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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Role of conformation transitions inadenylate kinase
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Role of conformation transitions inadenylate kinase

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A recent paper by Pisliakov et al. (1) asserts that it is a response toseveral papers, which, according to the authors (1), imply that“motions along conformational coordinates play an importantrole in the chemical step” (1). Because ref. 1 and most of the citedpapers in ref. 1 references 3,6,7, and 14 in Pisliakov et al. (1) areconcerned with adenylate kinase (AdK), my comments refer tothis enzyme. AdK has an open state, to which the substrates bindand from which the products are released, as well as a closed state,in which catalysis takes place. None of these cited references areconcerned with the chemical reaction or suggest that there iscoupling between the closing/opening conformational transitionsand the chemistry; catalysis in these papers refers to the overallrate and not to the chemical step. They show that the openingtransition after the chemical reaction is the rate-determining stepreference 14 in (1); i.e., in AdK, like triosephosphate isomerase,the chemistry has reached perfection (2). The two other papers,of which I am a coauthor, study the closing transition encodedin the structure references 6 and 7 in (1) and the role of fastmotions as lubricants (3) for hinge regions.

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