Literature summary for 3.2.2.5 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.

Search for more literature for 3.2.2.5

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment)	Organism
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
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

Protein Variants	Comment	Organism
E226	crystallization data	Homo sapiens
E226Q	crystallization data	Homo sapiens

Inhibitors

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

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	isoform CD38	-

Reaction

Reaction	Comment	Organism	Reaction ID
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

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Release 2023.1 (January 2023)