TY - JOUR
T1 - Characterization of a leucine aminopeptidase from Toxoplasma gondii
AU - Jia, Honglin
AU - Nishikawa, Yoshifumi
AU - Luo, Yuzi
AU - Yamagishi, Junya
AU - Sugimoto, Chihiro
AU - Xuan, Xuenan
N1 - Funding Information:
This work was funded by a grant from the Ministry of Education, Culture, Sports, Science, and Technology of Japan . We thank Dr. K.A. Joiner (Yale University) for providing the plasmid vector pHXNTPHA.
PY - 2010/3
Y1 - 2010/3
N2 - The M17 family leucine aminopeptidase (LAP) hydrolyzes amino acids from the N-terminus of peptides. Many LAPs from parasitic protozoa, including Plasmodium, Trypanosoma, and Leishmania, have been intensely investigated because of their crucial roles in parasite biology. In this study, the functional recombinant Toxoplasma gondii LAP (rTgLAP) was expressed in Escherichia coli, and its enzymatic activity against synthetic substrates for aminopeptidase, as well as cellular localization, was determined. The activity was strongly dependent on metal divalent cations, and was inhibited by bestatin, which is an inhibitor for metalloprotease. Our results indicated that TgLAP is a functional aminopeptidase in the cytoplasm of T. gondii.
AB - The M17 family leucine aminopeptidase (LAP) hydrolyzes amino acids from the N-terminus of peptides. Many LAPs from parasitic protozoa, including Plasmodium, Trypanosoma, and Leishmania, have been intensely investigated because of their crucial roles in parasite biology. In this study, the functional recombinant Toxoplasma gondii LAP (rTgLAP) was expressed in Escherichia coli, and its enzymatic activity against synthetic substrates for aminopeptidase, as well as cellular localization, was determined. The activity was strongly dependent on metal divalent cations, and was inhibited by bestatin, which is an inhibitor for metalloprotease. Our results indicated that TgLAP is a functional aminopeptidase in the cytoplasm of T. gondii.
KW - Enzymatic activity
KW - Leucine aminopeptidase
KW - Toxoplasma gondii
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U2 - 10.1016/j.molbiopara.2009.11.005
DO - 10.1016/j.molbiopara.2009.11.005
M3 - Article
C2 - 19931316
AN - SCOPUS:74249106457
SN - 0166-6851
VL - 170
SP - 1
EP - 6
JO - Molecular and Biochemical Parasitology
JF - Molecular and Biochemical Parasitology
IS - 1
ER -