Abstract:
:Phosphoenolpyruvate carboxylase was purified from corn root tips about 80-fold by centrifugation, ammonium sulfate fractionation, and anion exchange and gel filtration chromatography. The resulting preparation was essentially free from malate dehydrogenase, isocitrate dehydrogenase, malate enzyme, NADH oxidase, and pyruvate kinase activity. Kinetic analysis indicated that l-malate was a noncompetitive inhibitor of P-enolpyruvate carboxylase with respect to P-enolpyruvate (K(I) = 0.8 mm). d-Malate, aspartate, and glutamate inhibited to a lesser extent; succinate, fumarate, and pyruvate did not inhibit. Oxaloacetate was also a noncompetitive inhibitor of P-enolpyruvate carboxylase with an apparent K(I) of 0.4 mm. A comparison of oxaloacetate and l-malate inhibition suggested that the mechanisms of inhibition were different. These data indicated that l-malate may regulate CO(2) fixation in corn root tips by a feedback or end product type of inhibition.
journal_name
Plant Physioljournal_title
Plant physiologyauthors
Ting IPdoi
10.1104/pp.43.12.1919subject
Has Abstractpub_date
1968-12-01 00:00:00pages
1919-24issue
12eissn
0032-0889issn
1532-2548journal_volume
43pub_type
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