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Information on EC 3.2.1.33 - amylo-alpha-1,6-glucosidase and Organism(s) Homo sapiens and UniProt Accession P35573

for references in articles please use BRENDA:EC3.2.1.33
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EC Tree
IUBMB Comments
This enzyme hydrolyses an unsubstituted glucose unit linked by an alpha(1->6) bond to an alpha(1->4) glucose chain. The enzyme activity found in mammals and yeast is in a 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 then hydrolyse. Together, these two activities constitute the glycogen debranching system.
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Homo sapiens
UNIPROT: P35573
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
amylo-1,6-glucosidase, debrancher enzyme, amylo-alpha-1,6-glucosidase, debrancher protein, amylo-alpha-1,6-glucosidase activity, amylo-1,6-glucosidase/4-alpha-glucanotransferase, dextrin 6-glucohydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,4-glucan-4-glucosyltransferase/amylo-1,6-glucosidase
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4-alpha-glucano-transferase amylo-1,6-glucosidase
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alpha-(1,6)-glucosidase
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amylo-1,6-glucosidase
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amylo-1,6-glucosidase-oligo-1,4-1,4-transferase
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amylo-1,6-glucosidase/1,4-alpha-glucan 4-alpha-glucan 4-alpha-glycosyltransferase
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amylo-1,6-glucosidase/1,4-alpha-glucan:1,4-alpha-glucan 4-alpha-glycosyltransferase
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amylo-1,6-glucosidase/4-alpha-glucanotransferase
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amylo-1,6-glucosidase/oligo-1,4-1,4-glucantransferase
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amylopectin 1,6-glucosidase
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debrancher enzyme
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debrancher protein
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dextrin 6-alpha-D-glucosidase
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dextrin 6-alpha-glucosidase
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dextrin 6-glucanohydrolase
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dextrin 6-glucohydrolase
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dextrin-1,6-glucosidase
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dextrin:6-glucohydrolase
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glucosidase, amylo-1,6-
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glucosidase/transferase
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glycogen debranching enzyme
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glycogen debranching system
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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
glycogen phosphorylase limit dextrin debranching system
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indirect debranching enzyme
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oligo-alpha-1,4-glucan:alpha-1,4-glucan-4-glycosyltransferase-amylo-1,6-glucosidase
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transferase-glucosidase
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
glycogen phosphorylase-limit dextrin 6-alpha-glucohydrolase
This enzyme hydrolyses an unsubstituted glucose unit linked by an alpha(1->6) bond to an alpha(1->4) glucose chain. The enzyme activity found in mammals and yeast is in a 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 then hydrolyse. Together, these two activities constitute the glycogen debranching system.
CAS REGISTRY NUMBER
COMMENTARY hide
9012-47-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glycogen + H2O
glycogen + D-glucose
show the reaction diagram
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reverse reaction: incorporation of glucose into glycogen
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r
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
patients with Glycogen Storage Disease Type III. Bifunctional amylo-1,6-glucosidase and 4-alpha-glucanotransferase, protein possesses two separate domains for the transferase and glucosidase activities
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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cultivated
Manually annotated by BRENDA team
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from skin biopsies
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GDE_HUMAN
1532
0
174764
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
172600
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glycogen debranching enzyme, calculated from cDNA-derived amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G1448R
mutation detected in patient with Glycogen Storage Disease Type III. Significant loss in both enzymatic activites and carbohydrate binding ability, as well as enhancing targeting for proteasomal degradation
L620P
mutation detected in patient with Glycogen Storage Disease Type III. Mutation abolishes transferase activity
R1147G
mutation detected in patient with Glycogen Storage Disease Type III. Mutation impairs glucosidase function
Y1445ins
mutation detected in patient with Glycogen Storage Disease Type III. Significant loss in both enzymatic activites and carbohydrate binding ability, as well as enhancing targeting for proteasomal degradation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glycogen debranching enzyme
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
glycogen debranching enzyme, cDNA
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
study on patients with Glycogen Storage Disease Type III. Inactivation of either enzymatic activity is sufficient to cause Glycogen Storage Disease Type III disease. The carbohydrate binding domain of amylo-1,6-glucosidase,4-alpha-glucanotransferase plays a major role to coordinate its functions and regulation by the ubiquitin-proteasome system
medicine
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diagnosis, even prenatal, of type III glycogen storage disease: marked decrease or absence of amylo-1,6-glucosidase, glycogen debranching enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lee, E.Y.C.; Whelan, W.J.
Glycogen and starch debranching enzymes
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
5
191-234
1972
Homo sapiens, Mammalia, Oryctolagus cuniculus, Saccharomyces cerevisiae
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Manually annotated by BRENDA team
Justice, P.; Ryan, C.; Hsia, D.Y.Y.; Krmpotik, E.
Amylo-1,6-glucosidase in human fibroblasts: studies in type III glycogen storage disease
Biochem. Biophys. Res. Commun.
39
301-306
1970
Homo sapiens
Manually annotated by BRENDA team
Yang, B.Z.; Ding, J.H.; Enghild, J.J.; Bao, Y.; Chen, Y.T.
Molecular cloning and nucleotide sequence of cDNA encoding human muscle glycogen debranching enzyme
J. Biol. Chem.
267
9294-9299
1992
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Cheng, A.; Zhang, M.; Okubo, M.; Omichi, K.; Saltiel, A.R.
Distinct mutations in the glycogen debranching enzyme found in Glycogen Storage Disease Type III lead to impairment in diverse cellular functions
Hum. Mol. Genet.
18
2045-2052
2009
Homo sapiens (P35573)
Manually annotated by BRENDA team