Fractionation of Stable Carbon Isotopes by Phosphoenolpyruvate Carboxylase from C4 Plants
نویسندگان
چکیده
منابع مشابه
Fractionation of stable carbon isotopes by phosphoenolpyruvate carboxylase from c(4) plants.
The active species of "CO(2)" and the amount of fractionation of stable carbon isotopes have been determined for a partially purified preparation of phosphoenolpyruvate (PEP) carboxylase (EC 4.1.1.31) from corn (Zea mays) leaves. The rates of the enzyme reactions, using substrate amounts of HCO(3) (-), CO(2) or CO(2) plus carbonic anhydrase, show that HCO(3) (-) is the active species of "CO(2)"...
متن کاملEnzymatic fractionation of carbon isotopes by phosphoenolpyruvate carboxylase from c(4) plants.
The carbon atoms of glucose and malate in C(4) plants are 2 to 3 per thousand enriched in (12)C with respect to atmospheric CO(2); whereas these intermediates in C(3) plants are 15 to 18 per thousand enriched with (12)C with respect to atmospheric CO(2). The enzymatic synthesis of malate from phosphoenolpyruvate and bicarbonate in preparations of leaves of Sorghum bicolor, Haygrazer result in a...
متن کاملEnzymic Fractionation of the Stable Carbon Isotopes of Carbon Dioxide by Ribulose-1,5-bisphosphate Carboxylase.
The enzymic fractionation of the stable carbon isotopes of CO(2) (Deltaco(2)) was determined using a purified preparation of ribulose-1,5-bisphosphate (RuBP) carboxylase isolated from cotton (a C(3) plant) leaves. The bicarbonate concentration in the reaction mixture saturated the enzyme and furnished an infinite pool of (12)CO(2) and (13)CO(2) for enzyme fractionation. The RuBP was 96 to 98% p...
متن کاملCoordinate regulation of phosphoenolpyruvate carboxylase and phosphoenolpyruvate carboxykinase by light and CO2 during C4 photosynthesis.
The aim of this study was to investigate the relationship between the phosphorylation and activation states of phosphoenolpyruvate carboxykinase (PEPCK) and to investigate how the phosphorylation states of PEPCK and phosphoenolpyruvate carboxylase (PEPC) are coordinated in response to light intensity and CO(2) concentration during photosynthesis in leaves of the C(4) plant Guinea grass (Panicum...
متن کاملPhosphoenolpyruvate carboxylase from C4 leaves is selectively targeted for inhibition by anionic phospholipids.
Phosphoenolpyruvate carboxylase (PEPC; EC 4.1.1.31) is an enzyme playing a crucial role in photosynthesis of C4 plants. Here, we identify anionic phospholipids as novel regulators that inhibit C4 PEPC activity and provide evidence that the enzyme partially localizes to membranes. PEPC catalyzes the b-carboxylation of phosphoenolpyruvate (PEP) in a reaction that yields oxaloacetate and inorganic...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Plant Physiology
سال: 1977
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.59.4.564