Maize glutathione-dependent formaldehyde dehydrogenase: protein sequence and catalytic properties |
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Authors: | Ulrike Wippermann Judith Fliegmann Guy Bauw Christian Langebartels Konrad Maier Heinrich Sandermann |
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Institution: | GSF-Forschungszentrum für Umwelt und Gesundheit, Institut für Biochemische Pflanzenpathologie, Oberschleissheim, Germany. |
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Abstract: | Glutathione-dependent formaldehyde dehydrogenase (FDH; EC 1.2.1.1) has been purified 3900-fold from maize cell-suspension
cultures to a specific activity of 4.68 μmol (mg protein)−1 min−1. The homogeneous enzyme consisted of two identical subunits with a molecular mass of 42 kDa, and an isoelectric point of
5.8. Eight tryptic peptides were sequenced and gave a perfect fit to the protein sequence derived from maize Fdh cDNA (J. Fliegmann and H. Sandermann, 1997, Plant Mol Biol 34: 843–854). There was 62% identity with the eucaryotic FDH consensus
sequence. Michaelis constants of approx. 20 μm (formaldehyde), approx. 50 μm (glutathione) and approx. 31 μm (NAD+) were determined for the maize enzyme as well as for FDH partially purified from dog lung. Besides S-hydroxymethylglutathione, pentanol-1, octanol-1, and ω-hydroxyfatty acids served as substrates for both FDH preparations.
The unusual substrate specificity indicates that FDH may be involved in the detoxification of long-chain lipid peroxidation
products.
Received: 1 April 1998 / Accepted: 18 November 1998 |
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Keywords: | : Detoxification of formaldehyde Formal- dehyde dehydrogenase (glutathione-dependent) Protein sequence Zea (formaldehyde dehydrogenase) |
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