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2.3.1.B43: protein-lysine desuccinylase (NAD+)

This is an abbreviated version!
For detailed information about protein-lysine desuccinylase (NAD+), go to the full flat file.

Word Map on EC 2.3.1.B43

Reaction

NAD+
+
[protein]-N6-acetyl-L-lysine
=
nicotinamide
 +
[protein]-L-lysine
 +
2'-O-acetyl-ADP-ribose

Synonyms

CobB, CobB Sir2 protein, histone desuccinylase, hSIRT5, hSIRT6, lysine desuccinylase, mitochondrial NAD+-dependent lysine deacylase, NAD+ dependent deacetylase, NAD+-dependent protein deacetylase, NAD+-dependent protein deacylase, NAD+-dependent sirtuin deacetylase, nicotinamide adenine dinucleotide-dependent protein deacetylase, Sir2Af1, SIRT5, SIRT5iso1, SIRT5iso2, SIRT5iso3, SIRT5iso4, sirtuin 5, sirtuin 5 deacylase, sirtuin 5 lysine deacylase, sirtuin deacylase, sirtuin-5, zSIRT5

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.B43 protein-lysine desuccinylase (NAD+)

Crystallization

Crystallization on EC 2.3.1.B43 - protein-lysine desuccinylase (NAD+)

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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
purified recombinant detagged enzyme in complex with peptide inhibitors 2 and 15, sitting drop vapor diffusion method, mixing of 10 mg/ml protein with 1 mM inhibitor, crystallization in 0.002 ml of reservoir solution containing 0.1 M HEPES, pH 7.5, and 20% PEG 3350, 20°C, 2-4 days, X-ray diffraction structure determination and analysis at 2.4 A resolution, molecular replacement with search model PDB 4UTV and modeling
crystals of native and selenomethionine-derivatized cobB are grown at room temperature using the hanging-drop, vapor-diffusion method. The crystal structure of the Escherichia coli cobB core domain (residues 40–274) in complex with an 11-residue peptide containing residues 12–19 of histone H4 and acetylated at lysine 16 is determined by a combination of Zn2+ and Se multiwavelength anomalous diffraction to 1.96 A resolution
crystal structure of Sirt5 in complex with a thioacetyl peptide is obtained, The corresponding acetyl peptide could not be crystallized with Sirt5
crystal structure of Sirt5 in complex with fluor-de-Lys peptide and resveratrol and crystal structure of Sirt5 in complex with fluor-de-Lys peptide and piceatannol
crystal structures of a binary complex of SIRT5 with an H3K9 succinyl peptide and a binary complex of SIRT5 with a bicyclic intermediate obtained by incubating SIRT5-H3K9 thiosuccinyl peptide co-crystals with NAD+
hanging drop vapor diffusion method at 18°C. X-ray crystal structures of the ternary complex of SIRT5 bound to a peptide substrate and carba-NAD+ (an unreactive NAD+ analogue)
hanging drop vapor-diffusion method at 20°C. Crystal structures of SIRT5 in complex with ADP-ribose, and crystal structures of SIRT5 bound to suramin
purified recombinant enzyme SIRT5 in complex with succinylated histones, crystals of Sirt5-H4K122su and Sirt5-H2AK95su complexes are obtained from 0.1 M sodium cacodylate, pH 5.5, and 25% w/v PEG 4000 at 22°C. Sirt5-H4K91su complex is crystallized from 0.1 M Bis-Tris, pH 5.5, and 25% w/v PEG 3350, and Sirt5-H2BK120su complex is grown in 0.2 M sodium acetate trihydrate, 0.1 M sodium cacodylate trihydrate, pH 6.5, and 30% w/v PEG 8000, X-ray diffraction structure determination and analysis at 1.70-2.30 A resolution, molecular replacement using the structures PDB ID 3RIY as a searching model