Phosphoenol-3-bromopyruvate. A mechanism-based inhibitor of phosphoenolpyruvate carboxylase from maize.
نویسندگان
چکیده
منابع مشابه
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 i...
متن کاملEffects of the Phosphoenolpyruvate Carboxylase Inhibitor
The effect of 3,3-dichloro-2-(dihydroxyphosphinoylmethyl)propenoate (DCDP), an analog of phosphoenolpyruvate (PEP), on PEP carboxylase activity in crude leaf extracts and on photosynthesis of excised leaves was examined. DCDP is an effective inhibitor of PEP carboxylase from Zea mays or Pancum miliaceum; 50% inhibition was obtained at 70 or 350 micromolar, respectively, in the presence of I mil...
متن کاملPhosphoenolpyruvate Carboxylase from Maize Leaves. Studies Using ß-Methylated Phosphoenolpyruvate Analogues as Inhibitors and Substrates*
Daniel H. Gonzalez and Carlos S. Andreo Centro de Estudios Fotosinteticos y Bioqui'micos, Suipacha 531. 2000 Rosario. Argentina Z. Naturforsch. 41c, 1004—1010 (1986); received June 23/August 15, 1986 Phosphoenolpyruvate Carboxylase, Phosphoenolpyruvate Analogues, Reaction Mechanism, Maize Leaf 1. The phosphoenolpyruvate analogues phosphoenol-a-ketobutyrate and phosphoenol-aketoisovalerate are l...
متن کاملHysteresis and Reversible Cold Inactivation of Maize Phosphoenolpyruvate Carboxylase
Maize (Z ea mays L.) leaf phosphoenolpyruvate (PEP) carboxylase (PEPCase) (EC 4.1.1.31) showed a lag in activity when assayed after storage at 0 4 °C. The lag was prom oted by high pH on storage (7.8 8 .5) and was observed over a range o f assay pH (7.1 -8 .5 ). Therm al reacti vation o f the cold-stored enzyme by assay tem perature (18 °C) accounted for most o f the hysteretic effect, but pre...
متن کاملLimited proteolysis by trypsin influences activity of maize phosphoenolpyruvate carboxylase.
Maize phosphoenolpyruvate carboxylase (PEPC) was rapidly and completely inactivated by very low concentrations of trypsin at 37 degrees C. PEP+Mg2+ and several other effectors of PEP carboxylase offered substantial protection against trypsin inactivation. Inactivation resulted from a fairly specific cleavage of 20 kDa peptide from the enzyme subunit. Limited proteolysis under catalytic conditio...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1982
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)33318-0