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Literature summary for 3.2.1.2 extracted from

  • Ishikawa, K.; Nakatani, H.; Katsuya, Y.; Fukazawa, C.
    Kinetic and structural analysis of enzyme sliding on a substrate: multiple attack in beta-amylase (2007), Biochemistry, 46, 792-798.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of mutant enzyme W55R Glycine max

Protein Variants

Protein Variants Comment Organism
D53A mutant enzyme shows 13% of the wild-type activity towards maltoheptaose Glycine max
W55R mutant enzyme shows 20% of the wild-type activity towards maltoheptaose Glycine max

Organism

Organism UniProt Comment Textmining
Glycine max P10538
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
maltoheptaose + H2O the exo-type enzyme can catalyze the successive liberation of beta-maltose from the nonreducing ends of alpha-1,4-linked glucopyranosyl polymers. A phenomenon called multiple or repetitive attack is observed where the enzyme releases several maltose molecules in a single enzyme-substrate complex. The multiple attack action needs the force of enzyme sliding on the substrate. In addition, it is important for the multiple attack that the enzyme and substrate have the characteristics of a stable productive substrate-enzyme complex through a hydrogen bond between the nonreducing end of the substrate and the carboxyl residue of the enzyme Glycine max maltose + D-glucose + ?
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