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Literature summary for 2.4.1.248 extracted from

  • Suzuki, R.; Suzuki, N.; Fujimoto, Z.; Momma, M.; Kimura, K.; Kitamura, S.; Kimura, A.; Funane, K.
    Molecular engineering of cycloisomaltooligosaccharide glucanotransferase from Bacillus circulans T-3040: structural determinants for the reaction product size and reactivity (2015), Biochem. J., 467, 259-270.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
F268V/D469Y/A513V/Y515S mutant produces three times as much megalo-cycloisomaltooligosaccharides (10-12 glucose units) and 1.5 times as much total cycloisomaltooligosaccharides (7-12 glucose units) as compared with the wild-type. The modified product size specificity is attributable to the construction of novel substrate-binding sites in the B-2 substrate-binding site and reactivity is improved by mutation on subsite -3 on the catalytic domain Niallia circulans
additional information utational studies show that substrate-binding sites B-1 and B-2 contribute to recruiting substrate and maintaining product size respectively Niallia circulans

Organism

Organism UniProt Comment Textmining
Niallia circulans P94286
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Niallia circulans T-3040 P94286
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information CITase from Bacillus circulans T-3040 produces mainly cycloisomaltooligosaccharides of 8 units with little megalo-cycloisomaltooligosaccharides with 10-12 glucose units Niallia circulans ?
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additional information CITase from Bacillus circulans T-3040 produces mainly cycloisomaltooligosaccharides of 8 units with little megalo-cycloisomaltooligosaccharides with 10-12 glucose units Niallia circulans T-3040 ?
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?
soluble starch
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Niallia circulans cyclo-(-6)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-) + ?
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?
soluble starch
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Niallia circulans T-3040 cyclo-(-6)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-) + ?
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?