P2023
Phospho(enol)pyruvate Carboxylase from corn
ammonium sulfate suspension, ≥1 units/mg protein
Synonym(s):
Orthophosphate:oxaloacetate carboxylyase-(phosphorylating), PEP-carboxylase, Phosphoenolpyruvate Carboxylase from maize leaves
form
ammonium sulfate suspension
specific activity
≥1 units/mg protein
foreign activity
malic dehydrogenase, variable
malic enzyme, variable
storage temp.
2-8°C
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General description
Phospho(enol)pyruvate carboxylase is a ubiquitous, highly regulated oligomeric, cytosolic enzyme in plants.
Application
Phospho(enol)pyruvate carboxylase has been used in a study to assess activity of carbon metabolism enzymes in wheat plants treated with kartolin-4 and exposed to water stress. It has also been used in a study to investigate the specific density of leaf as a characteristic of the photosynthetic apparatus.
Biochem/physiol Actions
Phospho(enol)pyruvate Carboxylase from corn was found to be highly susceptible to trypsin digestion.
Physical form
Suspension in 2.4 M (NH4)2SO4 solution containing 10 mM phosphate buffer, pH 7.0, 1 mM biotin, 5 mM dithiothreitol and 1 mM phenylmethylsulfonyl fluoride
Other Notes
One unit will form 1.0 μmole of oxaloacetate from phospho(enol)pyruvate and CO2 per min at pH 8.5 at 25 °C.
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Katie J Dalziel et al.
FEBS letters, 586(7), 1049-1054 (2012-05-10)
Phosphoenolpyruvate carboxylase (PEPC) is a tightly controlled anaplerotic enzyme situated at a pivotal branch point of plant carbohydrate-metabolism. In developing castor oil seeds (COS) a novel allosterically-densensitized 910-kDa Class-2 PEPC hetero-octameric complex arises from a tight interaction between 107-kDa plant-type
R T Wedding et al.
Plant physiology, 84(4), 979-981 (1987-08-01)
Phosphenolpyruvate (PEP) carboxylase from leaves of Crassula argentea displays varying levels of sensitivity to inactivation by various proteolytic enzymes. In general, the native enzyme is sensitive to proteinases known to attack at the carbonyl end of lysine or arginine (trypsin
I I Cherniad'ev et al.
Prikladnaia biokhimiia i mikrobiologiia, 37(6), 706-712 (2002-01-05)
Enzymatic activities of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) (EC 4.1.1.39), phospho(enol)pyruvate carboxylase (EC 4.1.1.31), NAD malate dehydrogenase (EC 1.1.1.37), and NADP glyceraldehydephosphate dehydrogenase complex including phosphoglycerate kinase (EC 2.7.2.3) and glyceraldehydephosphate dehydrogenase (EC 1.2.1.13) were comparatively assayed in wheat seedlings of the
M Le Maire et al.
The Biochemical journal, 267(2), 431-439 (1990-04-15)
We have reinvestigated the use of ionizing radiations to measure the molecular mass of water-soluble or membrane proteins. The test was performed by using the most straightforward aspect of the technique, which consists of SDS/PAGE analysis of the protein-fragmentation process.
I I Cheniad'ev
Prikladnaia biokhimiia i mikrobiologiia, 37(4), 466-471 (2001-09-04)
At early stages of ontogeny (up to 50-60% of the maximum leaf area) of wheat (Triticum aestivum L.), meadow fescue (Festuca pratensis Huds.), reed fescue (F. arindinacea Schreb.), and sugar beet (Beta vulgaris L. var. saccharifera (Alef) Krass), there is
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