title: Identification of two catalytic domains in a luciferase secreted by the copepod Gaussia princeps.
abstract: Gaussia luciferase secreted by the copepod Gaussia princeps catalyzes the oxidation of coelenterazine to produce blue light. The primary structure of Gaussia luciferase deduced from the cDNA sequence shows two repeat sequences of 71 amino acid residues, suggesting the luciferase consists of two structural domains. Two domains in Gaussia luciferase were expressed independently in Escherichia coli cells, purified and characterized. We found that both domains have luminescence activity with coelenterazine, and the catalytic properties including luminescence spectrum, optimal pH, substrate specificity and luminescence stimulation by halogen ions (Cl-, Br- and I-) are identical to intact Gaussia luciferase. Thus, Gaussia luciferase has two catalytic domains for the luminescence reaction.
authors.affiliation: Yokohama Research Center, Chisso Corporation, 5-1 Okawa, Kanazawa-ku, Yokohama 236-8605, Japan.
authors.forename: Satoshi
authors.initials: S
authors.lastname: Inouye
authors.forename: Yuiko
authors.initials: Y
authors.lastname: Sahara
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D020134:Catalytic Domain; D002478:Cells, Cultured; D033342:Copepoda / Q000201:enzymology*; D018076:DNA, Complementary / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008156:Luciferases / Q000737:chemistry*; D008969:Molecular Sequence Data; D013379:Substrate Specificity
chemical_list: D018076:DNA, Complementary; D008156:Luciferases