On singular or dual positional specificity of lipoxygenases. The number of chiral products varies with alignment of methylene groups at the active site of the enzyme.

@article{Khn1990OnSO,
  title={On singular or dual positional specificity of lipoxygenases. The number of chiral products varies with alignment of methylene groups at the active site of the enzyme.},
  author={Hartmut K{\"u}hn and Howard W. Sprecher and AlanR. Brash},
  journal={The Journal of biological chemistry},
  year={1990},
  volume={265 27},
  pages={
          16300-5
        }
}
We tested a simple model which explains the singular or dual specificity of lipoxygenases. The dual specificity considered here is typified by the oxygenation of arachidonic acid by the reticulocyte lipoxygenase: two chiral products are formed (12S- and 15S-hydroperoxides, ratio approximately 1:9) via hydrogen abstraction from two separate methylene groups (C-10 and C-13). The rate-limiting step is known to involve this hydrogen abstraction, and we assumed that alignment of the methylenes with… CONTINUE READING

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