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Molecular and catalytic properties of an arginine kinase from the nematode Ascaris suum

Published online by Cambridge University Press:  25 July 2011

M. Nagataki ,
K. Uda ,
B.R. Jarilla ,
S. Tokuhiro ,
S. Wickramasinghe ,
T. Suzuki ,
D. Blair  and
T. Agatsuma
M. Nagataki
Affiliation:
Department of Environmental Health Sciences, Kochi Medical School, Oko, Nankoku City, Kochi783-8505, Japan
K. Uda
Affiliation:
Laboratory of Biochemistry, Faculty of Science, Kochi University, Kochi, 780-8520, Japan
B.R. Jarilla
Affiliation:
Department of Environmental Health Sciences, Kochi Medical School, Oko, Nankoku City, Kochi783-8505, Japan
S. Tokuhiro
Affiliation:
Department of Environmental Health Sciences, Kochi Medical School, Oko, Nankoku City, Kochi783-8505, Japan
S. Wickramasinghe
Affiliation:
Department of Environmental Health Sciences, Kochi Medical School, Oko, Nankoku City, Kochi783-8505, Japan
T. Suzuki
Affiliation:
Laboratory of Biochemistry, Faculty of Science, Kochi University, Kochi, 780-8520, Japan
D. Blair
Affiliation:
School of Marine and Tropical Biology, James Cook University, Townsville, Queensland4811, Australia
T. Agatsuma*
Affiliation:
Department of Environmental Health Sciences, Kochi Medical School, Oko, Nankoku City, Kochi783-8505, Japan
*
*Fax: +81 88 880 2535 E-mail: [email protected]
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Abstract

We amplified the cDNA coding for arginine kinase (AK) from the parasitic nematode Ascaris suum, cloned it in pMAL plasmid and expressed the enzyme as a fusion protein with the maltose-binding protein. The whole cDNA was 1260 bp, encoding 400 amino acids, and the recombinant protein had a molecular mass of 45,341 Da. Ascaris suum recombinant AK showed significant activity and strong affinity for the substrate l-arginine. It also exhibited high catalytic efficiency comparable with AKs from other organisms. Sequence analysis revealed high amino acid sequence identity between A. suum AK and other nematode AKs, all of which cluster in a phylogenetic tree. However, comparison of gene structures showed that A. suum AK gene intron/exon organization is quite distinct from that of other nematode AKs. Phosphagen kinases (PKs) from certain parasites have been shown to be potential novel drug targets or tools for detection of infection. The characterization of A. suum AK will be useful in the development of strategies for control not only of A. suum but also of related species infecting humans.

Type
Research Papers
Information
Journal of Helminthology , Volume 86 , Issue 3 , September 2012 , pp. 276 - 286
Copyright
Copyright © Cambridge University Press 2011

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