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Literature summary extracted from

  • van der Kaaij, R.M.; Yuan, X.L.; Franken, A.; Ram, A.F.; Punt, P.J.; van der Maarel, M.J.; Dijkhuizen, L.
    Two novel, putatively cell wall-associated and glycosylphosphatidylinositol-anchored alpha-glucanotransferase enzymes of Aspergillus niger (2007), Eukaryot. Cell, 6, 1178-1188.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.25 genes agtA and agtB, DNA and amino acid sequence determination and analysis, phylogenetic tree, overexpression in Aspergillus niger strain MGG029, subcloning in Escherichia coli Aspergillus niger

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.25 additional information an agtA knockout of Aspergillus niger shows an increased susceptibility towards the cell wall-disrupting compound, phenotypic characterization of CFW hypersensitive DELTAagtA strain and AgtA/AgtB overexpression strains, overview Aspergillus niger

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.4.1.25 cell wall associated Aspergillus niger 5618
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Organism

EC Number Organism UniProt Comment Textmining
2.4.1.25 Aspergillus niger
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 strains CBS 513.88, NRRL3122, and N402, isozymes AgtA and AgtB encoded by genes agtA and agtB
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Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.4.1.25 glycolipoprotein the enzyme is cell wall-associated via glycosylphosphatidylinositol anchoring Aspergillus niger

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.25 additional information both isozymes AgtA and AgtB show transglycosylation activity on donor substrates with alpha-(1,4)-glycosidic bonds and at least five anhydroglucose units forming alpha-(1,4)-glycosidic bonds. Their reaction products reach a degree of polymerization of at least 30. Maltose and larger maltooligosaccharides are the most efficient acceptor substrates, although AgtA also uses small nigerooligosaccharides containing alpha-(1,3)-glycosidic bonds as acceptor substrate, reaction products, overview. The enzyme also shows hydrolyzing activity with potato starch Aspergillus niger ?
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 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.25 AgtA
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 Aspergillus niger
2.4.1.25 AgtB
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 Aspergillus niger
2.4.1.25 More the enzyme belongs to the alpha-amylase family Aspergillus niger

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.25 37
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 assay at Aspergillus niger

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.25 5.5
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 assay at Aspergillus niger

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.4.1.25 4.2 8
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 Aspergillus niger