Premium
Glycogen Phosphorylase Sequences from the Amitochondriate Protists, Trichomonas vaginalis, Mastigamoeba balamuthi, Entamoeba histolytica and Giardia intestinalis 1
Author(s) -
WU GANG,
MÜLLER MIKLÖS
Publication year - 2003
Publication title -
journal of eukaryotic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 1066-5234
DOI - 10.1111/j.1550-7408.2003.tb00151.x
Subject(s) - biology , protist , entamoeba histolytica , trichomonas vaginalis , glycogen phosphorylase , dictyostelium discoideum , entamoeba , gene , trichomonas , giardia lamblia , protozoa , microbiology and biotechnology , genetics , biochemistry , glycogen
. Glycogen phosphorylase genes or messages from four amitochondriate eukaryotes, Trichomonas vaginalis, Mastigamoeba balamuthi, Entamoeba histolytica (two genes) and Giardia intestinalis , have been isolated and sequenced. The sequences of the amitochondriate protist enzymes appear to share a most recent common ancestor. The clade containing these sequences is closest to that of another protist, the slime mold ( Dictyostelium discoideum ), and is more closely related to fungal and plant phosphorylases than to mammalian and eubacterial homologs. Structure‐based amino acid alignment shows conservation of the residues and domains involved in catalysis and allosteric regulation by glucose 6‐phosphate but high divergence at domains involved in phosphorylation‐dependent regulation and AMP binding in fungi and animals. Protist phosphorylases, as their prokaryotic and plant counterparts, are probably not regulated by phosphorylation.