| EC |
3.2.1.33 |
| Accepted name: |
amylo-α-1,6-glucosidase |
| Reaction: |
Hydrolysis of (1→6)-α-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin |
| Other name(s): |
amylo-1,6-glucosidase; dextrin 6-α-D-glucosidase; amylopectin 1,6-glucosidase; dextrin-1,6-glucosidase; glycogen phosphorylase-limit dextrin α-1,6-glucohydrolase |
| Systematic name: |
glycogen phosphorylase-limit dextrin 6-α-glucohydrolase |
| Comments: |
This enzyme hydrolyses an unsubstituted glucose unit linked by an α(1→6) bond to an α(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-α-glucanotransferase), which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-α-glucosidase activity can then hydrolyse. Together, these two activities constitute the glycogen debranching system. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9012-47-9 |
| References: |
| 1. |
Brown, D.H. and Brown, B.I. Enzymes of glycogen debranching: Amylo-1,6-glucosidase (I) and oligo-1,4→1,4-glucanotransferase (II). Methods Enzymol. 8 (1966) 515–524. |
| 2. |
Lee, E.Y.C., Carter, J.H., Nielsen, L.D. and Fischer, E.H. Purification and properties of yeast amylo-1,6-glucosidase-oligo-1,4 leads to 1,4-glucantransferase. Biochemistry 9 (1970) 2347–2355. [PMID: 5424210] |
| 3. |
Nelson, T.E., Kolb, E. and Larner, J. Purification and properties of rabbit muscle amylo-1,6-glucosidase-oligo-1,4-1,4-transferase. Biochemistry 8 (1969) 1419–1428. [PMID: 5805288] |
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| [EC 3.2.1.33 created 1965, modified 2000] |
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