CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.60 | Sandwich |
|
2.60.40 | Immunoglobulin-like |
|
2.60.40.10 | Immunoglobulins |
Domain Context
CATH Clusters
| Superfamily | Immunoglobulins |
| Functional Family | Glycogen debranching enzyme |
Enzyme Information
| 3.2.1.196 |
Limit dextrin alpha-1,6-maltotetraose-hydrolase.
based on mapping to UniProt P15067
Hydrolysis of (1->6)-alpha-D-glucosidic linkages to branches with degrees of polymerization of three or four glucose residues in limit dextrin.
-!- This bacterial enzyme catalyzes a reaction similar to EC 3.2.1.33. -!- However, while EC 3.2.1.33 removes single glucose residues linked by 1,6-alpha-linkage, and thus requires the additional activity of EC 2.4.1.25 to act on limit dextrins formed by EC 2.4.1.1, this enzyme removes maltotriose and maltotetraose chains that are attached by 1,6-alpha-linkage to the limit dextrin main chain, generating a debranched limit dextrin without a need for another enzyme.
|
UniProtKB Entries (1)
| P15067 |
GLGX_ECOLI
Escherichia coli K-12
Glycogen debranching enzyme
|
PDB Structure
| PDB | 2WSK |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural Rationale for the Short Branched Substrate Specificity of the Glycogen Debranching Enzyme Glgx.
Proteins
|
