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It is defined as "catalysis of the hydrolysis of terminal, non-reducing alpha-linked alpha-D-glucose residue with release of alpha-D-glucose." In this sense, "alpha-glucosidase" can encompass a wide range of enzyme activitiess, differing by the linkage of their terminal (1→3, 1→4, or 1→6), the specific identity of their substrate (sucrose ...
Alpha-glucosidases are enzymes involved in breaking down complex carbohydrates such as starch and glycogen into their monomers. [2] They catalyze the cleavage of individual glucosyl residues from various glycoconjugates including alpha- or beta-linked polymers of glucose. This enzyme convert complex sugars into simpler ones.
Acid alpha-glucosidase, also called acid maltase, [5] is an enzyme that helps to break down glycogen in the lysosome. It is functionally similar to glycogen debranching enzyme , but is on a different chromosome, processed differently by the cell and is located in the lysosome rather than the cytosol. [ 6 ]
Since alpha-glucosidase inhibitors are competitive inhibitors of digestive enzymes, they must be taken at the start of main meals to have maximal effect. Their effects on blood sugar levels following meals will depend on the amount of complex carbohydrates in the meal.
Glycogen debranching enzyme is the only known eukaryotic enzyme that contains multiple catalytic sites and is active as a monomer. [21] [22] Some studies have shown that the C-terminal half of yeast GDE is associated with glucosidase activity, while the N-terminal half is associated with glucosyltransferase activity. [19]
76051 Ensembl ENSG00000214013 ENSMUSG00000062646 UniProt Q8TET4 Q8BVW0 RefSeq (mRNA) NM_198141 NM_001301409 NM_001301410 NM_172672 RefSeq (protein) NP_001288338 NP_001288339 NP_937784 NP_766260 Location (UCSC) Chr 15: 42.27 – 42.36 Mb Chr 2: 120.23 – 120.29 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Neutral alpha-glucosidase C is an enzyme that in humans is encoded by the ...
Maltase-glucoamylase is an alpha-glucosidase digestive enzyme. It consists of two subunits with differing substrate specificity. Recombinant enzyme studies have shown that its N-terminal catalytic domain has highest activity against maltose, while the C-terminal domain has a broader substrate specificity and activity against glucose oligomers. [7]
Inverting enzymes utilize two enzymic residues, typically carboxylate residues, that act as acid and base respectively, as shown below for a β-glucosidase. The product of the reaction has an axial position on C1, but some spontaneous changes of conformation can appear.
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