ASS1 Inhibitors
The chemical class of ASS1 inhibitors comprises a diverse array of compounds with distinct mechanisms of action that directly or indirectly modulate the activity of argininosuccinate synthase 1 (ASS1). These inhibitors play crucial roles in influencing the urea cycle, a fundamental metabolic pathway responsible for ammonia detoxification and arginine biosynthesis. The identified chemicals act through various strategies, such as competitive inhibition, biomechanical interference, and modulation of the microenvironment. Competitive inhibitors, including NOHA, ADMA, and L-Canavanine, obstruct the active site of ASS1 by competing with the natural substrate, L-arginine, thereby impeding the catalytic process of citrulline and aspartate synthesis. This direct interference with substrate binding exemplifies a mechanism through which these inhibitors can modulate ASS1 activity. Biomechanical modulators, like 2,3-Butanedione Monoxime (BDM), exert their inhibitory effects by altering the biomechanical properties of ASS1. In tissues where contractile elements are relevant, BDM impacts the enzyme's activity, showcasing an indirect mechanism of inhibition.
Several inhibitors, such as Arginase Inhibitors (e.g., BEC) and S-Methylisothiourea (SMTU), act indirectly by influencing the nitric oxide synthesis pathway. By inhibiting arginase or specific isoforms of nitric oxide synthase, these compounds disrupt the physiological feedback mechanisms regulating ASS1, resulting in altered enzyme activity. GMP and Dicarboxylic Acids operate through indirect mechanisms involving modulation of N-acetylglutamate levels and the microenvironment around ASS1, respectively. These compounds exemplify how diverse biochemical processes can be targeted to influence ASS1 activity. In summary, the chemical class of ASS1 inhibitors demonstrates a sophisticated interplay of compounds that can selectively and specifically modulate the activity of this key enzyme in nitrogen metabolism. The identified inhibitors offer valuable tools for dissecting the intricacies of the urea cycle and insight into disorders associated with arginine metabolism.
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
L-Arginine | 74-79-3 | sc-391657B sc-391657 sc-391657A sc-391657C sc-391657D | 5 g 25 g 100 g 500 g 1 kg | $20.00 $31.00 $61.00 $219.00 $352.00 | 2 | |
N G-Nitro-L-arginine (L-NNA) inhibits ASS1 by serving as a non-selective nitric oxide synthase (NOS) inhibitor. By blocking NOS activity, L-NNA indirectly inhibits ASS1, as nitric oxide is a product of ASS1-catalyzed reactions. This indirect inhibition involves L-NNA preventing the synthesis of nitric oxide, which, in turn, impacts the physiological feedback mechanisms regulating ASS1 activity. | ||||||
Mtr-S-methylisothiourea | 185674-97-9 | sc-286319 sc-286319A | 1 g 5 g | $132.00 $539.00 | ||
SMTU inhibits ASS1 by serving as a selective nitric oxide synthase (NOS) inhibitor. By specifically inhibiting inducible NOS (iNOS), SMTU indirectly inhibits ASS1, as nitric oxide is a product of ASS1-catalyzed reactions. This indirect inhibition involves SMTU preventing the synthesis of nitric oxide, impacting the physiological feedback mechanisms regulating ASS1 activity. | ||||||
2,3-Butanedione 2-Monoxime | 57-71-6 | sc-203774 sc-203774A sc-203774B sc-203774C | 25 g 100 g 250 g 500 g | $42.00 $78.00 $161.00 $286.00 | ||
2,3-Butanedione monoxime (BDM) inhibits ASS1 by affecting the biomechanical properties of the enzyme. BDM interferes with the contractile apparatus of smooth muscle, leading to the inhibition of ASS1 activity in tissues where contractile elements play a role in enzyme modulation. This indirect inhibition involves BDM modulating the biomechanical properties of ASS1, leading to changes in enzyme activity in tissues with contractile elements. | ||||||
Guanosine-5′-monophosphate | 85-32-5 | sc-295032 sc-295032A sc-295032B | 1 g 2.5 g 5 g | $322.00 $622.00 $1051.00 | 5 | |
Guanosine monophosphate (GMP) inhibits ASS1 by promoting the degradation of N-acetylglutamate, a cofactor for ASS1. GMP stimulates the activity of N-acetylglutamate synthase, which converts N-acetylglutamate to citrulline, leading to a reduction in ASS1 activity. This indirect inhibition involves GMP influencing the levels of N-acetylglutamate, impacting ASS1 activity and contributing to the modulation of the urea cycle. | ||||||
L-Canavanine | 543-38-4 | sc-364687 sc-364687A | 250 mg 1 g | $228.00 $666.00 | ||
L-Canavanine inhibits ASS1 by acting as a competitive inhibitor of L-arginine. L-Canavanine competes with L-arginine for binding to ASS1, blocking the active site and preventing the synthesis of citrulline and aspartate in the urea cycle. This direct inhibition involves L-Canavanine interfering with the substrate binding of L-arginine to ASS1, leading to a reduction in the enzyme's catalytic activity and modulation of the urea cycle. | ||||||
Guanidinoacetic Acid | 352-97-6 | sc-211571 sc-211571A sc-211571B | 25 mg 1 g 5 g | $169.00 $221.00 $278.00 | ||
Guanidinoacetic acid (GAA) inhibits ASS1 by serving as a substrate analog. GAA competes with L-arginine for binding to ASS1, blocking the active site and preventing the synthesis of citrulline and aspartate in the urea cycle. This direct inhibition involves GAA interfering with the substrate binding of L-arginine to ASS1, leading to a reduction in the enzyme's catalytic activity and modulation of the urea cycle. | ||||||