[HTML][HTML] Cystathionine β-synthase: structure, function, regulation, and location of homocystinuria-causing mutations
EW Miles, JP Kraus - Journal of Biological Chemistry, 2004 - ASBMB
Human CBS is an especially interesting PLP enzyme because it has a complex domain
structure (Fig. 1) and regulatory mechanism. The allosteric activator, S-adenosyl-L-
methionine (AdoMet), increases CBS activity about 3-fold (1) and likely binds to the C-
terminal regulatory domain (2). CBS from higher eukaryotes contains a unique heme moiety
of unknown function (3–5), which is not found in CBS from yeast (Saccharomyces
cerevisiae)(6–8) or from the protozoan hemoflagellate,
structure (Fig. 1) and regulatory mechanism. The allosteric activator, S-adenosyl-L-
methionine (AdoMet), increases CBS activity about 3-fold (1) and likely binds to the C-
terminal regulatory domain (2). CBS from higher eukaryotes contains a unique heme moiety
of unknown function (3–5), which is not found in CBS from yeast (Saccharomyces
cerevisiae)(6–8) or from the protozoan hemoflagellate,