Regulation of human cystathionine beta-synthase by S-adenosyl-L-methionine: evidence for two catalytically active conformations involving an autoinhibitory domain in the C-terminal region.

@article{Jnok2001RegulationOH,
  title={Regulation of human cystathionine beta-synthase by S-adenosyl-L-methionine: evidence for two catalytically active conformations involving an autoinhibitory domain in the C-terminal region.},
  author={Miroslav J{\'a}no{\vs}{\'i}k and Vladim{\'i}r Kery and Mette Gaustadnes and Kenneth N. Maclean and Jan P Kraus},
  journal={Biochemistry},
  year={2001},
  volume={40 35},
  pages={
          10625-33
        }
}
Cystathionine beta-synthase (CBS), condensing homocysteine and serine, represents a key regulatory point in the biosynthesis of cysteine via the transsulfuration pathway. Inherited deficiency of CBS causes homocystinuria. CBS is activated by S-adenosyl-L-methionine (AdoMet) by inducing a conformational change involving a noncatalytic C-terminal region spanning residues 414-551. We report the purification of two patient-derived C-terminal mutant forms of CBS, S466L and I435T, that provide new… CONTINUE READING
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