Carboxylation and dephosphorylation of phosphoenol-3-fluoropyruvate by maize leaf phosphoenolpyruvate carboxylase.
The analogue (Z)-phosphoenol-3-fluoropyruvate [(Z)-3-fluoro-2-(phosphono-oxy)propenoic acid] was tested as substrate of maize leaf phosphoenolpyruvate carboxylase. Studies with NaH14CO3 indicate that the analogue is carboxylated by the enzyme. However, this reaction accounts for only one-tenth of the activity measured by Pi liberation. The rest of the analogue is merely dephosphorylated. This is the first analogue for which both carboxylation and dephosphorylation have been observed.
Centro de Estudios Fotosintéticos y Bioquímicos (CEFOBI), Rosario, Argentina.
D H
DH
Gonzalez
C S
CS
Andreo
D001639:Bicarbonates / Q000378:metabolism; D002250:Carbon Radioisotopes; D002262:Carboxy-Lyases / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D006835:Hydrazones / Q000378:metabolism; D010728:Phosphoenolpyruvate / Q000031:analogs & derivatives* / Q000378:metabolism; D010730:Phosphoenolpyruvate Carboxylase / Q000378:metabolism*; D013053:Spectrophotometry; D003313:Zea mays / Q000201:enzymology*
C001072:2,4-dinitrophenylhydrazone; D001639:Bicarbonates; D002250:Carbon Radioisotopes; D006835:Hydrazones; D010728:Phosphoenolpyruvate; C041143:phosphoenol-3-fluoropyruvate; D002262:Carboxy-Lyases; D010730:Phosphoenolpyruvate Carboxylase