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Literature summary for 2.4.1.25 extracted from

  • Watanabe, Y.; Makino, Y.; Omichi, K.
    Donor substrate specificity of 4-alpha-glucanotransferase of porcine liver glycogen debranching enzyme and complementary action to glycogen phosphorylase on debranching (2008), J. Biochem., 143, 435-440.
    View publication on PubMed
Search for more literature for 2.4.1.25

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
64-O-alpha-maltooligosyl-pyridylamino-maltooctaose + maltohexaose 4-alpha-glucanotransferase action of porcine liver GDE on four 64-O-alpha-maltooligosyl-pyridylamino-maltooctaoses, in the presence or absence of an acceptor, maltohexaose, overview Sus scrofa 64-O-alpha-D-glucosyl-pyridylamino-maltooctaose + ?
-
 ?
additional information the enzyme liberates maltose oligomers from branched dextrins in presence or absence of acceptor maltohexaose, 6_4-O-alpha-glucosyl-pyridylamino-maltooctaose is liberated from 64-O-alpha-maltopentaosyl-pyridylamino-maltooctaose, 64-O-alpha-maltotetraosyl-pyridylamino-maltooctaose and 64-O-alpha-maltotriosyl-pyridylamino-maltooctaose, whereas 64-O-alpha-maltosyl-pyridylamino-maltooctaose is resistant to the enzyme, donor substrate specificity of GDE, GDE 4-alpha-glucanotransferase removes a maltotriosyl residue from the maltotetraosyl branch in a way that the alpha-1,6-linked glucosyl residue is retained, overview Sus scrofa ?
-
 ?

Synonyms

Synonyms Comment Organism
4-alpha-glucanotransferase
-
 Sus scrofa
GDE
-
 Sus scrofa
glycogen debranching enzyme
-
 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