EC 2.4.1.161 - Oligosaccharide 4-α-D-glucosyltransferase

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IntEnz Enzyme Nomenclature
EC 2.4.1.161

Names

Accepted name:
oligosaccharide 4-α-D-glucosyltransferase
Other names:
1,4-α-glucan:1,4-α-glucan 4-α-glucosyltransferase
amylase III
1,4-α-D-glucan:1,4-α-D-glucan 4-α-D-glucosyltransferase
α-1,4-transglucosylase
Systematic name:
(1→4)-α-D-glucan:(1→4)-α-D-glucan 4-α-D-glucosyltransferase

Reaction

Comments:

The enzyme acts on amylose, amylopectin, glycogen and maltooligosaccharides. 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 [3], while the enzyme from amoeba does not accept maltose [1,2]. Oligosaccharides with 1→6 linkages cannot function as donors, but can act as acceptors [3]. Unlike EC 2.4.1.25, 4-α-glucanotransferase, this enzyme can transfer only a single glucosyl residue.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0033825
CAS Registry Number: 9000-92-4
UniProtKB/Swiss-Prot:

References

  1. Nebinger, P.
    Separation and characterization of four different amylases of Entamoeba histolytica. I. Purification and properties.
    Biol. Chem. Hoppe-Seyler 367: 161-167 (1986). [PMID: 2423097]
  2. Nebinger, P.
    Separation and characterization of four different amylases of Entamoeba histolytica. II. Characterization of amylases.
    Biol. Chem. Hoppe-Seyler 367: 169-176 (1986). [PMID: 2423098]
  3. Larsbrink, J., Izumi, A., Hemsworth, G. R., Davies, G. J., Brumer, H.
    Structural enzymology of Cellvibrio japonicus Agd31B protein reveals alpha-transglucosylase activity in glycoside hydrolase family 31.
    J. Biol. Chem. 287: 43288-43299 (2012). [PMID: 23132856]

[EC 2.4.1.161 created 1989, modified 2013]