Cystathionine β-synthase: Difference between revisions
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Full-length CBS contains a C-terminal regulatory domain of ~140 residues, including two so-called 'CBS domains' (CBS1 of 53 residues and CBS2 of 57 residues). The C-terminal domain of CBS contains an autoinhibitory region that gets displaced from the active site upon binding of the allosteric activator AdoMet. | Full-length CBS contains a C-terminal regulatory domain of ~140 residues, including two so-called 'CBS domains' (CBS1 of 53 residues and CBS2 of 57 residues). The C-terminal domain of CBS contains an autoinhibitory region that gets displaced from the active site upon binding of the allosteric activator AdoMet. | ||
The fact that truncated CBS forms dimers rather than tetramers or higher order oligomers suggests that the regulatory domain is involved in tetramer formation. | The fact that truncated CBS forms dimers rather than tetramers or higher order oligomers suggests that the regulatory domain is involved in tetramer formation. | ||
[[Image:Reactions catalyzed by CBS.png]] | [[Image:Reactions catalyzed by CBS.png|400px]] | ||
== Disease == | == Disease == | ||