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- W2032026677 abstract "Summary From studies with related substrates it has been shown that the previously observed greater reactivity of benzoylleucine than of benzoylvaline, in the papain-catalyzed synthesis of anilides, is in accord with steric hindrance by the branching methyl in the valine substrate. This explanation invokes the principle of steric hindrance in enzyme-substrate interaction involving l -type substrates. The theoretical inferences of this sort of result have been indicated. The relative rankings of 13 benzamino acids in the above reaction were shown to differ when ficin was the catalyst, from the results obtained with papain. The effect of the position of the methyl substituent, however, again dominated in the contrast between leucine and valine. The relationships of yield to dilution of enzyme have been found to vary both with each of the enzymes and with the substrate. Newly obtained anilides have been characterized." @default.
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- W2032026677 date "1952-02-01" @default.
- W2032026677 modified "2023-10-10" @default.
- W2032026677 title "Enzymic synthesis of peptide bonds. IV. Effects of variation in substrate structure on relative extents of synthesis of benzoylamino acid anilides as catalyzed by papain and ficin" @default.
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- W2032026677 doi "https://doi.org/10.1016/s0003-9861(52)80022-0" @default.
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