherichia coli, Archaeoglobus fulgidus (O28597), Archaeoglobus fulgidus
Manually annotated by BRENDA team