Glycine N‐methyltransferases: A comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes

@article{Pakhomova2004GlycineNA,
  title={Glycine N‐methyltransferases: A comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes},
  author={Svetlana Pakhomova and Zigmund Luka and Steffi Grohmann and Conrad Wagner and Marcia E. Newcomer},
  journal={Proteins: Structure},
  year={2004},
  volume={57}
}
Glycine N‐methyltransferases (GNMTs) from three mammalian sources were compared with respect to their crystal structures and kinetic parameters. The crystal structure for the rat enzyme was published previously. Human and mouse GNMT were expressed in Escherichia coli in order to determine their crystal structures. Mouse GNMT was crystallized in two crystal forms, a monoclinic form and a tetragonal form. Comparison of the three structures reveals subtle differences, which may relate to the… 
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TLDR
This minireview will focus on the latest discoveries in the elucidation of the mechanism of that regulation of S-adenosylmethionine in mammals.
Methyltetrahydrofolate in folate-binding protein glycine N-methyltransferase.
  • Z. Luka
  • Biology, Medicine
    Vitamins and hormones
  • 2008
TLDR
The crystal structure of GNMT complexed with 5-CH(3)-THF revealed that there are two folate molecules bound to one tetrameric form ofGNMT, which is a basis for establishing of mechanism of inhibition of GN MT.
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TLDR
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