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  • Title: Structural insights into pathogenic mutations in heme-dependent cystathionine-beta-synthase.
    Author: Yamanishi M, Kabil O, Sen S, Banerjee R.
    Journal: J Inorg Biochem; 2006 Dec; 100(12):1988-95. PubMed ID: 17069888.
    Abstract:
    Human cystathionine beta-synthase plays a key role in maintaining low intracellular levels of homocysteine and is unique in being a pyridoxal phosphate-dependent enzyme that is a hemeprotein. It catalyzes the beta-replacement of serine and homocysteine to generate the condensation product, cystathionine. While the structure of a truncated catalytic core of the protein has been determined by crystallography, a model for the full-length enzyme has been developed guided by hydrogen-deuterium exchange mass spectrometric and docking studies. In this review, we have utilized the available structural models for human cystathionine beta-synthase to conduct a structure-function analysis of a select group of pathogenic mutations described in patients with hereditary hyperhomocysteinemia.
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