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3.2.2.5: NAD+ glycohydrolase

This is an abbreviated version!
For detailed information about NAD+ glycohydrolase, go to the full flat file.

Word Map on EC 3.2.2.5

Reaction

NAD+
+
H2O
=
ADP-D-ribose
 +
nicotinamide
 +
H+

Synonyms

(Streptococcus pyogenes NAD+ glycohydrolase), AA-NADase, Acute lymphoblastic leukemia cells antigen CD38, ADP-ribosyl cyclase/NAD+-glycohydrolase, ADPRC, ADRC, Antigen BP3, beta-NAD+ glycohydrolase, beta-NAD+glycohydrolase, BP-3 alloantigen, cADPr hydrolase, CagL, CD157, CD157 antigen, CD38, CD38 homolog, CD38 like activity, CD38H, co-toxin NADase, Cyclic ADP-ribose hydrolase, diphosphopyridine nucleosidase, diphosphopyridine nucleotidase, DPN hydrolase, DPNase, ecto-NAD-glycohydrolase, HvnA, HvnB, I-19, Lymphocyte differentiation antigen CD38, NACE, NAD glycohydrolase, NAD hydrolase, NAD nucleosidase, NAD(+) nucleosidase, NAD+ catabolizing enzyme, NAD+ glycohydrolase, NAD+-glycohydrolase, NAD+glycohydrolase, NAD-glycohydrolase, NADase, Nga, nicotinamide adenine dinucleotide glycohydrolase, nicotinamide adenine dinucleotide nucleosidase, NIM-R5 antigen, PA0093, PAAR motif containing protein, PFL_6209, pNADase, SmNACE, sNADase, SPN, T10, Tse6

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.2 Hydrolysing N-glycosyl compounds
                3.2.2.5 NAD+ glycohydrolase

Crystallization

Crystallization on EC 3.2.2.5 - NAD+ glycohydrolase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type and mutant enzymes, mixing of 0.001 ml of protein sample with 0.001 ml of precipitant solution containing 0.1 M imidazole, pH 7.5, and 12-24% PEG 4000, X-ray diffraction structure determination and analysis at 1.75-2.18 A resolution
-
CD38 in complex with ribosyl-2'-fluoro-deoxy-adenosine diphosphate or arabinosyl-2'-fluoro-deoxy-adenosine diphosphate ribose, soaking crystals in a solution containing either 5.2 mM inhibitor, and 100 mM MES, pH 6.0, 15% PEG 4000, and 30% glycerol, X-ray diffraction structure determination and analysis at 1.75-2.0 A resolution
wild-type and mutant E226Q in complex with cyclic ADP-ribose at 1.5 A resolution, with cyclic GDP-ribose at 1.68 A, and with NGD+ at 2.1A. Binding of cyclic ADP-ribose or cyclic GDP-ribose induce structural changes in the dipeptide E146D147 of 2.7 A. Resiudue E226 is critical in catalysis and in positioning of cyclic ADP-ribose
-
wild-type and mutant E226Q in complex with inhibitor N1-cyclic inosine diphosphate ribose at 1.7 and 1.176 A resolution, respectively
wild-type and mutant E226Q in complex with NAD+, NGD+, or GDP-ribose. The reaction intermediate is stabilized by polar interactions with the catalytic residue E226 rather than by a covalent linkage
-
to 1.4 A resolution, in complex with binding protein Tsi6
in complex with effector Tni2, to 1.7 A resolution
C-terminal glycohydrolase domain of SPN (residues 191-451) in complex with IFS, vapor diffusion method, using 20%-25% (w/v) PEG 8K and 100 mM Tris-HCl (pH 8.0), at 22°C
-
purified recombinant selenomethionine-labeled enzyme C-terminal domain (residues 193-451) in complex with the full-length inhibitor IFS, sitting drop vapor-diffusion method, mixing of 0.001 ml of protein solution with 0.001 ml of reservoir solution of 20% w/v tacsimate, pH 4.0, and 20% w/v PEG 3350, 22°C, X-ray diffraction structure determination and analysis at 1.70 A resolution, single-wavelength anomalous diffraction, modelling