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Cat No.
DIA-212
Description
Phosphoenolpyruvate carboxylase is an enzyme in the family of carboxy-lyases found in plants and some bacteria that catalyzes the addition of bicarbonate (HCO3?) to phosphoenolpyruvate (PEP) to form the four-carbon compound oxaloacetate and inorganic phosphate: PEP + HCO3-→ oxaloacetate + Pi. This reaction is used for carbon fixation in CAM (crassulacean acid metabolism) and C4 organisms, as well as to regulate flux through the citric acid cycle (also known as Krebs or TCA cycle) in bacteria and plants. The enzyme structure and its two step catalytic, irreversible mechanism have been well studied. PEP carboxylase is highly regulated, both by phosphorylation and allostery.
Abbr
PEPC (Microorganism)
Alias
PEPCase; PEPC
Species
Microorganism
Enzyme Commission Number
EC 4.1.1.31
Bio-activity
GradeⅢ 5.0U/mg-solid or more
Appearance
White amorphous powder, lyophilized
Molecular Mass
approx. 390 kDa (by gel filtration)
pH Stability
pH 5.0-8.0 (25°C, 24hr)
Michaelis Constant
1.9×10??M (Phosphoenolpyruvate)
Structure
4 Subunits (M.W.100,000) per mole of enzyme
Isoelectric point
6.0±0.1
Optimum pH
7.5-8.0
Optimum temperature
60°C
Stabilizers
BSA, sugar alcohols
Thermal stability
below 40°C (pH 7.0, 15min)
Stability
Stable at-20°C for at least one year
Applications
This enzyme is useful for enzymatic determination of carbon dioxide when coupled with malate dehydrogenase in clinical analysis.
Synonyms
PEP carboxylase; PEPCase; PEPC; EC 4.1.1.31; Phosphoenolpyruvate carboxylase; PDB ID: 3ZGE
