Allosteric regulation of Bacillus subtilis threonine deaminase, a biosynthetic threonine deaminase with a single regulatory domain.

@article{Shulman2008AllostericRO,
  title={Allosteric regulation of Bacillus subtilis threonine deaminase, a biosynthetic threonine deaminase with a single regulatory domain.},
  author={Anat Shulman and Elena A Zalyapin and M. Vyazmensky and O. Yifrach and Z. Barak and D. Chipman},
  journal={Biochemistry},
  year={2008},
  volume={47 45},
  pages={
          11783-92
        }
}
The enzyme threonine deaminase (TD) is a key regulatory enzyme in the pathway for the biosynthesis of isoleucine. TD is inhibited by its end product, isoleucine, and this effect is countered by valine, the product of a competing biosynthetic pathway. Sequence and structure analyses have revealed that the protomers of many TDs have C-terminal regulatory domains, composed of two ACT-like subdomains, which bind isoleucine and valine, while others have regulatory domains of approximately half the… Expand
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