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Literature summary for 2.4.1.25 extracted from

  • Ikeda, A.; Makino, Y.; Matsubara, H.
    Glycogen debranching pathway deduced from substrate specificity of glycogen debranching enzyme (2022), Glycoconj. J., 39, 345-355.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
glycogen + H2O Sus scrofa
-
?
-
?

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycogen + H2O
-
Sus scrofa ?
-
?
additional information analysis of the substrate specificities of 4-alpha-glucanotransferase and amylo-alpha-1,6-glucosidase (EC 3.2.1.33) using fluorogenic biantennary dextrins such as G-GG-G-(G-G-G-G<->)G-G-GPA (F4/4/2, where GPA = 1-deoxy-1-[(2-pyridyl)amino]-D-glucitol), G-(G-G-G-G<->)G-G-GPA (F1/4/2), and G-G-G-G-G-G-G-(G<->)G-G-GPA (F7/1/2). Contrary to the prevailing hypothesis, the main branch of F4/4/2 is an important donor substrate component of 4-alpha-glucanotransferase and does not serve as an acceptor substrate. But when G-G-G-G-G-GPA is added to the mixture, it successfully accepts a maltotriosyl (G3-) residue from F4/4/2. The debranching activity of GDE towards phosphorylase-limit glycogen substantially increases when methyl alpha-maltooligosides with lengths equal to or greater than that of methyl alpha-maltopentaoside (G5-OCH3) are added to the enzyme reaction mixture. GP-limit dextrin is a bifunctional substrate possessing both donor and acceptor moieties for GDE 4-alpha-glucanotransferase. Maltohexaose is both acceptor and activator of 4-alpha-glucanotransferase. Synthesis of fluorogenic biantennary dextrins F3/1/2, F4/1/2, F5/1/2, F4/1/3, F1/4/2, F4/4/2, and F4/4/3. Substrate specificity of GDE 4-alpha-glucanotransferase, overview Sus scrofa ?
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-

Synonyms

Synonyms Comment Organism
GDE
-
Sus scrofa
glycogen debranching enzyme
-
Sus scrofa
additional information see also EC 3.2.1.33 Sus scrofa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
assay at Sus scrofa

General Information

General Information Comment Organism
metabolism a distinct macroscopic debranching pathway is proposed: via 4-alpha-glucanotransferase, the G3-residue of the donor branch is transferred to a long (n >/= 5) linear Gn-residue linked to a different branching G residue Sus scrofa
physiological function glycogen debranching enzyme (GDE) is bifunctional in that it exhibits both 4-alpha-glucanotransferase (EC 2.4.1.25) and amylo-alpha-1,6-glucosidase activity at two distinct catalytic sites. GDE converts the phosphorylase-limit biantennary branch into a linear maltooligosyl residue, which is then subjected to phosphorylase, and glycogen degradation continues Sus scrofa