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- W2002125480 abstract "Evidence in favour of the functional importance of domain displacements upon substrate binding in enzymes is presented. This includes the following significant points: (1) in the ‘closed’ structure of yeast phosphoglycerate kinase, the γ-phosphate of ATP and hydroxyl group of 3-phosphoglycerate are screened from water, which makes possible the transfer of the phosphate group to 3-phosphoglycerate; (2) domain ‘locking’ is observed in the active forms of pig muscle 3-phosphoglycerate kinase (including the form of the enzyme with methylated easily-reacting SH groups), but it is absent in its inactive form with carboxamidomethylated SH groups, whereas all these forms have the same substrate-binding ability as the native enzyme." @default.
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- W2002125480 date "1988-09-01" @default.
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- W2002125480 title "Interdomain mobility of enzymes and its functional role" @default.
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- W2002125480 doi "https://doi.org/10.1016/0304-5102(88)85053-3" @default.
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