Porcine pancreatic a-amylase (EC 3.2. I . I ) produces short maltooligosaccharides from a single enzyme-substrate complex without dissociation by multiple or repetitive attack. Multiple attack is caused by relative sliding ofthe enzyme along the product chain ofthe enzyme-product complex without dis
Monte Carlo simulation of multiple attack mechanism of β-amylase-catalyzed reaction
✍ Scribed by Hiroshi Nakatani
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1997
- Tongue
- English
- Weight
- 118 KB
- Volume
- 42
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
b-Amylase (EC 3.2.1.2) produces maltose (dimer) from the nonreducing ends of a-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 b-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 b-amylase using heptamer, octamer, nanomer, and 11-mer as substrates. The only adjustable parameter for oddnumbered 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.
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