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Article

Structural insights into the Thermus thermophilus ADP-ribose pyrophosphatase mechanism via crystal structures with the bound substrate and metal.

The Journal of biological chemistry - 27 Aug 2004

Yoshiba Sachiko, Ooga Takushi, Nakagawa Noriko, Shibata Takehiko, Inoue Yorinao, Yokoyama Shigeyuki, Kuramitsu Seiki, Masui Ryoji

Abstract excerpt

ADP-ribose pyrophosphatase (ADPRase) catalyzes the divalent metal ion-dependent hydrolysis of ADP-ribose to ribose 5'-phosphate and AMP. This enzyme plays a key role in regulating the intracellular ADP-ribose levels, and prevents nonenzymatic ADP-ribosylation. To elucidate the pyrophosphatase hydrolysis mechanism employed by this enzyme, structural changes occurring on binding of substrate, metal and product were...

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PMID: 15210687
DOI: 10.1074/jbc.M403817200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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