Unlike in plants, Cystathionine beta-lyase in bacteria exhibits a one-step inhibition mechanism:
Through kinetic methods and X-ray crystallography, a time-dependent, slow-binding inhibition was observed.
It is believed that the inhibitor binds to the enzyme in a similar way as the substrate; however, after the abstraction of the α-proton, the reaction proceeds to create an inactive ketimine PLP derivative.
Unlike in plants, Cystathionine beta-lyase in bacteria exhibits a one-step inhibition mechanism:
Through kinetic methods and X-ray crystallography, a time-dependent, slow-binding inhibition was observed. It is believed that the inhibitor binds to the enzyme in a similar way as the substrate; however, after the abstraction of the α-proton, the reaction proceeds to create an inactive ketimine PLP derivative.
Cystathionine beta-lyase