@article{Saller1995Purif-8655,
  year={1995},
  doi={10.1111/j.1574-6968.1995.tb07705.x},
  title={Purification and some properties of (1R,2S)-1,2-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate dehydrogenase from Comamonas testosteroni T-2},
  number={1},
  volume={130},
  issn={0378-1097},
  journal={FEMS Microbiology Letters},
  pages={97--102},
  author={Saller, Elisabeth and Laue, Heike and Schläfli Oppenberg, Hans Rudolf and Cook, Alasdair M.}
}

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    <dc:contributor>Schläfli Oppenberg, Hans Rudolf</dc:contributor>
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    <dcterms:title>Purification and some properties of (1R,2S)-1,2-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate dehydrogenase from Comamonas testosteroni T-2</dcterms:title>
    <dcterms:abstract xml:lang="eng">AbstractInducible (1R,2S)-1,2-dihydroxy-3,5-cyclohexadiene-l,4-dicarboxylate (diene-diol) dehydrogenase was found in extracts of Comamonas testosteroni T-2 grown in p-toluate-or terephthalate-salts medium and it was purified using anion exchange, hydrophobic interaction and gel filtration chromatography. The enzyme is a homodimer with subunit Mr 39000. It had a specific activity of 500 mkat/kg of protein and was activated by the addition of Fe2+. The dehydrogenase converted 1 mol diene-diol and 1 mol NAD+ to 1 mol protocatechuic acid, 1 mol NADH and 1 mol CO2. Apparent Km-values of 43 µM (NAD+) and about 90 µM (diene-diol) were determined. The hydride ion was transferred to the si face of NAD+.</dcterms:abstract>
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    <dc:contributor>Cook, Alasdair M.</dc:contributor>
    <dc:contributor>Saller, Elisabeth</dc:contributor>
    <dc:creator>Laue, Heike</dc:creator>
    <dc:language>eng</dc:language>
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    <dcterms:bibliographicCitation>First publ. in: FEMS Microbiology Letters 130 (1995), 1, pp. 97-102</dcterms:bibliographicCitation>
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    <dcterms:issued>1995</dcterms:issued>
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    <dc:creator>Schläfli Oppenberg, Hans Rudolf</dc:creator>
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    <dc:contributor>Laue, Heike</dc:contributor>
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    <dc:creator>Saller, Elisabeth</dc:creator>
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    <dc:creator>Cook, Alasdair M.</dc:creator>
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