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Article

Structural basis for enzymatic evolution from a dedicated ADP-ribosyl cyclase to a multifunctional NAD hydrolase.

The Journal of biological chemistry - 2 Oct 2009

Liu Qun, Graeff Richard, Kriksunov Irina A, Jiang Hong, Zhang Bo, Oppenheimer Norman, Lin Hening, Potter Barry V L, Lee Hon Cheung, Hao Quan

Abstract excerpt

Cyclic ADP-ribose (cADPR) is a universal calcium messenger molecule that regulates many physiological processes. The production and degradation of cADPR are catalyzed by a family of related enzymes, including the ADP-ribosyl cyclase from Aplysia california (ADPRAC) and CD38 from human. Although ADPRC and CD38 share a common evolutionary ancestor, their enzymatic functions toward NAD and cADPR homeostasis have...

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PMID: 19640846
DOI: 10.1074/jbc.M109.031005
PMCID: PMC2785692

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