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. BEC is a potent slow-binding competitive inhibitor of recombinant rat liver arginase I with a Ki of 0.4-0.6 µM.1 It is also a potent inhibitor of human arginase II with Ki values of 0.31 µM and 30 nM at pH 7.5 and 9.5, respectively.2 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.1
1
Kim, N.N., Cox, J.D., Baggio, R.F., et al. 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. Biochemistry402678-2688(2001).
2
Colleluori, D.M., and Ash, D.E. Classical and slow-binding inhibitors of human type II arginase. Biochemistry409356-9362(2001).
Formal Name
S-(2-boronoethyl)-L-cysteine
CAS Number
63107-40-4
Molecular Formula
C5H12BNO4S
Formula Weight
193.0
Formulation
A crystalline solid
Purity
>98%
Stability
2 years
Storage
-20°C
Shipping
Wet ice
in continental US; may vary elsewhere
SMILES
Copy SMILES to clipboard
OB(O)CCSCC(N)C(=O)O
Background Reading
Kim, N.N., Cox, J.D., Baggio, R.F., et al. 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. Biochemistry402678-2688(2001).
Colleluori, D.M., and Ash, D.E. Classical and slow-binding inhibitors of human type II arginase. Biochemistry409356-9362(2001).
BEC is available in the following screening
library: