ISSN:
0006-3525
Keywords:
β-amylase
;
sweet potato
;
multiple attack
;
Monte Carlo
;
computer simulation
;
enzyme mechanism
;
enzyme kinetics
;
maltooligosaccharides
;
random walk model
;
statistical method
;
Chemistry
;
Polymer and Materials Science
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
β-Amylase (EC 3.2.1.2) produces maltose (dimer) from the nonreducing ends of α-1,4 glucosidic bonds of substrates like maltooligosaccharides, amylose, and amylopectin. The enzyme releases several maltose molecules from a single enzyme-substrate complex without dissociation by multiple or repetitive attack containing many branching reaction paths. The Monte Carlo method was applied to the simulation of the β-amylase-catalyzed reaction including the multiple attack mechanism. The simulation starts from a single enzyme molecule and a finite number of substrate molecules. The selection of the substrate by the enzyme and degree of multiple attack proceeds by random numbers produced from a computer. The simulation was carried out until the whole substrate and the intermediate molecules were consumed. The simulated data were compared with experimental data of sweet potato β-amylase using heptamer, octamer, nanomer, and 11-mer as substrates. The only adjustable parameter for odd-numbered substrates was the probability of multiple attack, while an additional adjustable parameter (a correction factor due to low reactivity of tetramer) was needed for even-numbered substrates. © 1997 John Wiley & Sons, Inc. Biopoly 42: 831-836, 1997
Additional Material:
7 Ill.
Type of Medium:
Electronic Resource
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