Literature for peptidase M24.006: bacillus Xaa-Pro aminopeptidase

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

2024
1. Xu,S., Grochulski,P. and Tanaka,T.
   Structural basis for the allosteric behaviour and substrate specificity of Lactococcus lactis Prolidase
   Biochim Biophys Acta Proteins Proteom1872, 141000-141000. PubMed  Europe PubMed DOI
2017
2. Kgosisejo,O., Chen,J.A., Grochulski,P. and Tanaka,T.
   Crystallographic structure of recombinant Lactococcus lactis prolidase to support proposed structure-function relationships
   Biochim Biophys Acta1865, 473-480. PubMed  Europe PubMed DOI  S
2013
3. Zaprasis,A., Brill,J., Thuring,M., Wunsche,G., Heun,M., Barzantny,H., Hoffmann,T. and Bremer,E.
   Osmoprotection of Bacillus subtilis through import and proteolysis of proline-containing peptides
   Appl Environ Microbiol79, 576-587. PubMed  Europe PubMed DOI
2012
4. Monnet,V.
   Xaa-Pro aminopeptidase (Lactococcus)
   [ISSN:978-0-12-407743-0]3, 1524-1525. DOI
5. Mossmann,D., Meisinger,C. and Vogtle,F.N.
   Processing of mitochondrial presequences
   Biochim Biophys Acta1819, 1098-1106. PubMed  Europe PubMed DOI  V
6. Stressler,T., Eisele,T., Schlayer,M. and Fischer,L.
   Production, active staining and gas chromatography assay analysis of recombinant aminopeptidase P from Lactococcus lactis ssp. lactis DSM 20481
   AMB Express2, 39-39. PubMed  Europe PubMed DOI  E
2011
7. Chen,J.A. and Tanaka,T.
   Charged residues on a flap-loop structure of Lactococcus lactis prolidase play critical roles in allosteric behavior and substrate inhibition
   Biochim Biophys Acta1814, 1677-1685. PubMed  Europe PubMed DOI
2009
8. Hu,K. and Tanaka,T.
   S1 site residues of Lactococcus lactis prolidase affect substrate specificity and allosteric behaviour
   Biochim Biophys Acta1794, 1715-1724. PubMed  Europe PubMed DOI  P
2008
9. Yang,S.I. and Tanaka,T.
   Characterization of recombinant prolidase from Lactococcus lactis - changes in substrate specificity by metal cations, and allosteric behavior of the peptidase
   FEBS J275, 271-280. PubMed  Europe PubMed DOI
2004
10. Monnet,V.
    X-Pro aminopeptidase (Lactococcus)
    [ISSN:0-12-079610-4]2, 930-931.  V
1999
11. Wegmann,U., Klein,J.R., Drumm,I., Kuipers,O.P. and Henrich,B.
    Introduction of peptidase genes from Lactobacillus delbrueckii subsp. lactis into Lactococcus lactis and controlled expression
    Appl Environ Microbiol65, 4729-4733. PubMed  Europe PubMed
1998
12. Matos,J., Nardi,M., Kumura,H. and Monnet,V.
    Genetic characterization of pepP, which encodes an aminopeptidase P whose deficiency does not affect Lactococcus lactis growth in milk, unlike deficiency of the X-prolyl dipeptidyl aminopeptidase
    Appl Environ Microbiol64, 4591-4595. PubMed  Europe PubMed
1997
13. Mc Donnell,M., FitzGerald,R., Fhaolain,I.N., Jennings,P.V. and O'Cuinn,G.
    Purification and characterization of aminopeptidase P from Lactococcus lactis subsp. cremoris
    J Dairy Res64, 399-407. PubMed  Europe PubMed
14. Rantanen,T. and Palva,A.
    Lactobacilli carry cryptic genes encoding peptidase-related proteins: characterization of a prolidase gene (pepQ) and a related cryptic gene (orfZ) from Lactobacillus delbrueckii subsp. bulgaricus
    Microbiology (Reading, Engl )143, 3899-3905. PubMed  Europe PubMed
1995
15. Stucky,K., Klein,J.R., Schuller,A., Matern,H., Henrich,B. and Plapp,R.
    Cloning and DNA sequence analysis of pepQ, a prolidase gene from Lactobacillus delbrueckii subsp. lactis DSM7290 and partial characterization of its product
    Mol Gen Genet247, 494-500. PubMed  Europe PubMed DOI
1984
16. Kaminogawa,S., Azuma,N., Hwang,I.-K., Suzuki,Y. and Yamauchi,K.
    Isolation and characterization of a prolidase from Streptococcus cremoris H61
    Agric Biol Chem48, 3035-3040. DOI