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Plasmodium falciparum: S-adenosyl-L-methionine decarboxylase.

Abstract
Putrescine-dependent S-adenosyl-L-methionine decarboxylase has been detected in the malaria parasite Plasmodium falciparum. Mg2+ did not affect the enzyme activity. The apparent Km value of the plasmodial enzyme for adenosyl-methionine was found to be 33 microM. Methylglyoxal bis(guanylhydrazone) competitively inhibited the enzyme activity with respect to adenosylmethionine. The inhibition constant for methylglyoxal bis(guanylhydrazone) was determined to be 0.46 microM. Spermidine was the main polyamine detected in the parasite. There was significant decrease in the S-adenosyl-L-methionine decarboxylase activity when the infected erythrocytes were incubated with chloroquine and mefloquine for 2 hr at 1 and 10 microM, respectively. Since at similar concentrations these drugs did not directly affect the plasmodial enzyme activity, the interaction of these drugs with the polyamine biosynthesis remains unclear.
AuthorsS Rathaur, R D Walter
JournalExperimental parasitology (Exp Parasitol) Vol. 63 Issue 2 Pg. 227-32 (Apr 1987) ISSN: 0014-4894 [Print] United States
PMID3552714 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Polyamines
  • Quinolines
  • Chloroquine
  • Carboxy-Lyases
  • Adenosylmethionine Decarboxylase
  • Mitoguazone
  • Mefloquine
  • Putrescine
Topics
  • Adenosylmethionine Decarboxylase (antagonists & inhibitors, metabolism)
  • Animals
  • Carboxy-Lyases (metabolism)
  • Chloroquine (pharmacology)
  • Erythrocytes (parasitology)
  • Humans
  • Hydrogen-Ion Concentration
  • Kinetics
  • Mefloquine
  • Mitoguazone (pharmacology)
  • Plasmodium falciparum (analysis, drug effects, enzymology)
  • Polyamines (analysis)
  • Putrescine (pharmacology)
  • Quinolines (pharmacology)

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