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  • Title: Purification and characterization of cytoplasmic NAD-dependent polypropylene glycol dehydrogenase from Stenotrophomonas maltophilia.
    Author: Tachibana S, Naka N, Kawai F, Yasuda M.
    Journal: FEMS Microbiol Lett; 2008 Nov; 288(2):266-72. PubMed ID: 19054086.
    Abstract:
    The oxidizing enzyme NAD(+)-dependent polypropylene glycol dehydrogenase (PPG-DH) was purified to homogeneity from the cytoplasmic fraction of Stenotrophomonas maltophilia grown on polypropylene glycol (diol type) 2000. The purified enzyme consisted of a homotetrameric protein (37 kDa subunit) with a molecular mass of around 154 kDa. The N-terminal amino acid sequence (25 residues) showed similarity to the sequences of NAD(+)-dependent secondary alcohol dehydrogenases and NADH-dependent reductases. The enzyme preferentially oxidized medium-chain secondary alcohols, di- and tri-propylene glycols and polypropylene glycols including those with secondary alcohol groups in their molecular structure. Consequently, the enzyme was classified into a group of NAD(+)-dependent secondary alcohol dehydrogenases.
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