Literature for peptidase S46.002: dipeptidyl-peptidase 11 (Porphyromonas gingivalis-type)

Summary Alignment Tree Sequences Sequence features Distribution Structure Literature Substrates

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    2015
  1. Sakamoto,Y., Suzuki,Y., Iizuka,I., Tateoka,C., Roppongi,S., Fujimoto,M., Inaka,K., Tanaka,H., Yamada,M., Ohta,K., Gouda,H., Nonaka,T., Ogasawara,W. and Tanaka,N.
    Structural and mutational analyses of dipeptidyl peptidase 11 from Porphyromonas gingivalis reveal the molecular basis for strict substrate specificity
    Sci Rep5, 11151-11151. PubMed  Europe PubMed DOI  P  S
  2. 2013
  3. Rouf,S.M., Ohara-Nemoto,Y., Ono,T., Shimoyama,Y., Kimura,S. and Nemoto,T.K.
    Phenylalanine 664 of dipeptidyl peptidase (DPP) 7 and phenylalanine 671 of DPP11 mediate preference for P2-position hydrophobic residues of a substrate
    FEBS Open Bio3, 177-183. PubMed  Europe PubMed DOI  P
  4. 2011
  5. Ohara-Nemoto,Y., Shimoyama,Y., Kimura,S., Kon,A., Haraga,H., Ono,T. and Nemoto,T.K.
    Asp- and Glu-specific novel dipeptidyl peptidase 11 of Porphyromonas gingivalis ensures utilization of proteinaceous energy sources
    J Biol Chem286, 38115-38127. PubMed  Europe PubMed DOI  P