Abstract
A TcAAD cDNA encoding a putative aryl‐alcohol dehydrogenase (AAD) was cloned from Taiwanofungus camphorata (Tc). The deduced amino acid sequence is conserved among the reported AADs. A 3‐D structural model of the TcAAD has been created based on the known structure of voltage‐dependent potassium channels subunit beta‐2 (PDB code: 3EAU). To characterize the TcAAD, the coding region was subcloned into an expression vector and transformed into Saccharomyces cerevisiae. The recombinant His6‐tagged TcAAD was overexpressed and purified by Ni affinity chromatography. The purified enzyme showed a band of approximately 39 kDa on a 12 % SDS‐PAGE. The molecular mass determined by MALDI‐TOF is 40.58 kDa which suggests that the purified enzyme is a monomeric enzyme. Using veratraldehyde as a substrate, the KM, Vmax of TcADD was determined at pH 6.0. Using benzyl alcohol derivatives as substrates, the oxidizing power of TcADD via NAD+ at pH 9.6 was studied.Grant Funding Source: National Science Council of the Republic of China, Taiwan under grant 100‐2313‐B‐019‐003‐MY3
Highlights
Aryl-alcohol dehydrogenases (AADs) have been known to involve in the metabolism of aromatic compounds
Understanding the properties of this TcAAD will be beneficial for its potential in xenobiotic detoxification or production of natural flavors
Cloning and characterization of a cDNA encoding TcAAD A putative TcAAD cDNA clone was identified on the basis of the consensus pattern and sequence homology to the published AADs in NCBI database
Summary
Aryl-alcohol dehydrogenases (AADs) have been known to involve in the metabolism of aromatic compounds. Based on the established EST, several antioxidant enzymes including a superoxide dismutase (Liau et al, 2007), a 1-Cys peroxiredoxin (Wen et al 2007), a catalase (Ken et al, 2008), a glutathione formaldehyde dehydrogenase (Huang et al, 2009), a dithiol glutaredoxin (Ken et al, 2009), a 2-Cys peroxiredoxin isozyme (Liau et al, 2010) and a monothiol glutaredoxin (Ken et al, 2011) have been cloned and characterized This encourages us further to search for active components from the established EST of T. camphorata for potential health food applications
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