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Broad Specificity of a Zinc-Dependent Small Alcohol Dehydrogenase From Thermotoga Maritima Involved in the Glycerol Dismutation Pathway

Lee, Christopher Ting-Kuang
Format
Thesis/Dissertation; Online
Author
Lee, Christopher Ting-Kuang
Advisor
Richardson, Fred
Mura, Cameron
Columbus, Linda
Bushweller, John
Cafiso, David
Abstract
A putative glycerol dehydrogenase (TM0423) from Thermotoga maritima was functionally characterized using bioinformatic and biochemical techniques. Glycerol dehydrogenases (EC 1.1.1.6) catalyze the oxidation of glycerol to dihydroxyacetone (DHA) with the concomitant reduction of NAD + to NADH, which can be assayed at 340 nm. Enzymatic activity of TM0423 was verified at 65 ◦ C in the presence of Zn 2+ . The use of other divalent cations, including Ni 2+ and Co 2+ , led to reasonable albeit varying levels of enzymatic activity. Exposure to the chelating agent EDTA resulted in complete loss of activity while subsequent reintroduction of metal co-factors to a metal-deficient reaction mixture restored function, suggesting that TM0423 is a divalent metal cation-dependent dehydrogenase. Additional substrates were screened to shed light on potential catalytic mechanisms. The thermostability and enzymatic activity of TM0423 makes it an attractive target for biofuel research. Note: Abstract extracted from PDF text
Language
English
Published
University of Virginia, Department of Chemistry, MS (Master of Science), 2012
Published Date
2012-05-01
Degree
MS (Master of Science)
Collection
Libra ETD Repository
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