Non-Oxidation–Reduction Reactions of Pyridine Nucleotides

Pekala, Phillip H.; Anderson, Bruce M.

doi:10.1016/b978-0-12-244750-1.50019-1

The Pyridine Nucleotide Coenzymes 1982

DOI: 10.1016/b978-0-12-244750-1.50019-1

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Non-Oxidation–Reduction Reactions of Pyridine Nucleotides

Phillip H. Pekala¹,

Bruce M. Anderson²

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Cited by 2 publications

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“…Introduction NAD glycohydrolases (NADases), which cleave NAD into nicotinamide and ADP-ribose, are a diverse class of enzymes found in species from microbes to mammals. They vary in size (20-120 kDa) and in cellular location (membrane bound to aqueous soluble) (Kaplan, 1960;Pekala and Anderson, 1982). Many eukaryotic NADases are membrane-associated ectoenzymes (Muller et al, 1983).…”

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Primary structure of a molluscan egg-specific NADase, a second-messenger enzyme.

et al. 1991

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An egg-specific NADase has been purified from the ovotestis of the marine mollusk Aplysia californica. The enzyme converts NAD to cyclic ADP-ribose (cADPR), which is a potent mobilizer of Ca2+. It is likely that the NADase serves to raise Ca2+ levels in the ova at appropriate times. A 1.2-kb cDNA clone containing the complete coding sequence of the native NADase protein was isolated from an unamplified ovotestis cDNA library and represents the first cloning of an NADase that generates cADPR. In vitro translation studies indicate that the protein initially has a signal sequence that may help to target it to discrete vesicles of the ova in which it is found. There are 12 cysteines in the open reading frame, two of these being in the signal sequence. No part of the sequence has significant similarity to other proteins or known nucleotide binding site consensus sequences. Northern blot analysis of poly(A)+ selected ovotestis RNA has identified an NADase mRNA of 1.85 kb. In situ hybridization analysis of cryostat sections from ovotestis has shown that the NADase mRNA is restricted to the immature ova, although the NADase protein is present in both immature and mature eggs.

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Primary structure of a molluscan egg-specific NADase, a second-messenger enzyme.

et al. 1991

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Erythrocyte CD38 as a prognostic marker in cancer

et al. 2007

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Non-Oxidation–Reduction Reactions of Pyridine Nucleotides

Cited by 2 publications

References 279 publications

Primary structure of a molluscan egg-specific NADase, a second-messenger enzyme.

Primary structure of a molluscan egg-specific NADase, a second-messenger enzyme.

Erythrocyte CD38 as a prognostic marker in cancer

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