beta-maltose 4-alpha-glucanotransferase activity
Definition
Target type: molecularfunction
Catalysis of the reaction: beta-D-glucose + a plant soluble heteroglycan = a plant soluble heteroglycan + maltose. [EC:2.4.1.25, GOC:pz]
Beta-maltose 4-alpha-glucanotransferase activity refers to the enzymatic activity that catalyzes the transfer of a maltose unit from a donor molecule, such as maltose or a larger oligosaccharide, to the non-reducing end of an acceptor molecule, typically an alpha-1,4-linked glucan chain. This process results in the formation of a new alpha-1,4-glucosidic linkage and the elongation of the acceptor molecule. The reaction is reversible, and the enzyme can also catalyze the reverse reaction, which involves the hydrolysis of alpha-1,4-glucosidic linkages.
The primary function of beta-maltose 4-alpha-glucanotransferase is to modify the structure of starch molecules. It can introduce branch points in amylose chains by transferring maltose units to existing alpha-1,4-linked glucan chains, forming alpha-1,6-glucosidic linkages. These branch points play a critical role in determining the physical and chemical properties of starch, such as its viscosity, gelatinization temperature, and digestibility.
The enzyme is also involved in the biosynthesis of amylopectin, a branched form of starch. It transfers maltose units from maltose or oligosaccharides to growing amylopectin chains, contributing to the formation of its characteristic branched structure.
Moreover, beta-maltose 4-alpha-glucanotransferase can be involved in the degradation of starch molecules. By hydrolyzing alpha-1,4-glucosidic linkages, it can break down starch into smaller oligosaccharides, which can be further degraded by other enzymes.
The activity of beta-maltose 4-alpha-glucanotransferase is regulated by various factors, including pH, temperature, and the presence of specific ions or cofactors. The enzyme is found in a wide range of organisms, including bacteria, fungi, plants, and animals, and plays a critical role in the metabolism of starch and other carbohydrates.'
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Proteins (1)
| Protein | Definition | Taxonomy |
|---|---|---|
| Glycogen debranching enzyme | A glycogen debranching enzyme that is encoded in the genome of human. [PRO:DNx, UniProtKB:P35573] | Homo sapiens (human) |
Compounds (11)
| Compound | Definition | Classes | Roles |
|---|---|---|---|
| 1-deoxynojirimycin | 1-deoxy-nojirimycin: structure in first source duvoglustat : An optically active form of 2-(hydroxymethyl)piperidine-3,4,5-triol having 2R,3R,4R,5S-configuration. | 2-(hydroxymethyl)piperidine-3,4,5-triol; piperidine alkaloid | anti-HIV agent; anti-obesity agent; bacterial metabolite; EC 3.2.1.20 (alpha-glucosidase) inhibitor; hepatoprotective agent; hypoglycemic agent; plant metabolite |
| miglustat | miglustat : A hydroxypiperidine that is deoxynojirimycin in which the amino hydrogen is replaced by a butyl group. miglustat: a glucosylceramide synthase inhibitor | piperidines; tertiary amino compound | anti-HIV agent; EC 2.4.1.80 (ceramide glucosyltransferase) inhibitor |
| 2,5-dihydroxymethyl-3,4-dihydroxypyrrolidine | 2,5-dihydroxymethyl-3,4-dihydroxypyrrolidine: structure given in first source | dihydroxypyrrolidine | |
| 1,4-dideoxy-1,4-iminoarabinitol | 1,4-dideoxy-1,4-iminoarabinitol: RN given refers to (2S-(2alpha,3beta,4alpha))-isomer; structure given in first source | ||
| migalastat | migalastat: a potent inhibitor of glycolipid biosynthesis | piperidines | |
| 2,5-dideoxy-2,5-imino-d-glucitol | 2,5-dideoxy-2,5-imino-D-glucitol: structure in first source | ||
| 1,4-dideoxy-1,4-imino-d-arabinitol | |||
| salacinol | salacinol: a sulfated thiosugar from Salacia reticulata (CELASTRACEAE); structure in first source | ||
| n-(5-adamantane-1-yl-methoxy-pentyl)deoxynojirimycin | |||
| l-altro-1-deoxynojirimycin | L-altro-1-deoxynojirimycin: structure in first source | ||
| neosalacinol |