P2023
Phospho(enol)pyruvate Carboxylase from corn
ammonium sulfate suspension, ≥1 units/mg protein
别名:
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.
存储类别
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Gloves
法规信息
新产品
此项目有
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
Raymond Chollet et al.
Annual review of plant physiology and plant molecular biology, 47, 273-298 (1996-06-01)
Since plant phosphoenolpyruvate carboxylase (PEPC) was last reviewed in the Annual Review of Plant Physiology over a decade ago (O'Leary 1982), significant advances have been made in our knowledge of this oligomeric, cytosolic enzyme. This review highlights this exciting progress
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
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
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