Eryngase: a Pleurotus eryngii aminopeptidase exhibiting peptide bond formation activity

Applied Microbiology and Biotechnology
Jiro ArimaTadanori Aimi

Abstract

An aminopeptidase that has peptide bond formation activity was identified in the cell-free extract of carpophore of Pleurotus eryngii. The enzyme, redesignated as eryngase, was purified for homogeneity and characterized. Eryngase had a molecular mass of approximately 79 kDa. It showed somewhat high stability with respect to temperature and pH; it was inhibited by iodoacetate. Among hydrolytic activities toward aminoacyl-p-nitroanilides (aminoacyl-pNAs), eryngase mainly hydrolyzed hydrophobic L-aminoacyl-pNAs and exhibited little activity toward D-Ala-pNA and D-Leu-pNA. In terms of peptide bond formation activity, eryngase used various aminoacyl derivatives as acyl donors and acceptors. The products were all dipeptidyl derivatives. Investigation of time dependence on peptide synthesis revealed that some peptides that are not recognized as substrates for hydrolytic activity of eryngase could become good targets for synthesis. Furthermore, eryngase has produced opioid dipeptides--L-kyotorphin (L-Tyr-L-Arg) and D-kyotorphin (L-Tyr-D-Arg)--using L-Tyr-NH(2) and D- and L-Arg-methyl ester respectively as an acyl donor and acceptor. Yield evaluation of kyotorphin synthesis indicated that the conversion ratio of substrate to kyotorphin ...Continue Reading

References

Aug 1, 1970·European Journal of Biochemistry·K Morihara, H Tsuzuki
Sep 1, 1980·Journal of Biochemistry·T Oka, K Morihara
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Dec 29, 2006·Chemistry & Biodiversity·Tobias HeckDieter Seebach
Mar 23, 2010·Journal of Biotechnology·Jiro ArimaTadashi Hatanaka
Apr 27, 2010·Applied and Environmental Microbiology·Jiro ArimaTadashi Hatanaka

Related Concepts

Aminopeptidase
Dipeptides
Enzyme Stability
Yeast Proteins
Hydrogen-Ion Concentration
Substrate Specificity
Pleurotus
Aminopeptidase
Analogs & derivatives
Donor Person

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