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ENZYME

ENZYME entry: EC 2.4.1.396

Accepted Name
4,6-alpha-glucanotransferase (linear and branched substrates, branched products)
Reaction catalysed
formation of a branched isomalto/malto-polysaccharide from branched malto-oligosaccharides
Comment(s)
  • The enzyme, discovered in several bacterial species, is similar to EC 2.4.1.395 yet is not able to act on sucrose.
  • The enzyme, which belongs to the glycoside hydrolase 70 (GH70) family, possesses both hydrolase and transglycosylase activities, cleaving endo alpha(1->4) linkages from the non-reducing end of maltooligosaccharides and adding the resulting oligosaccharides to the non-reducing end of alpha-D-glucan chains that terminate with a residue linked by an alpha-(1->4) linkage, forming an alpha(1->6) linkage.
  • The enzyme is not able to form successive alpha(1->6) linkages.
  • Unlike EC 2.4.1.394, which can only act on linear substrates, this enzyme is able to act on both linear and branched substrates, and can form the branched reuteran type of alpha-glucan.
Cross-references
BRENDA2.4.1.396
EC2PDB2.4.1.396
ExplorEnz2.4.1.396
PRIAM enzyme-specific profiles2.4.1.396
KEGG Ligand Database for Enzyme Nomenclature2.4.1.396
IUBMB Enzyme Nomenclature2.4.1.396
IntEnz2.4.1.396
MEDLINEFind literature relating to 2.4.1.396
MetaCyc2.4.1.396
Rhea expert-curated reactions2.4.1.396

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All ENZYME / UniProtKB/Swiss-Prot 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.-.-.-