Purification, Kinetic Properties, and cDNA Cloning of Mammalian Betaine-Homocysteine Methyltransferase*

@article{Garrow1996PurificationKP,
  title={Purification, Kinetic Properties, and cDNA Cloning of Mammalian Betaine-Homocysteine Methyltransferase*},
  author={T. Garrow},
  journal={The Journal of Biological Chemistry},
  year={1996},
  volume={271},
  pages={22831 - 22838}
}
  • T. Garrow
  • Published 1996
  • Biology, Medicine
  • The Journal of Biological Chemistry
  • Porcine liver betaine-homocysteine methyltransferase (BHMT; EC) was purified to homogeneity, and the Michaelis constants for betaine, dimethylacetothetin, and L-homocysteine are 23, 155, and 32 μM, respectively. The maximum rate of catalysis is 47-fold greater using dimethylacetothetin as a methyl donor compared with betaine. Partial amino acid sequence of porcine BHMT was obtained, and inosine-containing redundant oligonucleotide primers were used to amplify an 815-base pair sequence of the… CONTINUE READING
    211 Citations
    Human Methionine Synthase
    • 176
    • PDF
    Betaine-Homocysteine S-Methyltransferase is an Abundant Zinc Metalloenzyme in Liver
    Purification and Kinetic Properties of Betaine-Homocysteine Methyltransferase from Aphanothece halophytica
    • 12
    • Highly Influenced
    Human betaine-homocysteine methyltransferase is a zinc metalloenzyme.
    • 138

    References

    SHOWING 1-10 OF 47 REFERENCES
    Methionine metabolism in mammals: kinetic study of betaine-homocysteine methyltransferase.
    • 108
    Methionine metabolism in mammals. Distribution of homocysteine between competing pathways.
    • 353
    • PDF