Chemical inhibitors of MANEA exert their effects by targeting various enzymes in the glycosylation process, which is crucial for the proper folding and function of many proteins. Swainsonine, for example, inhibits alpha-mannosidase II, leading to the accumulation of misfolded glycoproteins. This accumulation disrupts the normal functioning of MANEA, as it relies on the precise trimming of mannose residues to properly hydrolyze the alpha-1,6-mannosidic linkages in N-linked glycoproteins. Similarly, Kifunensine targets mannosidase I, which is involved in the initial steps of glycoprotein processing. The inhibition by Kifunensine results in a build-up of high-mannose glycans, which can interfere with MANEA's subsequent actions in the glycosylation pathway. Deoxymannojirimycin and Deoxynojirimycin, both alpha-mannosidase inhibitors, directly compete with the natural substrates of MANEA, leading to a reduction in MANEA's ability to access and process these substrates.
The function of MANEA is further influenced by other inhibitors such as Castanospermine and 1-Deoxynojirimycin, which primarily target beta-glucosidases but also show activity against alpha-glucosidases. These inhibitors can lead to an indirect disruption of the glycosylation process by causing an accumulation of improperly processed glycoproteins. Such accumulation can impede the formation of suitable substrates for MANEA, inhibiting its enzymatic function. Imino sugars, with their broad-spectrum glycosidase inhibition, can similarly compete with MANEA substrates and disrupt its activity. Additionally, Bromoconduritol mimics the structure of MANEA substrates and can competitively inhibit the enzyme by occupying its active site. Acarbose, Voglibose, and Miglitol, all alpha-glucosidase inhibitors, can indirectly affect MANEA by disrupting the normal processing of glycoproteins, leading to an imbalance in the glycan structures necessary for MANEA's function. This disruption results from the inhibitors' capacity to cause an excess of glycoproteins that are not properly processed, which in turn can block the substrate binding site of MANEA, thus inhibiting its activity.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Swainsonine | 72741-87-8 | sc-201362 sc-201362C sc-201362A sc-201362D sc-201362B | 1 mg 2 mg 5 mg 10 mg 25 mg | $138.00 $251.00 $631.00 $815.00 $1832.00 | 6 | |
Swainsonine is an inhibitor of alpha-mannosidase II, an enzyme involved in the trimming of the mannose residues from N-linked glycoproteins in the Golgi apparatus. MANEA is known to be an enzyme with mannosidase activity. By inhibiting alpha-mannosidase II, Swainsonine can lead to the accumulation of misfolded glycoproteins, which could disrupt the glycosylation process where MANEA is involved, leading to its functional inhibition. | ||||||
Kifunensine | 109944-15-2 | sc-201364 sc-201364A sc-201364B sc-201364C | 1 mg 5 mg 10 mg 100 mg | $135.00 $540.00 $1025.00 $6248.00 | 25 | |
Kifunensine is a potent inhibitor of mannosidase I, enzymes that are crucial in the early steps of glycoprotein processing. Since MANEA is involved in the processing of N-linked oligosaccharides in the Golgi, the inhibition of mannosidase I by Kifunensine could cause an accumulation of high-mannose glycans, which may inhibit the downstream function of MANEA by substrate competition or overload. | ||||||
Deoxymannojirimycin hydrochloride | 84444-90-6 | sc-201360 sc-201360A | 1 mg 5 mg | $93.00 $239.00 | 2 | |
Deoxymannojirimycin acts as an inhibitor of alpha-mannosidases, which are key enzymes in the glycosylation pathway. MANEA, being involved in the hydrolysis of the alpha-1,6-mannosidic linkages in N-linked glycoproteins, could have its function inhibited due to the competitive inhibition exerted by Deoxymannojirimycin on the alpha-mannosidases, leading to disruption of the glycosylation process. | ||||||
Deoxynojirimycin | 19130-96-2 | sc-201369 sc-201369A | 1 mg 5 mg | $73.00 $145.00 | ||
Deoxynojirimycin, similar to Deoxymannojirimycin, targets alpha-mannosidases by acting as a competitive inhibitor. The inhibition of these enzymes can affect the glycosylation process, where MANEA is active. This could lead to a reduction in the availability of properly processed glycoprotein substrates for MANEA, thereby inhibiting its enzymatic function. | ||||||
Castanospermine | 79831-76-8 | sc-201358 sc-201358A | 100 mg 500 mg | $184.00 $632.00 | 10 | |
Castanospermine is an inhibitor of beta-glucosidase, but it also shows inhibitory activity against alpha-glucosidases, which can interfere with the glycosylation pathway. By inhibiting glucosidases, Castanospermine may cause an accumulation of glycoproteins with improper oligosaccharides that could indirectly inhibit MANEA's function by impeding proper substrate formation. | ||||||
Acarbose | 56180-94-0 | sc-203492 sc-203492A | 1 g 5 g | $226.00 $605.00 | 1 | |
Acarbose is primarily an inhibitor of alpha-glucosidases, which play a role in carbohydrate digestion. By inhibiting these enzymes, Acarbose can indirectly influence the glycosylation pathway that MANEA is a part of by causing a build-up of glycoproteins that can't be processed, potentially inhibiting the function of MANEA. | ||||||
Voglibose | 83480-29-9 | sc-204384 sc-204384A | 10 mg 50 mg | $198.00 $681.00 | ||
Voglibose is another alpha-glucosidase inhibitor that can indirectly inhibit MANEA by disrupting the normal glycosylation process. The inhibition of alpha-glucosidases could lead to the accumulation of glycoproteins with improper glycan chains, which in turn could prevent MANEA from functioning properly by blocking its substrate binding site. | ||||||
Miglitol | 72432-03-2 | sc-221943 | 10 mg | $161.00 | 1 | |
Miglitol functions as an alpha-glucosidase inhibitor and could similarly indirectly inhibit MANEA by interfering with the glycosylation pathway. | ||||||