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Literature summary extracted from

  • Tabata, S.; Hizukuri, S.
    Properties of yeast debranching enzyme and its specificity toward branched cyclodextrins (1992), Eur. J. Biochem., 206, 345-348.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.25 Oryctolagus cuniculus
-
 rabbit
-
2.4.1.25 Saccharomyces cerevisiae
-
 yeast
-
2.4.1.25 Saccharomyces cerevisiae
-
 D-346, ATCC 56960
-
3.2.1.33 Oryctolagus cuniculus
-
-
-
3.2.1.33 Saccharomyces cerevisiae
-
 D-346, ATCC 56960
-
3.2.1.41 Oryctolagus cuniculus
-
-
-
3.2.1.41 Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.25
-
 Saccharomyces cerevisiae
3.2.1.33 glycogen debranching enzyme Saccharomyces cerevisiae
3.2.1.33 glycogen debranching enzyme Oryctolagus cuniculus
3.2.1.41
-
 Saccharomyces cerevisiae
3.2.1.41
-
 Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.1.25 muscle
-
 Oryctolagus cuniculus
-
3.2.1.33 muscle
-
 Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.1.25 3.85
-
-
 Saccharomyces cerevisiae
3.2.1.33 3.85
-
-
 Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.25 6-O-alpha-D-glucosyl-cyclodextrins + H2O
-
 Saccharomyces cerevisiae D-glucose + cyclodextrins
-
 ?
2.4.1.25 6-O-alpha-D-glucosyl-cyclomalto-octaose + H2O
-
 Saccharomyces cerevisiae D-glucose + cyclodextrins
-
 ?
2.4.1.25 6-O-alpha-D-glucosyl-cyclomaltoheptaose + H2O
-
 Saccharomyces cerevisiae D-glucose + cyclodextrins
-
 ?
2.4.1.25 additional information appears to be exclusively oligo-1,4-1,4-glucantransferase-amylo 1,6-glucosidase and does not have isoamylase Saccharomyces cerevisiae ?
-
 ?
2.4.1.25 additional information does not act on 6-O-alpha-maltosyl cyclomaltoheptaose Saccharomyces cerevisiae ?
-
 ?
2.4.1.25 additional information does not act on 6-O-alpha-maltosyl cyclomaltoheptaose Oryctolagus cuniculus ?
-
 ?
3.2.1.33 6-O-alpha-D-glucosyl cyclodextrin + H2O
-
 Saccharomyces cerevisiae D-glucose + cyclodextrin
-
 ?
3.2.1.33 6-O-alpha-D-glucosyl cyclodextrin + H2O branched Oryctolagus cuniculus D-glucose + cyclodextrin
-
 ?
3.2.1.33 6-O-alpha-D-glucosyl cyclomalto-octaose + H2O
-
 Saccharomyces cerevisiae D-glucose + cyclomalto-octaose
-
 ?
3.2.1.33 6-O-alpha-D-glucosyl cyclomalto-octaose + H2O
-
 Oryctolagus cuniculus D-glucose + cyclomalto-octaose
-
 ?
3.2.1.33 6-O-alpha-D-glucosyl cyclomaltoheptaose + H2O
-
 Saccharomyces cerevisiae D-glucose + cyclomaltoheptaose
-
 ?
3.2.1.33 6-O-alpha-D-glucosyl cyclomaltoheptaose + H2O
-
 Oryctolagus cuniculus D-glucose + cyclomaltoheptaose
-
 ?
3.2.1.33 6-O-alpha-D-glucosyl cyclomaltohexaose + H2O poor substrate Saccharomyces cerevisiae D-glucose + cyclomaltohexaose
-
 ?
3.2.1.33 6-O-alpha-D-glucosyl cyclomaltohexaose + H2O poor substrate Oryctolagus cuniculus D-glucose + cyclomaltohexaose
-
 ?
3.2.1.33 6-O-alpha-maltotetraosyl cyclomaltoheptaose + H2O very poor substrate Oryctolagus cuniculus ?
-
 ?
3.2.1.33 6-O-alpha-maltotetraosyl cyclomaltoheptaose + H2O poor substrate Saccharomyces cerevisiae ?
-
 ?
3.2.1.33 6-O-alpha-maltotriosyl cyclomaltoheptaose + H2O very poor substrate Oryctolagus cuniculus ?
-
 ?
3.2.1.33 6-O-alpha-maltotriosyl cyclomaltoheptaose + H2O poor substrate Saccharomyces cerevisiae ?
-
 ?
3.2.1.33 glycogen phosphorylase-limit dextrin + H2O
-
 Saccharomyces cerevisiae limit dextrin + D-glucose
-
 r
3.2.1.33 glycogen phosphorylase-limit dextrin + H2O phi-dextrin Oryctolagus cuniculus limit dextrin + D-glucose
-
 r
3.2.1.33 additional information 6-O-alpha-maltosyl cyclomaltoheptaose: not a substrate Saccharomyces cerevisiae ?
-
 ?
3.2.1.33 additional information 6-O-alpha-maltosyl cyclomaltoheptaose: not a substrate Oryctolagus cuniculus ?
-
 ?
3.2.1.41 6-O-alpha-maltosyl cyclodextrin + H2O similar enzyme Saccharomyces cerevisiae glucose + cyclodextrin
-
 ?
3.2.1.41 6-O-alpha-maltosyl cyclodextrin + H2O similar enzyme Oryctolagus cuniculus glucose + cyclodextrin
-
 ?
3.2.1.41 6-O-alpha-maltotriosyl cyclomaltoheptaose + H2O
-
 Oryctolagus cuniculus glucose + cyclodextrin
-
 ?
3.2.1.41 6-O-alpha-maltotriosyl cyclomaltoheptaose + H2O similar enzyme Saccharomyces cerevisiae glucose + cyclodextrin
-
 ?
3.2.1.41 6-O-alpha-maltotriosyl cyclomaltohexaose + H2O similar enzyme Saccharomyces cerevisiae glucose + cyclodextrin
-
 ?
3.2.1.41 6-O-alpha-maltotriosyl cyclomaltohexaose + H2O similar enzyme Oryctolagus cuniculus glucose + cyclodextrin
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.33 glycogen debranching system EC 3.2.1.33 found in mammals and yeast is in a single polypeptide chain containing two active centres. The other activity is similar to that of EC 2.4.1.25, 4-alpha-glucanotransferase, which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-alpha-glucosidase activity can hydrolyse. Together, these two activities constitute the glycogen debranching system Saccharomyces cerevisiae
3.2.1.33 glycogen debranching system EC 3.2.1.33 found in mammals and yeast is in a single polypeptide chain containing two active centres. The other activity is similar to that of EC 2.4.1.25, 4-alpha-glucanotransferase, which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-alpha-glucosidase activity can hydrolyse. Together, these two activities constitute the glycogen debranching system Oryctolagus cuniculus
3.2.1.41 debranching enzyme similar enzyme Saccharomyces cerevisiae
3.2.1.41 debranching enzyme similar enzyme Oryctolagus cuniculus