Characterization of a Plasmodium vivax cysteine proteinase gene identifies uniquely conserved amino acids that may mediate the substrate specificity of malarial hemoglobinases.
The gene encoding a cysteine proteinase of the human malaria parasite Plasmodium vivax has been identified and characterized. The sequence predicted by the proteinase gene shares several unique features with the sequences of two recently characterized cysteine proteinases of other malarial species. These features include the conservation of a number of amino acids that are predicted, based on a recently devised model for the related Plasmodium falciparum cystine proteinase, to be located near the enzyme's active site. We hypothesize that these residues have been conserved to maintain optimal proteolytic specificity in the hydrolysis of globin by malaria parasites.
Rosenthal
P J
PJ
Department of Medicine, University of California, San Francisco 94143-0811.
Ring
C S
CS
Chen
X
X
Cohen
F E
FE
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D003198:Computer Simulation; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D017125:Genes, Protozoan; D005914:Globins / Q000378:metabolism; D006454:Hemoglobins / Q000378:metabolism; D006801:Humans; D006868:Hydrolysis; D008969:Molecular Sequence Data; D010966:Plasmodium vivax / Q000201:enzymology* / Q000235:genetics; D016133:Polymerase Chain Reaction; D016415:Sequence Alignment; D013379:Substrate Specificity
D006454:Hemoglobins; D005914:Globins; D003546:Cysteine Endopeptidases