BEC is a potent slow-binding competitive inhibitor of recombinant rat liver arginase I (Ki = 0.4-0.6 μM), as well as human arginase II (Ki = 0.31 μM and 30 nM at pH 7.5 and 9.5, respectively), though it does not inhibit murine iNOS at concentrations up to 1 mM. BEC significantly enhances NO-dependent relaxation of human penile corpus canvernosum smooth muscle in vitro at concentrations between 0.1-1.0 mM. L-Arginine serves as a common substrate for both nitric oxide synthase (NOS) and arginase in the cell. NOS catalyzes the oxidation of arginine to citrulline and NO with Nω-hydroxy-L-arginine (NOHA) formed as an intermediate. Arginase, on the other hand, catalyzes the hydrolysis of arginine into urea and L-ornithine.
1. Kim, N N., et al., 2001. Probing erectile function: S-(2-boronoethyl)-L-cysteine binds to arginase as a transition state analogue and enhances smooth muscle relaxation in human penile corpus cavernosum. Biochemistry. 40(9): 2678-88. PMID: 11258879
2. Colleluori, D M., et al., 2001. Classical and slow-binding inhibitors of human type II arginase. Biochemistry. 40(31): 9356-62. PMID: 11478904
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