S-(3-Carboxypropyl)-L-cysteine

S-(3-Carboxypropyl)-L-cysteine (CPC) (71 μM; 3 min) potently and selectively inhibits recombinant human CSE in a cystathionine cleavage assay, with an IC₅₀ of 71 μM, while sparing other H₂S biogenesis enzymes (CBS, MST, CAT)^[1].
S-(3-Carboxypropyl)-L-cysteine (30-150 μM; 3 min) acts as a competitive inhibitor of recombinant human CSE, with higher affinity for the cystathionine cleavage reaction (K_i = 50 μM) than the cysteine-dependent H₂S synthesis reaction (K_i = 180 μM), and effectively inhibits H₂S synthesis even when added simultaneously with cysteine^[1].
S-(3-Carboxypropyl)-L-cysteine (1.0 mM) binds to recombinant human CSE with a K_d of 26 μM, in a primarily enthalpically driven interaction^[1].
S-(3-Carboxypropyl)-L-cysteine (5 mM) forms a stable aminoacrylate intermediate in the active site of recombinant human CSE, inducing a closed active-site conformation with a well-ordered N-terminal loop, as observed in the 2.5 Å resolution crystal structure^[1].
S-(3-Carboxypropyl)-L-cysteine (CPC) (0.5-10 mM; 17 h) inhibits transsulfuration flux by 80-90% at 5 mM in cultured HepG2, HEK293, and SH-SY5Y cells after 17 h, with complete inhibition achieved at 6 mM in HepG2 cells after 10 h^[1].

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