Two polymorphic forms of human histamine methyltransferase: structural, thermal, and kinetic comparisons.

@article{Horton2001TwoPF,
  title={Two polymorphic forms of human histamine methyltransferase: structural, thermal, and kinetic comparisons.},
  author={John R. Horton and K Sawada and Maiko Nishibori and Xing Zhang and Xiaodong Cheng},
  journal={Structure},
  year={2001},
  volume={9 9},
  pages={837-49}
}
BACKGROUND Histamine plays important biological roles in cell-to-cell communication; it is a mediator in allergic responses, a regulator of gastric acid secretion, a messenger in bronchial asthma, and a neurotransmitter in the central nervous system. Histamine acts by binding to histamine receptors, and its local action is terminated primarily by methylation. Human histamine N-methyltransferase (HNMT) has a common polymorphism at residue 105 that correlates with the high- (Thr) and low- (Ile… CONTINUE READING
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