C1744
Phosphoenolpyruvate carboxylase microbial
≥5.0 unit/mg solid
Synonym(s):
PEPC
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About This Item
Specific activity:
≥5.0 unit/mg solid
Product Name
Phosphoenolpyruvate carboxylase microbial, ≥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 .
Other Notes
One unit causes the oxidation of one micromole of NADH per minute at pH 8.0 at 30°C.
Physical form
White amorphous lyophilized powder containing BSA and sugar alchohols as stabilizers.
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
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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)
Multiple origins of allopolyploid wheatgrass Elymus caninus revealed by RPB2, PepC and TrnD/T genes.
Chi Yan et al.
Molecular phylogenetics and evolution, 64(3), 441-451 (2012-05-24)
We examined evolutionary mechanisms in the tetraploid Elymus caninus by comparing the phylogenetic relationships of 21 accessions suggested by sequence data from two single copy nuclear genes, the largest subunit of RNA polymerase II (RPB2) and phosphoenolpyruvate carboxylase (pepC), and
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
Judith Katharina Paulus et al.
Nature communications, 4, 1518-1518 (2013-02-28)
The C4-photosynthetic carbon cycle is an elaborated addition to the classical C3-photosynthetic pathway, which improves solar conversion efficiency. The key enzyme in this pathway, phosphoenolpyruvate carboxylase, has evolved from an ancestral non-photosynthetic C3 phosphoenolpyruvate carboxylase. During evolution, C4 phosphoenolpyruvate carboxylase
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
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