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- Zinc in lipase L1 from Geobacillus stearothermophilus L1 and structural implications on thermal stability
- Won Chan Choi; Myung Hee Kim; H S Ro; S R Ryu; Tae Kwang Oh; Jung-Kee Lee
- Bibliographic Citation
- FEBS Letters, vol. 579, no. 16, pp. 3461-3466
- Publication Year
- Lipase L1 from Geobacillus stearothermophilus L1 contains an unusual extra domain, making a tight intramolecular interaction with the main catalytic domain through a Zn2+-binding coordination. To elucidate the role of the Zn2+, we disrupted the Zn2+-binding site by mutating the zinc-ligand residues (H87A, D61A/H87A, and D61A/H81A/H87A/D238A). The activity vs. temperature profiles of the mutant enzymes showed that the disruption of the Zn2+-binding site resulted in a notable decrease in the optimal temperature for maximal activity from 60 to 45-50°C. The mutations also abolished the Zn2+-induced thermal stabilization. The wild-type enzyme revealed a 34.6-fold increase in stabilization with the addition of Zn2+ at 60°C, whereas the mutant enzymes exhibited no response to Zn2+. Additional circular dichroism spectroscopy studies also confirmed the structural stabilizing role of Zn2+ on lipase L1 at elevated temperatures.
- geobacillus stearothermophilus L1thermostable lipaseZn2+
- Appears in Collections:
- Division of Biomedical Research > Microbiome Convergence Research Center > 1. Journal Articles
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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