Claim · model-written summary
Phosphoenolpyruvate was also hydrolysed by a phosphatase in unpurified plant extracts.
- Taxon
- cucumber
Cucumis sativust0 - Organ / stage
- plant tissuese0
- Gene
- a phosphatasee0
- Outcome
- Phosphoenolpyruvatee0
Verbatim
e0“Phosphoenolpyruvate, which is the substrate for the enzyme for the enzyme pyruvate kinase, is also hydrolysed by a phosphatase when the former enzyme is assayed in unpurified extracts from plant tissues.”
t0“A phosphatase as a potential indicator of the phosphorus status of the glasshouse cucumber (Cucumis sativus)”
Title
Robert T. Besford Journal of the Science of Food and Agriculture 1978. doi:10.1002/jsfa.2740290203
Other claims from this paper (5)
- Association With added MgSO 4, phosphatase activity was highly correlated with cucumber leaf P content.
- Association Phosphatase activity was unaffected by variation in cucumber leaf N, K, or Mg.
- Method / resource Cucumber leaf pyruvate kinase activity can indicate plant K or Mg status.
- Method / resource Associated phosphatase activity indicates cucumber P status.
- Method / resource Combined enzyme assays could rapidly assess cucumber K, Mg, and P status within 2 h.