scholarly journals Reduced activity of the hypertension-associated Lys528Arg mutant of human adipocyte-derived leucine aminopeptidase (A-LAP)/ER-aminopeptidase-1

FEBS Letters ◽  
2006 ◽  
Vol 580 (7) ◽  
pp. 1833-1838 ◽  
Author(s):  
Yoshikuni Goto ◽  
Akira Hattori ◽  
Yasuhiro Ishii ◽  
Masafumi Tsujimoto
Keyword(s):  
Leucine Aminopeptidase ◽  
Human Adipocyte ◽  
Aminopeptidase A ◽  
Reduced Activity

Up-regulation of leucine aminopeptidase-A in cadmium-treated tomato roots

Planta ◽  
2011 ◽  
Vol 234 (4) ◽  
pp. 857-863 ◽  
Author(s):  
Latifa Boulila-Zoghlami ◽  
Philippe Gallusci ◽  
Frances M. Holzer ◽  
Gilles J. Basset ◽  
Whabi Djebali ◽  
...  
Keyword(s):  
Leucine Aminopeptidase ◽  
Tomato Roots ◽  
Aminopeptidase A

scholarly journals Distribution of Adipocyte-derived Leucine Aminopeptidase (A-LAP)/ER-aminopeptidase (ERAP)-1 in Human Uterine Endometrium

2004 ◽  
Vol 52 (9) ◽  
pp. 1169-1175 ◽  
Author(s):  
Daijiro Shibata ◽  
Hisao Ando ◽  
Akira Iwase ◽  
Tetsuro Nagasaka ◽  
Akira Hattori ◽  
...  
Keyword(s):  
Leucine Aminopeptidase ◽  
Uterine Endometrium ◽  
Aminopeptidase A ◽  
Human Uterine Endometrium

scholarly journals Microarray Analysis of Tomato’s Early and Late Wound Response Reveals New Regulatory Targets for Leucine Aminopeptidase A

PLoS ONE ◽  
2013 ◽  
Vol 8 (10) ◽  
pp. e77889 ◽  
Author(s):  
Melissa A. Scranton ◽  
Jonathan H. Fowler ◽  
Thomas Girke ◽  
Linda L. Walling
Keyword(s):  
Microarray Analysis ◽  
Leucine Aminopeptidase ◽  
Wound Response ◽  
Aminopeptidase A

Characterization of a leucine aminopeptidase of Babesia gibsoni

Parasitology ◽  
2009 ◽  
Vol 136 (9) ◽  
pp. 945-952 ◽  
Author(s):  
H. JIA ◽  
M. A. TERKAWI ◽  
G. O. ABOGE ◽  
Y.-K. GOO ◽  
Y. LUO ◽  
...  
Keyword(s):  
Amino Acid ◽  
Free Amino Acid ◽  
Free Amino ◽  
Drug Targets ◽  
Leucine Aminopeptidase ◽  
Divalent Cations ◽  
Specific Inhibitor ◽  
Babesia Gibsoni ◽  
Aminopeptidase A

SUMMARYPeptidases of parasitic protozoa are currently under intense investigation in order to identify novel virulence factors, drug targets, and vaccine candidates, except in Babesia. Leucine aminopeptidases in protozoa, such as Plasmodium and Leishmania, have been identified to be involved in free amino acid regulation. We report here the molecular and enzymatic characterization, as well as the localization of a leucine aminopeptidase, a member of the M17 cytosolic aminopeptidase family, from B. gibsoni (BgLAP). A functional recombinant BgLAP (rBgLAP) expressed in Escherichia coli efficiently hydrolysed synthetic substrates for aminopeptidase, a leucine substrate. Enzyme activity of the rBgLAP was found to be optimum at pH 8·0 and at 37°C. The substrate profile was slightly different from its homologue in P. falciprum. The activity was also strongly dependent on metal divalent cations, and was inhibited by bestatin, which is a specific inhibitor for metalloprotease. These results indicated that BgLAP played an important role in free amino acid regulation.

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