Phosphatase of Chlamydomonas reinhardi: biochemical and cytochemical approach with specific mutants.
The unicellular alga Chlamydomonas reinhardi produces two constitutive acid phosphatases and three depressible phosphatases (a neutral and two alkaline ones) that can utilize napthyl phosphate as a substrate. Specific mutants depressible phosphatase were used to investigate biochemical properties and the cytochemical localization of these enzymes. The two constitutive phosphatases show similar pH optima (about 5.0) and Km values (2 x 10(-3) to 3.3 x 10(-3) M) but differ in their heat sensitivity and affinity for glycerophosphate.
D000135:Acid Phosphatase / Q000302:isolation & purification; D000469:Alkaline Phosphatase / Q000302:isolation & purification / Q000378:metabolism; D002473:Cell Wall / Q000201:enzymology; D002474:Cell-Free System; D002696:Chlamydomonas / Q000201:enzymology*; D005994:Glycerophosphates / Q000378:metabolism; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D009154:Mutation; D010744:Phosphoric Monoester Hydrolases / Q000302:isolation & purification / Q000378:metabolism; D012995:Solubility; D014617:Vacuoles / Q000201:enzymology
D005994:Glycerophosphates; D000469:Alkaline Phosphatase; D000135:Acid Phosphatase; D010744:Phosphoric Monoester Hydrolases