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Literature summary extracted from

  • Nimpiboon, P.; Kaulpiboon, J.; Krusong, K.; Nakamura, S.; Kidokoro, S.; Pongsawasdi, P.
    Mutagenesis for improvement of activity and thermostability of amylomaltase from Corynebacterium glutamicum (2016), Int. J. Biol. Macromol., 86, 820-828.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.25 expressed in Escherichia coli BL21(DE3) cells Corynebacterium glutamicum

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.25 A406L the mutant shows higher thermostability at 35-40°C, higher intermolecular transglucosylation activity with an upward shift in the optimum temperature and a slight increase in the optimum pH for disproportionation and cyclization reactions compared to the wild type enzyme. The mutant shows higher specific activities for starch transglucosylation (2.1fold) and disproportionation (1.4fold) than those of the wild type Corynebacterium glutamicum
2.4.1.25 A406V the mutant shows higher thermostability at 50°C, higher intermolecular transglucosylation activity with an upward shift in the optimum temperature and a slight increase in the optimum pH for disproportionation and cyclization reactions compared to the wild type enzyme. The mutant shows higher specific activities for starch transglucosylation (2.8fold) and disproportionation (2.1fold) than those of the wild type Corynebacterium glutamicum

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.25 Corynebacterium glutamicum
-
-
-
2.4.1.25 Corynebacterium glutamicum ATCC 13032
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.25 HisTrap affinity column chromatography, and gel filtration Corynebacterium glutamicum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.25 maltoheptaose + maltoheptaose
-
 Corynebacterium glutamicum ?
-
 ?
2.4.1.25 maltoheptaose + maltoheptaose
-
 Corynebacterium glutamicum ATCC 13032 ?
-
 ?
2.4.1.25 maltohexaose + maltohexaose
-
 Corynebacterium glutamicum maltooligosaccharide
-
 ?
2.4.1.25 maltohexaose + maltohexaose
-
 Corynebacterium glutamicum ATCC 13032 maltooligosaccharide
-
 ?
2.4.1.25 maltopentaose + maltopentaose
-
 Corynebacterium glutamicum maltooligosaccharides
-
 ?
2.4.1.25 maltopentaose + maltopentaose
-
 Corynebacterium glutamicum ATCC 13032 maltooligosaccharides
-
 ?
2.4.1.25 maltose + maltose worst substrate Corynebacterium glutamicum ?
-
 ?
2.4.1.25 maltotetraose + maltotetraose
-
 Corynebacterium glutamicum maltooligosaccharides
-
 ?
2.4.1.25 maltotetraose + maltotetraose
-
 Corynebacterium glutamicum ATCC 13032 maltooligosaccharides
-
 ?
2.4.1.25 maltotriose + maltotriose most efficient substrate Corynebacterium glutamicum maltooligosaccharides
-
 ?
2.4.1.25 maltotriose + maltotriose most efficient substrate Corynebacterium glutamicum ATCC 13032 maltooligosaccharides
-
 ?
2.4.1.25 pea starch + glycosyl acceptor
-
 Corynebacterium glutamicum ?
-
 ?
2.4.1.25 soluble potato starch + glycosyl acceptor
-
 Corynebacterium glutamicum ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.25 amylomaltase
-
 Corynebacterium glutamicum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.25 45
-
-
 Corynebacterium glutamicum

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.4.1.25 35 40 at short incubation time for 15 min at 40°C, the remaining activity of the wild type enzyme is 39.5%, whereas for 30 min incubation, the activity remained is 15.2%. At 35°C for a longer incubation time of 3 h, the remaining activity of the wild type enzyme is 45% Corynebacterium glutamicum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.25 6
-
-
 Corynebacterium glutamicum