Abstract
Cyclization and disproportionation catalyzed by the cyclodextrin glycosyltransferase (EC 2.4.1.19) from Klebsiella pneumoniae M 5 al with various maltooligosaccha-rides and with maltodextrin DP 19 were studied to determine the rate parameters for each substrate.
Maltooctaose proved to be the smallest substrate for direct cyclization. The enzyme did not have higher affinity to maltodextrin DP 19, suggesting that the active site spans 8 glucose units. The rates of disproportionation markedly depended on the chain length of substrate. Disproportionation of maltotriose yielded maltose and maltotetraose, and of maltotetraose maltose and maltohexaose. As the initial products of cyclization from maltooctaose were maltose and cyclomaltohexaose, the catalytic site is likely to be situated between subsites 2 and 3. Magnitudes of subsite affinities were evaluated from the rate parameters of disproportionation. The highest values were found for subsites 2 and 3. The results point to a ping-pong-mechanism of the reaction.
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Bender, H. (1988). Studies on the Reaction Mechanism of Cyclodextrin Glycosyltransferases: Subsite Analysis. In: Huber, O., Szejtli, J. (eds) Proceedings of the Fourth International Symposium on Cyclodextrins. Advances in Inclusion Science, vol 5. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-2637-0_3
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DOI: https://doi.org/10.1007/978-94-009-2637-0_3
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