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3.2.1.33: amylo-alpha-1,6-glucosidase

This is an abbreviated version!
For detailed information about amylo-alpha-1,6-glucosidase, go to the full flat file.

Word Map on EC 3.2.1.33

Reaction

6-O-alpha-D-glucosyl cyclomaltoheptaose
+
H2O
=
D-glucose
+
cyclomaltoheptaose

Synonyms

1,4-glucan-4-glucosyltransferase/amylo-1,6-glucosidase, 4-alpha-glucano-transferase amylo-1,6-glucosidase, alpha-(1,6)-glucosidase, alpha-1,6-glucosidase, amylo-1,6-glucosidase, amylo-1,6-glucosidase-oligo-1,4-1,4-transferase, amylo-1,6-glucosidase/1,4-alpha-glucan 4-alpha-glucan 4-alpha-glycosyltransferase, amylo-1,6-glucosidase/1,4-alpha-glucan:1,4-alpha-glucan 4-alpha-glycosyltransferase, amylo-1,6-glucosidase/4-alpha-glucanotransferase, amylo-1,6-glucosidase/oligo-1,4-1,4-glucantransferase, amylo-alpha-1,6-glucosidase, amylo-alpha-1,6-glucosidase activity, amyloglucosidase, amylopectin 1,6-glucosidase, debrancher enzyme, debrancher protein, dextrin 6-alpha-D-glucosidase, dextrin 6-alpha-glucosidase, dextrin 6-glucanohydrolase, dextrin 6-glucohydrolase, dextrin-1,6-glucosidase, dextrin:6-glucohydrolase, GDE, GDE amylo-alpha-1,6-glucosidase, glucosidase, amylo-1,6-, glucosidase/transferase, glycogen debranching enzyme, glycogen debranching system, glycogen phosphorylase dextrin 6-glucanohydrolase, glycogen phosphorylase limit dextrin alpha-1,6-glucohydrolase, glycogen phosphorylase limit dextrin debranching system, indirect debranching enzyme, NPDE, oligo-alpha-1,4-glucan:alpha-1,4-glucan-4-glycosyltransferase-amylo-1,6-glucosidase, SSO2094, transferase-glucosidase, TreX

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.33 amylo-alpha-1,6-glucosidase

General Information

General Information on EC 3.2.1.33 - amylo-alpha-1,6-glucosidase

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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
germline mutations lead to glycogen storage disease type III. Agl deletion increases the incidence of bladder cancer, supporting its role as a suppressor of transformation
physiological function