C1744
Phosphoenolpyruvate carboxylase microbial
≥5.0 unit/mg solid
Synonym(s):
PEPC
Sign In to View Organizational & Contract Pricing.
Select a Size
About This Item
Specific activity:
≥5.0 unit/mg solid
form
lyophilized powder
specific activity
≥5.0 unit/mg solid
mol wt
~390 kDa
storage temp.
−20°C
Quality Level
Application
Phosphoenolpyruvate carboxylase (PEPC) is an enzyme useful for enzymatic determination of carbon dioxide when coupled with malate dehydrogenase in clinical analysis. PEPC is also used to study carbon assimilation, post-translational regulation and allosteric regulation in various plants .
Biochem/physiol Actions
Phosphoenolpyruvate carboxylase (PEPC) catalyzes the addition of bicarbonate to phosphoenolpyruvate (PEP) to form the four-carbon compound oxaloacetate and inorganic phosphate . In CAM and C4 plants, PEPC catalyzes the photosynthetic assimilation of CO2 into an organic acid. PEPC is activated by glucose-6-phosphate and is inhibited by malate and aspartate. PEPC comprises about 0.5-2% of the soluble protein in alfalfa and soybean nodules .
Physical form
White amorphous lyophilized powder containing BSA and sugar alchohols as stabilizers.
Other Notes
One unit causes the oxidation of one micromole of NADH per minute at pH 8.0 at 30°C.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
含少量动物源组分生物产品
常规特殊物品
This item has
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Mika Nomura et al.
Plant & cell physiology, 47(5), 613-621 (2006-03-10)
Phosphoenolpyruvate carboxylase (PEPC, EC 4.1.1.31) is believed to play a significant role in supporting nitrogen fixation via anaplerotic CO2 fixation for recycling carbon in nodules. Using the antisense technique, we decreased the expression levels of the nodule-enhanced PEPC gene (Ljpepc1)
Patrizia De Nisi et al.
Plant physiology and biochemistry : PPB, 57, 168-174 (2012-06-19)
The regulation exerted by the Fe status in the plant on Fe deficiency responses was investigated in Cucumis sativus L. roots at both biochemical and molecular levels. Besides the two activities strictly correlated with Fe deficiency response, those of the
Jitender Singh et al.
Gene, 500(2), 224-231 (2012-06-20)
Phosphoenolpyruvate carboxylase is an ubiquitous cytosolic enzyme that catalyzes the ß-carboxylation of phosphoenolpyruvate (PEP) and is encoded by multigene family in plants. It plays an important role in carbon economy of plants by assimilating CO2 into organic acids for subsequent
Masataka Wakayama et al.
Journal of plant research, 126(2), 233-241 (2012-10-18)
The C(4) grass Arundinella hirta exhibits a unique C(4) anatomy, with isolated Kranz cells (distinctive cells) and C(4)-type expression of photosynthetic enzymes in the leaf sheath and stem as well as in the leaf blade. The border zones between these
Jianfang Xu et al.
PloS one, 7(5), e37438-e37438 (2012-05-23)
Ulva prolifera, a typical green-tide-forming alga, can accumulate a large biomass in a relatively short time period, suggesting that photosynthesis in this organism, particularly its carbon fixation pathway, must be very efficient. Green algae are known to generally perform C₃
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service