ADP-ribose pyrophosphatase
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<StructureSection load='1khz' size='450' side='right' scene='48/488514/Cv/1' caption='ADP-ribose pyrophosphatase dimer complex with methylene ADP-ribose, Cl- (large green) and Mg+2 (small green) ions, [[1khz]]'> | <StructureSection load='1khz' size='450' side='right' scene='48/488514/Cv/1' caption='ADP-ribose pyrophosphatase dimer complex with methylene ADP-ribose, Cl- (large green) and Mg+2 (small green) ions, [[1khz]]'> | ||
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== Function == | == 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.<ref>PMID:11323725</ref> ADPRP belongs to the family of NUDIX hydrolase. | + | '''ADP-ribose pyrophosphatase''' (ADPRP) or '''ADPRase''' 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.<ref>PMID:11323725</ref> ADPRP belongs to the family of NUDIX hydrolase. |
== Structural highlights == | == Structural highlights == | ||
Current revision
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References
- ↑ Gabelli SB, Bianchet MA, Bessman MJ, Amzel LM. The structure of ADP-ribose pyrophosphatase reveals the structural basis for the versatility of the Nudix family. Nat Struct Biol. 2001 May;8(5):467-72. PMID:11323725 doi:10.1038/87647
- ↑ Gabelli SB, Bianchet MA, Ohnishi Y, Ichikawa Y, Bessman MJ, Amzel LM. Mechanism of the Escherichia coli ADP-ribose pyrophosphatase, a Nudix hydrolase. Biochemistry. 2002 Jul 30;41(30):9279-85. PMID:12135348
