Re-engineering of Bacterial Luciferase; For New Aspects of Bioluminescence

Title:Re-engineering of Bacterial Luciferase; For New Aspects of Bioluminescence

Volume: 19 Issue: 1

Author(s): Da-Som Kim, Jeong-Ran Choi, Jeong-Ae Ko*Kangmin Kim*

Affiliation:

• Department of Horticulture, College of Agriculture & Life Sciences, Chonbuk National University, Jeonju, 561-756,Korea

• Division of Biotechnology, Chonbuk National University, Iksan, 570-752,Korea

Keywords: Aldehyde, bacterial luciferase, flavin, mobile loop, protein engineering, bioluminescence.

Abstract: Bacterial luminescence is the end-product of biochemical reactions catalyzed by the luciferase enzyme. Nowadays, this fascinating phenomenon has been widely used as reporter and/or sensors to detect a variety of biological and environmental processes. The enhancement or diversification of the luciferase activities will increase the versatility of bacterial luminescence. Here, to establish the strategy for luciferase engineering, we summarized the identity and relevant roles of key amino acid residues modulating luciferase in Vibrio harveyi, a model luminous bacterium. The current opinions on crystal structures and the critical amino acid residues involved in the substrate binding sites and unstructured loop have been delineated. Based on these, the potential target residues and/or parameters for enzyme engineering were also suggested in limited scale. In conclusion, even though the accurate knowledge on the bacterial luciferase is yet to be reported, the structure-guided site-directed mutagenesis approaches targeting the regulatory amino acids will provide a useful platform to re-engineer the bacterial luciferase in the future.

Cite this article as:

Kim Da-Som, Choi Jeong-Ran, Ko Jeong-Ae*, Kim Kangmin*, Re-engineering of Bacterial Luciferase; For New Aspects of Bioluminescence, Current Protein & Peptide Science 2018; 19 (1) . https://dx.doi.org/10.2174/1389203718666161122104530