Literature for peptidase S09.074: tyrosyl aminopeptidase (Raphanus-type)

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2018
1. Tokai,S., Bito,T., Shimizu,K. and Arima,J.
   Methionine residues lining the substrate pathway in prolyl oligopeptidase from Pleurotus eryngii play an important role in substrate recognition
   Biosci Biotechnol Biochem82, 1107-1115. PubMed  Europe PubMed DOI
2017
2. Tokai,S., Bito,T., Shimizu,K. and Arima,J.
   Effect of oxidation of the non-catalytic beta-propeller domain on the substrate specificity of prolyl oligopeptidase from Pleurotus eryngii
   Biochem Biophys Res Commun487, 356-361. PubMed  Europe PubMed DOI
2014
3. Arima,J., Tokai,S., Chiba,M., Ichiyanagi,T., Yabuta,Y., Mori,N. and Aimi,T.
   Gene cloning and biochemical characterization of eryngase, a serine aminopeptidase of Pleurotus eryngii belonging to the family S9 peptidases
   Biosci Biotechnol Biochem78, 1856-1863. PubMed  Europe PubMed DOI
2011
4. Tsuji,A., Fujisawa,Y., Mino,T. and Yuasa,K.
   Identification of a plant aminopeptidase with preference for aromatic amino acid residues as a novel member of the prolyl oligopeptidase family of serine proteases
   J Biochem150, 525-534. PubMed  Europe PubMed DOI  P
2010
5. Arima,J., Chiba,M., Ichiyanagi,T., Yabuta,Y., Mori,N. and Aimi,T.
   Eryngase: a Pleurotus eryngii aminopeptidase exhibiting peptide bond formation activity
   Appl Microbiol Biotechnol87, 1791-1801. PubMed  Europe PubMed DOI