Ornithine Decarboxylase of Leishmania Donovani: Biochemical Properties and Possible Role of N-Terminal Extension

ISSN: 1875-5305 (Online)
ISSN: 0929-8665 (Print)


Volume 21, 12 Issues, 2014


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Protein & Peptide Letters

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Ornithine Decarboxylase of Leishmania Donovani: Biochemical Properties and Possible Role of N-Terminal Extension

Author(s): Mousumi Das, Ritesh Kumar and Vikash Kumar Dubey

Affiliation: Department of Biotechnology, Indian Institute of Technology Guwahati, Assam, India- 781039

Abstract

Leishmaniasis is a widespread tropical disease caused by protozoan parasite Leishmania which belongs to order kinetoplastida and family trypanosomatidae. Ornithine decarboxylase is key enzyme in polyamine biosynthesis in Leishmania donovani. Here, we report biochemical characterization of ornithine decarboxylase from L. donovani. Furthermore, we have also investigated the role of N-terminal extension (250 amino acids) found in ornithine decarboxylase of L. donovani (LdODC). The removal of N-terminal extended region of LdODC results in improved stability of the protein. However, the truncated LdODC does not show any activity. Apparently, while N-terminal extended region of LdODC helps in proper folding of the protein for catalytic activity, there is a stability trade-off. The native full length LdODC with N-terminal extension has activity but lower stability. Comparison of biochemical properties of both, full-length and truncated enzymes, have provided interesting insights about the role of N-terminal extension in the protein

Keywords: Ornithine decarboxylase, Leishmaniasis, inhibitors

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Article Details

Volume: 21
First Page: 1
Last Page: 7
Page Count: 7
DOI: 10.2174/0929866521666140616115357
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