Article

Planta

, Volume 208, Issue 1, pp 12-18

First online:

Maize glutathione-dependent formaldehyde dehydrogenase: protein sequence and catalytic properties

  • Ulrike WippermannAffiliated withGSF-Forschungszentrum für Umwelt und Gesundheit, Institut für Biochemische Pflanzenpathologie, Ingolstädter Landstraße 1, D-85764 Oberschleißheim, Germany
  • , Judith FliegmannAffiliated withGSF-Forschungszentrum für Umwelt und Gesundheit, Institut für Biochemische Pflanzenpathologie, Ingolstädter Landstraße 1, D-85764 Oberschleißheim, Germany
  • , Guy BauwAffiliated withLaboratorium voor Genetica, via the Department of Genetics, affiliated to the Flanders Interuniversity Institute for Biotechnology, Universiteit Gent, B-9000 Gent, Belgium
  • , Christian LangebartelsAffiliated withGSF-Forschungszentrum für Umwelt und Gesundheit, Institut für Biochemische Pflanzenpathologie, Ingolstädter Landstraße 1, D-85764 Oberschleißheim, Germany
  • , Konrad MaierAffiliated withGSF-Forschungszentrum für Umwelt und Gesundheit, Institut für Inhalationsbiologie, Ingolstädter Landstraße 1, D-85764 Oberschleißheim, Germany
  • , Heinrich SandermannAffiliated withGSF-Forschungszentrum für Umwelt und Gesundheit, Institut für Biochemische Pflanzenpathologie, Ingolstädter Landstraße 1, D-85764 Oberschleißheim, Germany

Rent the article at a discount

Rent now

* Final gross prices may vary according to local VAT.

Get Access

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.

Key words: Detoxification of formaldehyde Formal- dehyde dehydrogenase (glutathione-dependent) Protein sequence Zea (formaldehyde dehydrogenase)