Figure 6: Schematic diagram of redox-switch modulation of CaTHL.
From: Redox-switch regulatory mechanism of thiolase from Clostridium acetobutylicum
CaTHL catalyses the condensation reaction of acetyl-CoA to acetoacetyl-CoA. In an oxidized status, two catalytic cysteine residues, Cys88 and Cys378, are oxidized forming a disulfide bond, leading to the enzyme inactive and eventually the blockage of the C4 metabolites (n-butanol and butyric acid) biosynthesis. When the environment is switched to a reduced status, the disulfide bond is broken and thiol groups of two catalytic residues form an active site environment, enabling the C4 metabolites (n-butanol and butyric acid) biosynthesis.
