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Structural basis for substrate activation and regulation by cystathionine beta-synthase (CBS) domains in cystathionine [beta]-synthase.(BIOCHEMISTRY)(Author abstract)(Report)

Koutmos, Markos ; Kabil, Omer ; Smith, Janet L. ; Banerjee, Ruma

Proceedings of the National Academy of Sciences of the United States, Dec 7, 2010, Vol.107(49), p.20958(6) [Tạp chí có phản biện]

ISSN: 0027-8424

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  • Nhan đề:
    Structural basis for substrate activation and regulation by cystathionine beta-synthase (CBS) domains in cystathionine [beta]-synthase.(BIOCHEMISTRY)(Author abstract)(Report)
  • Tác giả: Koutmos, Markos ; Kabil, Omer ; Smith, Janet L. ; Banerjee, Ruma
  • Chủ đề: Substitution Reactions -- Research ; Cysteine -- Chemical Properties ; Homocysteine -- Chemical Properties
  • Là 1 phần của: Proceedings of the National Academy of Sciences of the United States, Dec 7, 2010, Vol.107(49), p.20958(6)
  • Mô tả: The catalytic potential for [H.sub.2]S biogenesis and homocysteine clearance converge at the active site of cystathionine [beta]-synthase (CBS), a pyridoxal phosphate-dependent enzyme. CBS catalyzes [beta]-replacement reactions of either serine or cysteine by homocysteine to give cystathionine and water or [H.sub.2]S, respectively. In this study, high-resolution structures of the full-length enzyme from Drosophila in which a carbanion (1.70 [Angstrom]) and an aminoacrylate intermediate (1.55 [Angstrom]) have been captured are reported. Electrostatic stabilization of the zwitterionic carbanion intermediate is afforded by the close positioning of an active site lysine residue that is initially used for Schiff base formation in the internal aldimine and later as a general base. Additional stabilizing interactions between active site residues and the catalytic intermediates are observed. Furthermore, the structure of the regulatory "energy-sensing" CBS domains, named after this protein, suggests a mechanism for allosteric activation by S-adenosylmethionine. crystallography | hydrogen sulfide doi/ 10.1073/pnas.1011448107
  • Ngôn ngữ: English
  • Số nhận dạng: ISSN: 0027-8424

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