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Structure and properties of luciferase from Photobacterium phosphoreum.

作者信息

Ferri S R, Soly R R, Szittner R B, Meighen E A

机构信息

Department of Biochemistry, McGill University, Montreal, Quebec, Canada.

出版信息

Biochem Biophys Res Commun. 1991 Apr 15;176(1):541-8. doi: 10.1016/0006-291x(91)90959-b.

Abstract

The nucleotide sequences of the luxA and luxB genes coding for the alpha and beta subunits, respectively, of luciferase from Photobacterium phosphoreum have been determined. The predicted amino acid sequences of the alpha and beta subunits were shown to be significantly different from other bacterial luciferases with 62 to 88% identity with the alpha subunits and 47 to 71% identity with the beta subunits of other species. Expression of the different luciferases appear to correlate with the number of modulator codons. Kinetic properties of P. phosphoreum luciferase were shown to reflect the bacterium's natural cold temperature habitat.

摘要

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