C1744
Phosphoenolpyruvate carboxylase microbial
≥5.0 unit/mg solid
Synonym(s):
PEPC
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About This Item
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form
lyophilized powder
Quality Level
specific activity
≥5.0 unit/mg solid
mol wt
~390 kDa
storage temp.
−20°C
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 .
Unit Definition
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.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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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)
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
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
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
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
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