Specific features of phosphomonoesterase of Entamoeba histolytica (NIH-200).
Axenically grown E. histolytica possess significant acid phosphatase activity. The Km of the enzyme was found to be 7.1 x 10(-3) and was maximally active at pH 4.5. Acid phosphatase activity was significantly inhibited by Cu2+, cysteine and was activated by tartrate and fluoride. It was found that E. histolytica acid phosphatase differs in some properties as compared to the enzyme reported from other sources.
Agrawal
A
A
Division of Biochemistry, Central Drug Research Institute, Lucknow, India.
Prasad
H C
HC
Pandey
V C
VC
Sagar
P
P
D000818:Animals; D003300:Copper / Q000494:pharmacology; D003545:Cysteine / Q000494:pharmacology; D004748:Entamoeba histolytica / Q000201:enzymology*; D004789:Enzyme Activation; D005459:Fluorides / Q000494:pharmacology; D010744:Phosphoric Monoester Hydrolases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D013644:Tartrates / Q000494:pharmacology
D013644:Tartrates; D003300:Copper; D010744:Phosphoric Monoester Hydrolases; D003545:Cysteine; D005459:Fluorides