TAILIEUCHUNG - Báo cáo khoa học: Hydrolysis of diadenosine polyphosphates by nucleotide pyrophosphatases/phosphodiesterases

Diadenosine polyphosphates (ApnAs) act as extracellular signaling molecules in a broad variety of tissues. They were shown to be hydrolyzed by surface-located enzymes in an asymmetric manner, generating AMP and Apn-1 from ApnA. The molecular identity of the enzymes responsible remains analyzed the potential ofNPP1, NPP2, and NPP3, the three members of the ecto-nucleotide pyro-phosphatase/phosphodiesterase family, to hydrolyze the diadenosine polyphosphates diadenosine 5¢,5¢¢¢-P 1 ,P 3 -triphosphate (Ap3A),. | Eur. J. Biochem. 270 2971-2978 2003 FEBS 2003 doi Hydrolysis of diadenosine polyphosphates by nucleotide pyrophosphatases phosphodiesterases Petra Vollmayer1 Timothy Clair2 James W. Goding3 Kimihiko Sano4 Jorg Servos1 and Herbert Zimmermann1 1AK Neurochemie Biozentrum der J. W. Goethe-Universitaet Frankfurt am Main Germany 2Laboratory of Pathology NCI National Institutes of Health Bethesda Maryland USA 3Department of Pathology and Immunology Monash University Alfred Hospital Prahran Victoria Australia 4Department of Pediatrics Kobe University School of Medicine Kobe Japan Diadenosine polyphosphates ApnAs act as extracellular signaling molecules in a broad variety of tissues. They were shown to be hydrolyzed by surface-located enzymes in an asymmetric manner generating AMP and Apn-1 from ApnA. The molecular identity of the enzymes responsible remains unclear. We analyzed the potential of NPP1 NPP2 and NPP3 the three members of the ecto-nucleotide pyro-phosphatase phosphodiesterase family to hydrolyze the diadenosine polyphosphates diadenosine 5 5 -P1 P3-triphosphate Ap3A diadenosine 5 5 -P1 P4-tetraphos-phate Ap4A and diadenosine 5 5 -P1 P5-pentaphosphate Ap5A and the diguanosine polyphosphate diguanosine 5 5 -P1 P4-tetraphosphate Gp4G . Each of the three enzymes hydrolyzed Ap3A Ap4A and Ap5A at comparable rates. Gp4G was hydrolyzed by NPP1 and NPP2 at rates similar to Ap4A but only at half this rate by NPP3. Hydrolysis was asymmetric involving the a b-pyrophos-phate bond. ApnA hydrolysis had a very alkaline pH optimum and was inhibited by EDTA. Michaelis constant Km values for Ap3A were M M and M for NPP1 NPP2 and NPP3 respectively. Our results suggest that NPP1 NPP2 and NPP3 are major enzyme candidates for the hydrolysis of extracellular diadenosine polyphosphates in vertebrate tissues. Keywords diadenosine polyphosphate diguanosine polyphosphate ectonucleotidase nucleotide pyrophosphatase nucleotide phosphodiesterase.

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