Maize Phosphoenolpyruvate Carboxylase
نویسندگان
چکیده
منابع مشابه
Hysteresis 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...
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 کاملRegulation at the phosphoenolpyruvate branchpoint in Azotobacter vinelandii: phosphoenolpyruvate carboxylase.
Phosphoenolpyruvate carboxylase (EC 4.1.1.31) from Azotobacter vinelandii, like the corresponding enzyme from other organisms, is activated by acetyl coenzyme A and inhibited by l-aspartate. Both modifiers affect primarily the affinity of the enzyme for phosphoenolpyruvate. This is the first enzyme with a strictly anaplerotic (intermediate-replacing) function to be tested for response to the ad...
متن کاملCarboxylation 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...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2005
ISSN: 0021-9258
DOI: 10.1074/jbc.m408768200