title: Trypanosome and animal lanosterol synthases use different catalytic motifs.
abstract: [see reaction]. Animals, fungi, and some protozoa convert oxidosqualene to lanosterol in the ring-forming reaction in sterol biosynthesis. The Trypanosoma cruzi lanosterol synthase has now been cloned. The sequence shares with the T. brucei lanosterol synthase a tyrosine substitution for the catalytically important active-site threonine found in animal and fungal lanosterol synthases.
authors.affiliation: Department of Chemistry, Rice University, 6100 South Main Street, Houston, Texas 77005, USA.
authors.forename: B M
authors.initials: BM
authors.lastname: Joubert
authors.forename: F S
authors.initials: FS
authors.lastname: Buckner
authors.forename: S P
authors.initials: SP
authors.lastname: Matsuda
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D020134:Catalytic Domain; D006801:Humans; D019751:Intramolecular Transferases / Q000378:metabolism*; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D014349:Trypanosoma cruzi / Q000201:enzymology*
chemical_list: D019751:Intramolecular Transferases; C021924:lanosterol synthase