Online Archive of University of Virginia Scholarship
Broad Specificity of a Zinc-dependent Small Alcohol Dehydrogenase from Thermotoga Maritima Involved in the Glycerol Dismutation Pathway633 views
Author
Lee, Christopher Ting-Kuang, Department of Chemistry, University of Virginia
Advisors
Columbus, Linda, Department of Chemistry, University of Virginia
Mura, Cameron, Department of Chemistry, University of Virginia
Cafiso, David, Department of Chemistry, University of Virginia
Richardson, Fred, Department of Chemistry, University of Virginia
Bushweller, John, Department of Molecular Phys and Biological Physics, University of Virginia
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
Degree
MS (Master of Science)
Language
English
Rights
All rights reserved (no additional license for public reuse)
Lee, Christopher Ting-Kuang. Broad Specificity of a Zinc-dependent Small Alcohol Dehydrogenase from Thermotoga Maritima Involved in the Glycerol Dismutation Pathway. University of Virginia, Department of Chemistry, MS (Master of Science), 2012-05-01, https://doi.org/10.18130/V3FD40.
