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Title 

Zinc in lipase L1 from Geobacillus stearothermophilus L1 and structural implications on thermal stability

Authors 

Won Chan ChoiMyung Hee KimH S RoS R RyuTae Kwang OhJung-Kee Lee

Publisher 

Elsevier

Issue Date 

2005

Citation 

FEBS Letters, vol. 579, no. 16, pp. 3461-3466

Keywords 

geobacillus stearothermophilus L1thermostable lipaseZn2+triacylglycerol lipasezincgeobacillus stearothermophilusthermostabilityenzyme stabilitylipase

Abstract 

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.

ISSN 

0014-5793

Link 

http://dx.doi.org/10.1016/j.febslet.2005.05.016

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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