Publikation: Purification and some properties of (1R,2S)-1,2-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate dehydrogenase from Comamonas testosteroni T-2
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1995
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FEMS Microbiology Letters. 1995, 130(1), pp. 97-102. ISSN 0378-1097. eISSN 1574-6968. Available under: doi: 10.1111/j.1574-6968.1995.tb07705.x
Zusammenfassung
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+.
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Fachgebiet (DDC)
570 Biowissenschaften, Biologie
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Terephthalate, Diene-diol dehydrogenase, Enzyme purification, Comamonas testosteroni T-2, Biodegradation
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SALLER, Elisabeth, Heike LAUE, Hans Rudolf SCHLÄFLI OPPENBERG, Alasdair M. COOK, 1995. Purification and some properties of (1R,2S)-1,2-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate dehydrogenase from Comamonas testosteroni T-2. In: FEMS Microbiology Letters. 1995, 130(1), pp. 97-102. ISSN 0378-1097. eISSN 1574-6968. Available under: doi: 10.1111/j.1574-6968.1995.tb07705.xBibTex
@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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<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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