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CO inhibition of CBS. CO binds to the heme prosthetic group in the active form of CBS, leading to the release of the thiolate of Cys52 followed by protonating and breaking the salt bridge of Arg266. Consequently, the orientations of the helix domain and the PLP cofactor change in favor of the inactive enolimine tautomer. Therefore, the catalytic activity is inhibited upon CO binding.
