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Betaine-Homocysteine S-Methyltransferase is an Abundant Zinc Metalloenzyme in Liver

  • Andrew P. BreksaIII
  • Timothy A. Garrow
Chapter
  • 17 Downloads

Keywords

Inductively Couple Plasma Analysis Zinc METALLOENZYME Methylmethane Thiosulfonate BHMT Activity Abundant Zinc 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Garrow, T.A., 1996, Purification, kinetic properties, and cDNA cloning of mammalian betaine-homocysteine methyltransferase, J. Biol. Chem. 271:22831–22838.CrossRefGoogle Scholar
  2. Goulding, C.W. and Matthews, R.G., 1997, Cobalamin-dependent methionine synthase from Escherichia coli: involvement of zinc in homocysteine activation, Biochemistry 36:15749–15757.CrossRefGoogle Scholar
  3. Millian, N.S. and Garrow, T.A., 1998 Human betaine-homocysteine methyltransferase is a zinc metalloenzyme, Arch. Biochem. Biophys. 356:93–98.CrossRefGoogle Scholar
  4. Peariso, K., Goulding, C.W, Huang, S., Matthews, R.G., and Pennerhahn J.E., 1998, Characterization of the zinc binding site in methionine synthase enzymes of Escherichia coli: the role of zinc in the methylation of homocysteine, J. Amer. Chem. Soc. 120:8410–8416.CrossRefGoogle Scholar

Copyright information

© Kluwer Academic Publishers 2002

Authors and Affiliations

  • Andrew P. BreksaIII
    • 1
  • Timothy A. Garrow
    • 1
  1. 1.Department of Food Science and Human NutritionUniversity of IllinoisUrbanaUSA

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