Literature for peptidase P01.001: DmpA aminopeptidase

Summary Alignment Tree Sequences Sequence features Distribution Structure Literature Substrates

(Topics flags: S Structure, P Specificity, V Review. To select only the references relevant to a single topic, click the link above. See explanation.)

    2012
  1. Frere,J.M. and Van Beeumen,J.
    DmpA L-aminopeptidase D-Ala esterase/amidase of Ochrobactrum anthropi
    [ISSN:978-0-12-407742-3]3, 3663-3666. DOI
  2. 2009
  3. Heck,T., Seebach,D., Osswald,S., Ter Wiel,M.K., Kohler,H.P. and Geueke,B.
    Kinetic resolution of aliphatic beta-amino acid amides by beta-aminopeptidases
    Chembiochem10, 1558-1561. PubMed  Europe PubMed DOI
  4. 2007
  5. Heck,T., Kohler,H.P., Limbach,M., Flogel,O., Seebach,D. and Geueke,B.
    Enzyme-catalyzed formation of beta-peptides: beta-peptidyl aminopeptidases BapA and DmpA acting as beta-peptide-synthesizing enzymes
    Chem Biodivers4, 2016-2030. PubMed  Europe PubMed DOI
  6. 2006
  7. Heck,T., Limbach,M., Geueke,B., Zacharias,M., Gardiner,J., Kohler,H.P. and Seebach,D.
    Enzymatic degradation of beta- and mixed alpha,beta-oligopeptides
    Chem Biodivers3, 1325-1348. PubMed  Europe PubMed DOI  P
  8. 2005
  9. Cheng,H. and Grishin,N.V.
    DOM-fold: a structure with crossing loops found in DmpA, ornithine acetyltransferase, and molybdenum cofactor-binding domain
    Protein Sci14, 1902-1910. PubMed  Europe PubMed DOI
  10. Komeda,H. and Asano,Y.
    A DmpA-homologous protein from Pseudomonas sp. is a dipeptidase specific for beta-alanyl dipeptides
    FEBS J272, 3075-3084. PubMed  Europe PubMed DOI
  11. 2004
  12. Frere,J.M. and Van Beeumen,J.
    DmpA L-aminopeptidase D-Ala esterase/amidase of Ochrobactrum anthropi
    [ISSN:0-12-079610-4]2, 2055-2057.  V
  13. 2000
  14. [YEAR:15-2-2000]Bompard-Gilles,C., Villeret,V., Davies,G.J., Fanuel,L., Joris,B., Frere,J.M. and Van Beeumen,J.
    A new variant of the Ntn hydrolase fold revealed by the crystal structure of L-aminopeptidase D-Ala-esterase/amidase from Ochrobactrum anthropi
    Structure8, 153-162. PubMed  Europe PubMed DOI  S
  15. 1999
  16. Bompard-Gilles,C., Villeret,V., Fanuel,L., Joris,B., Frere,J.M. and Van Beeumen,J.
    Crystallization and preliminary X-ray analysis of a new L-aminopeptidase-D-amidase/D-esterase activated by a Gly-Ser peptide bond hydrolysis
    Acta Crystallogr D Biol Crystallogr55, 699-701. PubMed  Europe PubMed DOI
  17. [YEAR:1-7-1999]Fanuel,L., Goffin,C., Cheggour,A., Devreese,B., Van Driessche,G., Joris,B., Van Beeumen,J. and Frere,J.M.
    The DmpA aminopeptidase from Ochrobactrum anthropi LMG7991 is the prototype of a new terminal nucleophile hydrolase family
    Biochem J341, 147-155. PubMed  Europe PubMed DOI
  18. Fanuel,L., Thamm,I., Kostanjevecki,V., Samyn,B., Joris,B., Goffin,C., Brannigan,J., Van Beeumen,J. and Frere,J.M.
    Two new aminopeptidases from Ochrobactrum anthropi active on D-alanyl-p-nitroanilide
    Cell Mol Life Sci55, 812-818. PubMed  Europe PubMed DOI