Quantitative analysis of the action of Taka-amylase A on maltotriose.
The action of Taka-amylase A from Asp. oryzae was studied quantitatively by the product analysis method using unlabeled maltotriose and maltotriose labeled at the reducing end as substrates. It was found that the ratio of the unlabeled products, maltose (G2) and glucose (G1) exceeded unity, and that the ratio of the labeled products, G2/G1 was strongly dependent on the initial substrate concentrations. The results can only be explained by a transglycosylation or condensation mechanism or both. Analysis of maltose labeled at the nonreducing or reducing end reveal that the ratio of the transglycosylation to the condensation mechanism was about 20:1 with about 80 mM maltotriose. A computer simulation was made on a reaction scheme involving the termolecular-shifted complex, transglycosylation and condensation besides hydrolysis, by using reported subsite affinities as modified by the authors. The simulation reproduced the experimental results satisfactorily.
D000681:Amylases / Q000378:metabolism*; D001236:Aspergillus oryzae / Q000201:enzymology; D001665:Binding Sites; D005947:Glucose / Q000032:analysis; D008320:Maltose / Q000032:analysis; D009844:Oligosaccharides / Q000378:metabolism*; D011485:Protein Binding; D014312:Trisaccharides
D009844:Oligosaccharides; D014312:Trisaccharides; C008317:maltotriose; D008320:Maltose; D000681:Amylases; D005947:Glucose