C-terminal region of the active domain enhances enzymatic activity in dinoflagellate luciferase†
Abstract
The dinoflagellate luciferase of Lingulodinium polyedrum has three catalytic domains in its single polypeptide chain (Mr = 137 kDa), and each 42 kDa domain is enzymatically active. Deletion mutants for N- or C-terminal regions of domain 3 of the luciferase, ranging from 29 to 38 kDa, were constructed and expressed in E. colicells. The activities of N-terminal deleted mutants were above 20% of wild type, but showed different pH-activity profiles. By contrast, the activities of C-terminal deleted mutants decreased drastically to below 1% of wild type, although their pH-activity profiles and
- This article is part of the themed collection: Bioluminescence