On the binding of aminoalkyl adenylates to isoleucyl-tRNA synthetase from Escherichia coli MRE 600.

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 Kd's ranging from 3.1.10(-4) M with glycinol-AMP ester to 3.7.10(-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).

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Flossdorf J,Marutzky R,Messer K,Kula MR

doi

10.1093/nar/4.3.673

subject

Has Abstract

pub_date

1977-03-01 00:00:00

pages

673-83

issue

3

eissn

0305-1048

issn

1362-4962

journal_volume

4

pub_type

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