title: Adenylyl and guanylyl cyclases from the malaria parasite Plasmodium falciparum.
abstract: Completion of several malaria parasite genome sequences and advances in Plasmodium gene manipulation technology, will lead to significant advances in our knowledge of the biology of these organisms. Biochemical analysis of the cyclic nucleotide signalling pathways of P. falciparum has provided important information on malaria parasite development. The Plasmodium purine nucleotide cyclase enzymes have extremely unusual structures and the regulatory mechanisms controlling parasite enzyme activity are distinct from those operating on the analogous host molecules. Study of these enzymes could therefore lead to novel strategies for anti-malarial intervention in addition to providing unique insights into the intriguing biology of the parasite.
authors.affiliation: Department of Infectious and Tropical Diseases, London School of Hygiene & Tropical Medicine, Keppel Street, London WC1E 7HT, UK. david.baker@lshtm.ac.uk
authors.forename: David A
authors.initials: DA
authors.lastname: Baker
mesh_terms: D000262:Adenylyl Cyclases / Q000235:genetics / Q000502:physiology*; D000595:Amino Acid Sequence; D000818:Animals; D000242:Cyclic AMP / Q000502:physiology; D006152:Cyclic GMP / Q000502:physiology; D006162:Guanylate Cyclase / Q000502:physiology*; D006790:Host-Parasite Interactions / Q000502:physiology; D008969:Molecular Sequence Data; D010963:Plasmodium falciparum / Q000201:enzymology* / Q000502:physiology; D024642:Potassium Channels, Voltage-Gated / Q000235:genetics; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D017385:Sequence Homology
chemical_list: D024642:Potassium Channels, Voltage-Gated; D000242:Cyclic AMP; D000262:Adenylyl Cyclases; D006162:Guanylate Cyclase; D006152:Cyclic GMP