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- W2078701662 abstract "The binding of nine aminoalkyl adenylates to isoleucyl-tRNA synthetase from Escherichia coli MRE 600 was measured and compared with the binding of the cognate amino acids. It was found that they bind.rather tightly to the enzyme, the K ranging from 3.1.10−4 M with glycinol-AMP ester to 3.7.18−9 M with L-isoleucinol-AMP ester. The binding is not affected by magnesium. It is shown that the free energies of binding of the esters can be calculated adding a constant contribution of the AMP-moiety of about - 4.1 (- 17) kcal/mole (kJ/mole) to the free energies of binding of the cognate amino acids, which we have reported earlier (19,25,26)." @default.
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- W2078701662 date "1977-01-01" @default.
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- W2078701662 title "On the binding of aminoalkyl adenytates to isoleucyl-tRNA synthetase from Escherichia coli MRE 600" @default.
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- W2078701662 doi "https://doi.org/10.1093/nar/4.3.673" @default.
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