BEC hydrochlorideBEC hydrochloride
MedChemExpress (MCE)
HY-19548A
222638-67-7
98.0%
4°C, stored under nitrogen *In solvent : -80°C, 6 months
-20°C, 1 month (stored under nitrogen)
Room temperature in continental US
may vary elsewhere.
BEC hydrochloride is a slow-binding and competitive Arginase II inhibitor with Ki of 0.31 μM and 30 nM at pH 7.5 and pH 9.5, respectively.
The X-ray crystal structure of the arginase-BEC complex has been determined at 2.3 Å resolution from crystals perfectly twinned by hemihedry. The structure of the complex reveals that the boronic acid moiety undergoes nucleophilic attack by metal-bridging hydroxide ion to yield a tetrahedral boronate anion that bridges the binuclear manganese cluster, thereby mimicking the tetrahedral intermediate (and its flanking transition states) in the arginine hydrolysis reaction[2].
Administration of the arginase inhibitor BEC decreases arginase activity and causes alterations in NO homeostasis, which are reflected by increases in S-nitrosylated and nitrated proteins in the lungs from inflamed mice. BEC enhances perivascular and peribronchiolar lung inflammation, mucus metaplasia, NF-κB DNA binding, and mRNA expression of the NF-κB-driven chemokine genes CCL20 and KC, and leads to further increases in airways hyperresponsiveness[3].
Ki: 0.31 μM (BEC hydrochloride, at pH 7.5) and 30 nM (BEC hydrochloride, at pH 9.5)[1] In Vitro The X-ray crystal structure of the arginase-BEC complex has been determined at 2.3 Å resolution from crystals perfectly twinned by hemihedry. The structure of the complex reveals that the boronic acid moiety undergoes nucleophilic attack by metal-bridging hydroxide ion to yield a tetrahedral boronate anion that bridges the binuclear manganese cluster, thereby mimicking the tetrahedral intermediate (and its flanking transition states) in the arginine hydrolysis reaction[2]. MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only. 0 --> BEC hydrochloride Related Antibodies
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[1]. Colleluori DM, et al. Classical and slow-binding inhibitors of human type II arginase. Biochemistry. 2001 Aug 7
40(31):9356-62. [Content Brief]
[2]. Kim NN, 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. Biochemistry. 2001 Mar 6
40(9):2678-88. [Content Brief]
[3]. Ckless K, et al. Inhibition of arginase activity enhances inflammation in mice with allergic airway disease, in association with increases in protein S-nitrosylation and tyrosine nitration. J Immunol. 2008 Sep 15
181(6):4255-64. [Content Brief]