title: Mutagenesis of firefly luciferase shows that cysteine residues are not required for bioluminescence activity.
abstract: Conflicting reports exist in the literature as to whether sulfhydryl groups are essential for firefly luciferase activity. Inactivation of Photinus pyralis luciferase with N-tosyl-L-phenylalanine chloromethyl ketone (TPCK) and site-directed mutagenesis demonstrate that the cysteine residues are not absolutely required for activity. However, loss of P. pyralis luciferase activity is observed when any of the 4 cysteine residues is replaced with serine.
authors.affiliation: Department of Biochemistry, Faculty of Education, Shizuoka University, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Ohmiya
authors.forename: F I
authors.initials: FI
authors.lastname: Tsuji
mesh_terms: D000818:Animals; D001517:Coleoptera / Q000201:enzymology*; D003545:Cysteine; D004791:Enzyme Inhibitors / Q000494:pharmacology; D007700:Kinetics; D008156:Luciferases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D049449:Luminescence; D016297:Mutagenesis, Site-Directed; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012694:Serine; D013045:Species Specificity; D014108:Tosylphenylalanyl Chloromethyl Ketone / Q000494:pharmacology
chemical_list: D004791:Enzyme Inhibitors; D011994:Recombinant Proteins; D014108:Tosylphenylalanyl Chloromethyl Ketone; D012694:Serine; D008156:Luciferases; D003545:Cysteine