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Issue 102, 2016
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Characterization of Cd36_03230p, a putative vanillin dehydrogenase from Candida dubliniensis

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Abstract

A coding sequence (CD36-03230) from the yeast Candida dubliniensis had been previously annotated as a vanillin dehydrogenase (VDH). The corresponding protein (CD36-03230p) was recombinantly expressed in Escherichia coli and analysed. The protein is most likely a tetramer in solution as judged by crosslinking and gel filtration experiments. CD36-03230p is an active aldehyde dehydrogenase favouring cyclic and aromatic substrates. Positive cooperativity and substrate inhibition were observed with some substrates. The redox cofactor NADP+ and substrates affected the thermal stability of the protein. Interestingly, the enzyme had no detectable activity with vanillin suggesting that the annotation is incorrect. It has been previously hypothesized that a methionine residue at a key position in the active site of yeast aldehyde dehydrogenases sterically hinders cyclic substrates and restricts specificity to aliphatic aldehydes. Molecular modeling of CD36-03230p demonstrates that it has an isoleucine residue (Ile-156) at this position, further strengthening this hypothesis.

Graphical abstract: Characterization of Cd36_03230p, a putative vanillin dehydrogenase from Candida dubliniensis

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Publication details

The article was received on 05 Sep 2016, accepted on 10 Oct 2016, published on 14 Oct 2016 and first published online on 14 Oct 2016


Article type: Communication
DOI: 10.1039/C6RA22209A
Citation: RSC Adv., 2016,6, 99774-99780
  • Open access: Creative Commons BY license
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    Characterization of Cd36_03230p, a putative vanillin dehydrogenase from Candida dubliniensis

    S. Datta, U. S. Annapure and D. J. Timson, RSC Adv., 2016, 6, 99774
    DOI: 10.1039/C6RA22209A

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