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    Candida albicans SOU1 encodes a sorbose reductase required for L-sorbose Utilization

    Access Status
    Fulltext not available
    Authors
    Greenberg, J.
    Price, N.
    Oliver, Richard
    Sherman, F.
    Rustchenko, E.
    Date
    2005
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Greenberg JR, Price NP, Oliver RP, Sherman F, & Rustchenko E. (2005) Candida albicans SOU1 encodes a sorbose reductase required for L-sorbose Utilization. Yeast. 22, 957-969
    DOI
    10.1002/yea.1282
    Faculty
    Department of Environmental & Agriculture
    School of Agriculture and Environment
    Faculty of Science and Engineering
    Remarks

    A copy of this item may be available from Professor Richard Oliver

    Email: Richard.oliver@curtin.edu.au

    URI
    http://hdl.handle.net/20.500.11937/17830
    Collection
    • Curtin Research Publications
    Abstract

    Previous work in our laboratory showed that L-sorbose utilization in Candida albicans is subject to a novel form of regulation which involves a reversible increase or decrease in the copy number of chromosome 5. Furthermore, the structural gene SOU1 is required for L-sorbose utilization and encodes a member of the short chain dehydrogenase family. However, the precise function of SOU1 was not known and neither was the pathway for L-sorbose utilization. We have now expressed SOU1 at a high level from a replicative plasmid having a constitutive ADH1 promoter and purified a version of Sou1p tagged with the FLAG epitope at the N-terminus. Sou1FLAGNp has a sorbose reductase activity which utilizes NADPH as a co-factor and converts L-sorbose to D-sorbitol. It can also less efficiently utilize fructose as a substrate with NADPH as a co-factor, converting fructose to mannitol. In agreement with prediction, the purified enzyme has a subunit molecular weight of 31 kDa and a pI of about 4.8. It probably consists of four identical subunits and has a pH optimum of 6.2. The L-sorbose utilization pathway in C. albicans probably converts L-sorbose to fructose-6-phosphate via D-sorbitol as an intermediate. The first step is catalysed by Sou1p. We also found that C. albicans extracts have a D-sorbitol-6-phosphate dehydrogenase activity, not encoded by SOU1, which utilizes NADP as a co-factor. This activity has not been described previously in yeasts and may be involved in the conversion of phosphorylated D-sorbitol to fructose-6-phosphate or glucose-6-phosphate.

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