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ENZYME entry: EC 184.108.40.206
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|Transfers the non-reducing terminal alpha-D-glucose residue from a (1->4)-alpha-D-glucan to the 4-position of a free glucose or of a glucosyl residue at the non-reducing terminus of a (1->4)-alpha-D-glucan, thus bringing about the rearrangement of oligosaccharides|
- The enzyme acts on amylose, amylopectin, glycogen and
- No detectable free glucose is formed, indicating the enzyme does not
act as a hydrolase.
- The enzyme from the bacterium Cellvibrio japonicus has the highest
activity with maltotriose as a donor, and also accepts maltose, while
the enzyme from amoeba does not accept maltose.
- Oligosaccharides with 1->6 linkages cannot function as donors,
but can act as acceptors.
- Unlike EC 220.127.116.11, this enzyme can transfer only a single glucosyl
|PRIAM enzyme-specific profiles||18.104.22.168|
|KEGG Ligand Database for Enzyme Nomenclature||22.214.171.124|
|IUBMB Enzyme Nomenclature||126.96.36.199|
|MEDLINE||Find literature relating to 188.8.131.52|
|Rhea expert-curated reactions||184.108.40.206|
entries corresponding to 2.4.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.4.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.-.-.-