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Literature summary for 4.1.1.31 extracted from

  • Schuller, K.A.; Plaxton, W.C.; Turpin, D.H.
    Regulation of phosphoenolpyruvate carboxylase from the green alga Selenastrum minutum (1990), Plant Physiol., 93, 1303-1311.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
dihydroxyacetone phosphate isoenzyme PEPC2 is inactivated 6fold by 2.0 mM, 52% activation by isoenzyme PEPC2 Monoraphidium minutum
glutamine isoenzyme PEPC1 is inactivated more than 4fold by 2 mM, 8% activation of isoenzyme PEPC2 Monoraphidium minutum

Inhibitors

Inhibitors Comment Organism Structure
2-oxoglutarate isoenzyme PEPC1 is more sensitive to inhibition than isoenzyme PEPC2 Monoraphidium minutum
Asp isoenzyme PEPC1 is more sensitive to inhibition than isoenzyme PEPC2 Monoraphidium minutum
Glu isoenzyme PEPC1 is more sensitive to inhibition than isoenzyme PEPC2 Monoraphidium minutum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
-
Monoraphidium minutum

Organism

Organism UniProt Comment Textmining
Monoraphidium minutum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial, 2 isoforms: PEPC1 and PEPC2 Monoraphidium minutum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.036
-
isoenzyme PEPC1 Monoraphidium minutum
0.138
-
isoenzyme PEPC2 Monoraphidium minutum

Storage Stability

Storage Stability Organism
-80°C, stable for at least 1 month Monoraphidium minutum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphoenolpyruvate + CO2
-
Monoraphidium minutum phosphate + oxaloacetate
-
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