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

(1999) PLANTA. 208(1). p.12-18
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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 mu mol (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, Slant Mol Biol 34: 843-854). There was 62% identity with the eucaryotic FDH consensus sequence. Michaelis constants of approx. 20 mu m (formaldehyde), approx; 50 mu m (glutathione) and approx. 31 mu m (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 omega-hydroxy-fatty 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.
Keywords
formaldehyde dehydrogenase (glutathione-dependent), detoxification of formaldehyde, protein sequence, Zea (formaldehyde dehydrogenase), III ALCOHOL-DEHYDROGENASE, PLANT-METABOLISM, MOLECULAR ANALYSIS, CLASS-P, CLASS-I, LIVER, GENE, DETOXIFICATION, CHROMATOGRAPHY, PURIFICATION

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Citation

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Chicago
Wipperman, Ulrike, Judith Fliegmann, Guy Bauw, Christian Langebartels, Konrad Maier, and Heinrich Sandermann Jr. 1999. “Maize Glutathione-dependent Formaldehyde Dehydrogenase: Protein Sequence and Catalytic Properties.” Planta 208 (1): 12–18.
APA
Wipperman, U., Fliegmann, J., Bauw, G., Langebartels, C., Maier, K., & Sandermann, H., Jr. (1999). Maize glutathione-dependent formaldehyde dehydrogenase: protein sequence and catalytic properties. PLANTA, 208(1), 12–18.
Vancouver
1.
Wipperman U, Fliegmann J, Bauw G, Langebartels C, Maier K, Sandermann H Jr. Maize glutathione-dependent formaldehyde dehydrogenase: protein sequence and catalytic properties. PLANTA. 1999;208(1):12–8.
MLA
Wipperman, Ulrike, Judith Fliegmann, Guy Bauw, et al. “Maize Glutathione-dependent Formaldehyde Dehydrogenase: Protein Sequence and Catalytic Properties.” PLANTA 208.1 (1999): 12–18. Print.
@article{173540,
  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 mu mol (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, Slant Mol Biol 34: 843-854). There was 62% identity with the eucaryotic FDH consensus sequence. Michaelis constants of approx. 20 mu m (formaldehyde), approx; 50 mu m (glutathione) and approx. 31 mu m (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 omega-hydroxy-fatty 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.},
  author       = {Wipperman, Ulrike and Fliegmann, Judith and Bauw, Guy and Langebartels, Christian and Maier, Konrad and Sandermann, Heinrich, Jr.},
  issn         = {0032-0935},
  journal      = {PLANTA},
  keywords     = {formaldehyde dehydrogenase (glutathione-dependent),detoxification of formaldehyde,protein sequence,Zea (formaldehyde dehydrogenase),III ALCOHOL-DEHYDROGENASE,PLANT-METABOLISM,MOLECULAR ANALYSIS,CLASS-P,CLASS-I,LIVER,GENE,DETOXIFICATION,CHROMATOGRAPHY,PURIFICATION},
  language     = {eng},
  number       = {1},
  pages        = {12--18},
  title        = {Maize glutathione-dependent formaldehyde dehydrogenase: protein sequence and catalytic properties},
  url          = {http://dx.doi.org/10.1007/s004250050529},
  volume       = {208},
  year         = {1999},
}

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