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Literature summary extracted from

  • Liu, Q.; Kriksunov, I.A.; Graeff, R.; Munshi, C.; Lee, H.C.; Hao, Q.
    Structural basis for the mechanistic understanding of human CD38-controlled multiple catalysis (2006), J. Biol. Chem., 281, 32861-32869.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.2.5 enzymatic domain of CD38 Homo sapiens
3.2.2.5 expression of extramembrane domain in Saccharomyces cerevisiae Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.2.5 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 Homo sapiens
3.2.2.5 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 Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.2.2.5 E226 crystallization data Homo sapiens
3.2.2.5 E226Q crystallization data Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.2.5 ADP-ribose product inhibition Homo sapiens
3.2.2.5 GDP-ribose
-
 Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.2.2.5 Homo sapiens
-
 isoform CD38
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.2.5 NAD+ + H2O = ADP-D-ribose + nicotinamide + H+ the polar interactions between E226 and the substrate 2',3'-OH groups are essential for initiating catalysis. S193 has a regulatory role during catalysis and is likely to be involved in intermediate stabilization Homo sapiens
a