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. 1981 Mar 1;193(3):737–742. doi: 10.1042/bj1930737

Cleavage by trypsin and by the proteinase from Armillaria mellea at epsilon-N-formyl-lysine residues.

F P Barry, S Doonan, C A Ross
PMCID: PMC1162661  PMID: 6796050

Abstract

Kinetic studies were made of the hydrolysis by trypsin of alpha-N-acetylglycyl-L-lysine methyl ester and of its neutral analogue alpha-N-acetylglycyl-epsilon-N-formyl-L-lysine methyl ester. The latter substance is a moderately good substrate for trypsin, and this observation is discussed in terms of the substrate specifically of the enzyme. The actions of trypsin and of the lysine-specific proteinase from Armillaria mellea on both a native and a formylated polypeptide substrate were compared. Both enzymes were found to hydrolyse specifically bonds to epsilon-N-formyl-lysine in the formylated substrate.

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Selected References

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