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Literature summary for 3.2.2.5 extracted from

  • Liu, Q.; Kriksunov, I.A.; Moreau, C.; Graeff, R.; Potter, B.V.; Lee, H.C.; Hao, Q.
    Catalysis-associated conformational changes revealed by human CD38 complexed with a non-hydrolyzable substrate analog (2007), J. Biol. Chem., 282, 24825-24832.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
wild-type and mutant E226Q in complex with inhibitor N1-cyclic inosine diphosphate ribose at 1.7 and 1.176 A resolution, respectively Homo sapiens

Protein Variants

Protein Variants Comment Organism
E226Q crystallization data Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
N1-cyclic inosine diphosphate ribose
-
Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P28907 isoform CD38
-

Reaction

Reaction Comment Organism Reaction ID
NAD+ + H2O = ADP-D-ribose + nicotinamide + H+ residues E146, D147, and W125 work collaboratively to facilitate the formation of the Michaelis complex Homo sapiens

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.26
-
pH 4.5, 20-24°C Homo sapiens N1-cyclic inosine diphosphate ribose