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.
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 |
|