ADP-ribose pyrophosphatase
From Proteopedia
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| - | '''ADP-ribose pyrophosphatase''' (ADPRP) catalyzes the reaction which converts ADP-ribose to AMP and D-ribose 5-phosphate. ADPRP contains Mg+2 | + | |
| + | == Function == | ||
| + | |||
| + | '''ADP-ribose pyrophosphatase''' (ADPRP) catalyzes the reaction which converts ADP-ribose to AMP and D-ribose 5-phosphate. ADPRP contains Mg+2 ion. ADPRP regulates the level of ADP-ribose (ADPR) in the cell. Excess of ADPR can inactivate proteins with nucleotide-binding site by binding to them. | ||
| + | |||
| + | == Structural highlights == | ||
| + | |||
| + | ADPRP contains two domains: the N-terminal domain responsible for dimer stabilization and the C-terminal which contains the active site. The C-terminal domain contains the Nudix (Nucleoside Diphosphate linked to X) sequence which is typical to pyrophosphatases and binds the metal ion. Residues from both monomers of ADPRP participate in the active site. | ||
==3D structures of ADP-ribose pyrophosphatase== | ==3D structures of ADP-ribose pyrophosphatase== | ||
Revision as of 10:13, 28 October 2015
Function
ADP-ribose pyrophosphatase (ADPRP) catalyzes the reaction which converts ADP-ribose to AMP and D-ribose 5-phosphate. ADPRP contains Mg+2 ion. ADPRP regulates the level of ADP-ribose (ADPR) in the cell. Excess of ADPR can inactivate proteins with nucleotide-binding site by binding to them.
Structural highlights
ADPRP contains two domains: the N-terminal domain responsible for dimer stabilization and the C-terminal which contains the active site. The C-terminal domain contains the Nudix (Nucleoside Diphosphate linked to X) sequence which is typical to pyrophosphatases and binds the metal ion. Residues from both monomers of ADPRP participate in the active site.
3D structures of ADP-ribose pyrophosphatase
Updated on 28-October-2015
