Extracellular folate deaminase of Dictyostelium discoideum.
Folate deaminase released from cells of Dictyostelium discoideum is heterogeneous with respect to molecular weight and stability at 60 degrees C. The most heat-stable component isoelectrofocuses in a broad band at approx. pH 6. The Km value of this component for folate is approx. 7 x 10(-7)M and Mr approx. 40 000. The major portion if not all of the deaminase binds to immobilized concanavalin A and lentil lectin. Extracellular folate deaminase has a pH-optimum of approx. pH 6.0. This is higher than that of lysosomal enzymes, which are also glycoproteins released into the extracellular medium.
D000619:Aminohydrolases / Q000378:metabolism*; D000242:Cyclic AMP / Q000378:metabolism; D004023:Dictyostelium / Q000378:metabolism*; D005492:Folic Acid / Q000378:metabolism; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D015800:Protozoan Proteins
D015800:Protozoan Proteins; D005492:Folic Acid; D000242:Cyclic AMP; D000619:Aminohydrolases; C020144:folic acid deaminase, Dictyostelium discoideum