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Expression and biochemical characterization of a type I methionine aminopeptidase of Plasmodium vivax.

Abstract：

:Methionine aminopeptidases (MetAPs), ubiquitous enzymes that play an important role in nascent protein maturation, have been recognized as attractive targets for the development of drugs against pathogenic protozoa including Plasmodium spp. Here, we characterized partial biochemical properties of a type I MetAP of Plasmodium vivax (PvMetAP1). PvMetAP1 had the typical amino acid residues essential for metal binding and substrate binding sites, which are well conserved in the type I MetAP family enzymes. Recombinant PvMetAP1 showed activity in a broad range of neutral pHs, with optimum activity at pH 7.5. PvMetAP1 was stable under neutral and alkaline pHs, but was relatively unstable under acidic conditions. PvMetAP1 activity was highly increased in the presence of Mn(2+), and was effectively inhibited by a metal chelator, EDTA. Fumagillin and aminopeptidase inhibitors, amastatin and bestatin, also showed an inhibitory effect on PvMetAP1. The enzyme had a highly specific hydrolytic activity for N-terminal methionine. These results collectively suggest that PvMetAP1 belongs to the family of type I MetAPs and may play a pivotal role for the maintenance of P. vivax physiology by mediating protein maturation and processing of the parasite.

journal_name

Protein Expr Purif

journal_title

Protein expression and purification

authors

Kang JM,Ju JW,Kim JY,Ju HL,Lee J,Lee KH,Lee WJ,Sohn WM,Kim TS,Na BK

doi

10.1016/j.pep.2015.01.003

subject

Has Abstract

pub_date

2015-04-01 00:00:00

pages

48-53

eissn

1046-5928

issn

1096-0279

pii

S1046-5928(15)00004-2

journal_volume

108

pub_type

杂志文章

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