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- W2020883629 abstract "The results show that enzyme I of gramicidin S synthetase activates d-leucine in a manner analogous to that of l-leucine (ATP +d-leucine ⇌d-leucyl-adenylate + PP1) and binds two moles of d-leucine in thioester linkage. It has therefore two thiol sites for d-leucine, compared to one for the l-isomer. One of the sites seems to be the thiol site for L-leucine which is therefore stereo-unspecific. The results also indicate that the site for the formation of the aminoacyl adenylates is the same for the two isomers. In contrast to thioester-bound l-leucine, enzyme-bound D-leucine does not catalyze the ATP-[14C]AMP exchange reaction. At a molar ratio of l-leucine: D-leucine equal to 4, gramicidin S synthesis is almost completely inhibited and the growth of the peptide chain stops at the tetrapeptide stage (D-Phe-l-Pro-l-Val-L-Orn). Enzyme-bound D-leucine is thus not able to replace L-leucine in the formation of the pentapeptide." @default.
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- W2020883629 date "1972-10-01" @default.
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- W2020883629 title "The Mechanism of the Inhibition of Gramicidin-S Synthesis by d-Leucine" @default.
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- W2020883629 doi "https://doi.org/10.1111/j.1432-1033.1972.tb02080.x" @default.
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