1980
DOI: 10.1016/0031-9422(80)85007-2
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The cyclic nucleotide phosphodiesterases of spinach chloroplasts and microsomes

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Cited by 34 publications
(12 citation statements)
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“…cNMP phosphodiesterase enzymatic activity is present in plant cells (22,26,30) and acts to catabolize cAMP and maintain homeostatic levels in the cytosol after changes that occur in the level of this secondary messenger during signaling cascades (4). We hypothesized that blocking the breakdown of endogenous cAMP by inhibition of cNMP phosphodiesterase activity could therefore affect NO generation in the plant cell.…”
Section: Cnmp Cngcs and Immune Signalingmentioning
confidence: 99%
“…cNMP phosphodiesterase enzymatic activity is present in plant cells (22,26,30) and acts to catabolize cAMP and maintain homeostatic levels in the cytosol after changes that occur in the level of this secondary messenger during signaling cascades (4). We hypothesized that blocking the breakdown of endogenous cAMP by inhibition of cNMP phosphodiesterase activity could therefore affect NO generation in the plant cell.…”
Section: Cnmp Cngcs and Immune Signalingmentioning
confidence: 99%
“…Intriguingly, characteristics of the second class of plant cyclic nucleotide phosphodiesterases suggest a function in RNA degradation, which was first proposed by Lin and Varner (1972). Therefore, it is not surprising that tomato extracellular cyclic nucleotide phosphodiesterase shares several key characteristics with preparations of phosphodiesterases from pea (Lin and Varner, 1972), barley (Vandepeute et al, 1973), potato (Ashton and Polya, 1975;Zan-Kowalczewska et al, 1984), sunflower (Junker et al, 1977), spinach (Brown et al, 1980), lettuce (Chiatante et al, 1988), or Lemna (Gangwani et al, 1994, such as molecular mass of the monomer unit (65-80 kD), an acidic pH optimum (pH 5-7), lack of requirement for bivalent metal ions, and broad substrate specificity. In general, higher plant cyclic nucleotide phosphodiesterases of this class hydrolyze, irrespective of the nucleobase present, 2Ј:3Ј-cyclic NMP to 3Ј-NMP at a higher rate than 3Ј:5Ј-cyclic NMP to a mixture of 3Ј-NMP and 5Ј-NMP, typically in a ratio of 7 to 1 (Lin and Varner, 1972), which is similar to the ratio observed for the tomato enzyme (6:1).…”
Section: Discussionmentioning
confidence: 98%
“…In contrast, the I c phosphodiesterase had highest activity with 3h,5h-cGMP and 3h,5h-cAMP and little activity with their 2h,3h isomers, had a less acidic pH optimum of 6.1, was sensitive to inhibition by methylxanthines, and liberated 5h-mononucleotides as the main product ; it also displayed sensitivity to endogenous protein effectors and was activated by Ca# + (Brown et al, 1979b). Further examination of I c phosphodiesterase revealed that it occurred in multienzyme complexes of molecular mass 187 and 370 kDa in association with acid phosphatase, ribonuclease, nucleotidase and ATPase (Brown et al, 1980a).…”
Section: mentioning
confidence: 99%