Cross-Talk between the Catalytic Core and the Regulatory Domain in Cystathionine β-Synthase: Study by Differential Covalent Labeling and Computational Modeling†

@inproceedings{Hnzda2010CrossTalkBT,
  title={Cross-Talk between the Catalytic Core and the Regulatory Domain in Cystathionine β-Synthase: Study by Differential Covalent Labeling and Computational Modeling†},
  author={Ale{\vs} Hn{\'i}zda and Vojtěch Spiwok and Vojtěch Jurga and V. Kozich and Milan Kod{\'i}{\vc}ek and Jan P Kraus},
  booktitle={Biochemistry},
  year={2010}
}
Cystathionine β-synthase (CBS) is a modular enzyme which catalyzes condensation of serine with homocysteine. Cross-talk between the catalytic core and the C-terminal regulatory domain modulates the enzyme activity. The regulatory domain imposes an autoinhibition action that is alleviated by S-adenosyl-l-methionine (AdoMet) binding, by deletion of the C-terminal regulatory module, or by thermal activation. The atomic mechanisms of the CBS allostery have not yet been sufficiently explained. Using… CONTINUE READING

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